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Enzyme Nomenclature
Information on EC 2.4.1.19 - cyclomaltodextrin glucanotransferase
Word Map on EC 2.4.1.19
- 2.4.1.19
- cyclodextrins
- cgtases
- starch
- synthesis
-
cyclization
- circulans
-
alkalophilic
-
transglycosylation
- glucoamylase
- paenibacillus
- beta-cyclodextrins
- gamma-cyclodextrins
- nutrition
- maltodextrins
- pharmacology
- industry
- amylose
- acarbose
-
disproportionation
-
alpha-cd
- alpha-amylases
- beta-cds
- maltooligosaccharides
- cyclomaltohexaose
-
gamma-cds
-
amylolytic
- food industry
- amylopectin
- maltotetraose
- maltopentaose
- agriculture
- maltohexaose
-
starch-degrading
-
starch-binding
-
site-saturation
- pullulanase
-
alpha-1,4-glucans
- beta-amylase
-
thermoanaerobacterium
- maltotriose
- thermosulfurigenes
- clarkii
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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EC NUMBER 
COMMENTARY 
2.4.1.19
-
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RECOMMENDED NAME
GeneOntology No.
cyclomaltodextrin glucanotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond
Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond
cyclomaltodextrins (Schardinger dextrins) of various sizes (6,7,8, etc. glucose units) are formed reversibly from starch and similar substrates. Will also disproportionate linear maltodextrins without cyclizing (cf. EC 2.4.1.25, 4-alpha-glucanotransferase)
-
-
-
Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond
reaction in four steps via cyclization, disproportionation, hydrolysis, and coupling. The second step of the reaction involves the transfer of the covalently bound saccharide to an acceptor molecule
-
Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond
reaction in four steps via cyclization, disproportionation, hydrolysis, and coupling. The second step of the reaction involves the transfer of the covalently bound saccharide to an acceptor molecule
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyclization
-
-
-
-
hexosyl group transfer
hydrolysis
-
-
-
-
transglycosylation
-
-
-
-
hexosyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-glucan:(1->4)-alpha-D-glucan 4-alpha-D-[(1->4)-alpha-D-glucano]-transferase (cyclizing)
Cyclomaltodextrins (Schardinger dextrins) of various sizes (6,7,8, etc. glucose units) are formed reversibly from starch and similar substrates. Will also disproportionate linear maltodextrins without cyclizing (cf. EC 2.4.1.25, 4-alpha-glucanotransferase).
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CAS REGISTRY NUMBER
COMMENTARY
9030-09-5
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Bacillus sp. A2-5a
ATCC 9995; B. sp. var. alkalophilus No. 38-2, ATCC 21783; E 192; no. 8
-
-
B. sp. var. alkalophilus No. 38-2, ATCC 21783
-
-
-
488826, 488831, 488835, 488836, 488839, 488842, 488845, 488852, 488864, 684523, 701867, 703802, 706912
-
-
27 strains, e.g. strains 20RF, 8SB and 24WE, isolated from 17 Bulgarian alkaline and normal habitats, springs and soils
-
-
alkalophilic strain 1011; alkalophilic strain 1-1; alkalophilic strain 17-1; alkalophilic strain 20RF; alkalophilic strain 38-2; alkalophilic strain 8SB; alkalophilic strain A2-5a; alkalophilic strain G-825-6; alkalophilic strain I-5; strain B1018; strain BL-31; strain G1; strain KC201; strains B1018, BL-31, G1, KC201, and TS1-1, and the alkalophilic strains 1-1, 17-1, 38-2, 1011, 8SB, 20RF, A2-5a, G-825-6, and I-5; strain TS1-1
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-
-
488826, 488831, 488833, 488838, 488841, 488842, 488849, 488851, 488852, 488854, 488858, 488859, 488863, 668001, 702736
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-
i.e. Geobacillus stearothermophilus, strain NO2; strain ET1
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-
NO2, gene cgt-1, nucleotide sequence accession number; NO2 gene cgt-232, nucleotide sequence accession number; NO2 gene cgt-5, nucleotide sequence accession number
SwissProt
formerly Klebsiella pneumoniae M5a1
-
-
-
-
-
-
488826, 488827, 488828, 488829, 488830, 488831, 488833, 488835, 488836, 488840, 488842, 488848, 488849, 488851, 488852, 488854, 488857, 488858, 488862, 488864, 658396, 659739, 660533, 673388, 673578, 702790, 719222, 735493, 735512, 736290, 736538, 736787
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-
IFO3490, gene cgtM, nucleotide sequence accession number
SwissProt
thermotolerant strain T16 isolated from hot spring soil in northern Thailand
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-
-
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B1001, DNA sequence of CGTase gene, EMBL/GenBank/DDBJ database accession No.
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
it is an important hydrolytic enzyme that carries out reversible intermolecular as well as intramolecular transglycosylation and performs cyclization, coupling and disproportionation of maltooligosaccharides
physiological function
-
the enzyme is responsible for cyclodextrin formation. Cyclodextrins are cyclic, nonreducing oligo-glucopyranose molecules linked via alpha(1,4)-glycosidic bonds mainly consisting of six, seven, or eight glucose residue, alpha-, beta-, or gamma-cyclodextrin, respectively
physiological function
-
the enzyme is responsible for cyclodextrin formation. Cyclodextrins are cyclic, nonreducing oligo-glucopyranose molecules linked via alpha(1,4)-glycosidic bonds mainly consisting of six, seven, or eight glucose residue, alpha-, beta-, or gamma-cyclodextrin, respectively
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + D-glucose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + maltose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltotriose
4,6-benzylidene-alpha-D-4-nitrophenylmaltoheptaose + D-glucose
4,6-benzylidene-maltopentaose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose
-
blocked p-nitrophenyl-(alpha-1,4-glucopyranosyl)6-D-glucose , weak cleavage
-
-
?
alpha-1,4-glucan + glycosyl acceptor
cyclohexaamylose + cycloheptaamylose + cyclooctaamylose
alpha-cyclodextrin + ascorbic acid
L-ascorbic acid-2-O-alpha-D-glucoside + L-ascorbic acid-2-O-alpha-D-oligoglucoside
-
-
-
-
r
alpha-cyclodextrin + D-glucose
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
alpha-cyclodextrin + D-lactose
O-beta-D-galactopyranosyl-1,4-O-beta-D-glucopyranosyl alpha-D-glucopyranoside + glucose
alpha-cyclodextrin + isoascorbic acid
L-isoascorbic acid-2-O-alpha-D-glucoside + L-isoascorbic acid-2-O-alpha-D-oligoglucoside
-
-
-
-
r
alpha-cyclodextrin + maltohexaose
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
alpha-cyclodextrin + maltose
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
alpha-cyclodextrin + maltotetraose
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
alpha-cyclodextrin + maltotriose
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
alpha-cyclodextrin + sucrose
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
amylopectin + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
alpha-cyclodextrin is preferentially produced. With a longer incubation period, the alpha-cyclodextrin to beta-cyclodextrin ratio declines
larger cyclodextrins (>8 glucose units) are formed in the initial reaction period
-
?
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
amylose + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
alpha-cyclodextrin is preferentially produced. With a longer incubation period, the alpha-cyclodextrin to beta-cyclodextrin ratio declines
larger cyclodextrins (>8 glucose units) are formed in the initial reaction period
-
?
amylose + glycosyl acceptor
cyclodextrin
-
-
higher yield of large-ring cyclodextrins are ontained with a reaction temperature of 60°C compared to 40°C
-
?
beta-cyclodextrin + D-glucose
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + maltohexaose
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + maltotetraose
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + sucrose
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
corn starch + glycosyl acceptor
cyclodextrins
-
-
beta-cyclodextrin is the major product
-
?
cyclomaltohexaose + cyclo-[alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-6)-alpha-D-Glcp-(1-3)-alpha-D-Glp-(1-6)]
cyclo-[alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-6)-alpha-D-Glcp-(1-3)-[alpha-D-Glcp-(1-4)]-alpha-D-Glp-(1-6)]
-
-
-
-
?
cyclomaltohexaose + cyclo-[alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-6)-alpha-D-Glcp-(1-3)-alpha-D-Glp-(1-6)]
cyclo-[alpha-D-Glcp-(1-3)-[alpha-D-Glcp-(1-4)]-alpha-D-Glcp-(1-6)-alpha-D-Glcp-(1-3)-[alpha-D-Glcp-(1-4)]-alpha-D-Glp-(1-6)]
-
-
-
-
?
cyclomaltohexaose + D-lactose
O-beta-D-galactopyranosyl-1,4-O-beta-D-glucopyranosyl alpha-D-glucopyranoside + maltooligosyl sugars
cyclomaltohexaose + methyl alpha-D-glucopyranoside
maltodextrin glycoside
-
the reactions are optimized by using different ratios of the D-glucopyranosides to cyclomaltohexaose. The lower ratios of 0.5-1.0 give a wide range of sizes from d.p. 2-17 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 9–17, decrease, and the small and intermediate sizes, d.p. 2–8, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 4–8, decrease, and the small sizes, d.p. 2 and 3 become predominant
-
-
?
cyclomaltohexaose + methyl beta-D-glucopyranoside
maltodextrin glycoside
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the reactions are optimized by using different ratios of the D-glucopyranosides to cyclomaltohexaose. The lower ratios of 0.5-1.0 give a wide range of sizes from d.p. 2-17 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 9–17, decrease, and the small and intermediate sizes, d.p. 2–8, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 4–8, decrease, and the small sizes, d.p. 2 and 3 become predominant
-
-
?
cyclomaltohexaose + phenyl alpha-D-glucopyranoside
maltodextrin glycoside
-
the reactions are optimized by using different ratios of the D-glucopyranosides to cyclomaltohexaose. The lower ratios of 0.5–1.0 give a wide range of sizes from d.p. 2–17 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 9–17, decrease, and the small and intermediate sizes, d.p. 2–8, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 4–8, decrease, and the small sizes, d.p. 2 and 3 become predominant
-
-
?
cyclomaltohexaose + phenyl beta-D-glucopyranoside
maltodextrin glycoside
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the reactions are optimized by using different ratios of the D-glucopyranosides to cyclomaltohexaose. The lower ratios of 0.5–1.0 give a wide range of sizes from d.p. 2–17 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 9–17, decrease, and the small and intermediate sizes, d.p. 2–8, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 4–8, decrease, and the small sizes, d.p. 2 and 3 become predominant
-
-
?
dextrin
beta-cyclodextrin + alpha-cyclodextrin
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the maximum conversion of dextrin to beta-cyclodextrin and alpha-cyclodextrin is 29% both for the soluble and immobilized enzymes
-
-
?
gamma-cyclodextrin + glycosyl acceptor
maltooligosaccharide
-
-
-
-
r
L-ascorbic acid + beta-cyclodextrin
L-ascorbic acid-2-O-alpha-D-glucoside + ?
-
-
-
?
L-ascorbic acid + maltodextrin
L-ascorbic acid-2-O-alpha-D-glucoside + ?
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-
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?
L-ascorbic acid-(2-O-alpha-D-glucosyl)2 + glycosyl acceptor
Lascorbic acid alpha-D-glucoside + D-glucosyl-[glycosyl acceptor]
-
-
-
r
L-ascorbic acid-(2-O-alpha-D-glucosyl)2 + H2O
L-ascorbic acid-2-O-alpha-D-glucoside + D-glucose
-
-
-
r
L-ascorbic acid-(2-O-alpha-D-glucosyl)3 + glycosyl acceptor
L-ascorbic acid-(2-O-alpha-D-glucosyl)2 + D-glucosyl-[glycosyl acceptor]
-
-
-
r
L-ascorbic acid-(2-O-alpha-D-glucosyl)3 + H2O
L-ascorbic acid-(2-O-alpha-D-glucosyl)2 + D-glucose
-
-
-
r
L-ascorbic acid-(2-O-alpha-D-glucosyl)4 + glycosyl acceptor
L-ascorbic acid-(2-O-alpha-D-glucosyl)3 + glucosyl-[glycosyl acceptor]
-
-
-
r
L-ascorbic acid-(2-O-alpha-D-glucosyl)4 + H2O
L-ascorbic acid-(2-O-alpha-D-glucosyl)3 + D-glucose
-
-
-
r
L-ascorbic acid-2-O-alpha-D-glucoside + H2O
L-ascorbic acid + D-glucose
-
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
maltohexaose + L-ascorbic acid
L-ascorbic acid-(2-O-alpha-D-glucosyl)6
-
-
-
r
maltopentaose + glycosyl acceptor
beta-cyclodextrin
-
ATCC 21783
-
r
maltose + ascorbic acid
L-ascorbic acid-2-O-alpha-D-glucoside + D-glucose
-
-
-
r
native starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
alpha-cyclodextrin is preferentially produced. With a longer incubation period, the alpha-cyclodextrin to beta-cyclodextrin ratio declines
larger cyclodextrins (>8 glucose units) are formed in the initial reaction period
-
?
p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose + glycosyl acceptor
p-nitrophenyl-D-glucose + p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose + ?
-
E 192
main product p-nitrophenyl-glucose when chain length of substrate is 4 glucose or less, p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose when substrate chain length is 5 or more glucose residues
?
p-nitrophenyl-(alpha-1,4-glucopyranosyl)3-D-glucose + glycosyl acceptor
p-nitrophenyl alpha-D-glucoside + p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose + ?
-
E 192
product proportions 48:31:21
?
p-nitrophenyl-(alpha-1,4-glucopyranosyl)6-D-glucose + glycosyl acceptor
p-nitrophenyl-glucose + p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose + p-nitrophenyl-(glucose)3 + p-nitrophenyl-(alpha-1,4-glucopyranosyl)3-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)4-D-glucose + ?
-
E 192
product proportions 33:27:16:6:17
?
p-nitrophenyl-(alpha-1,4-glucopyranosyl)7-D-glucose + glycosyl acceptor
p-nitrophenyl-glucose + p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)3-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)4-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)5-D-glucose + ?
-
E 192
product proportions 16:51:12:13:4:4
?
p-nitrophenyl-(glucose)5 + glycosyl acceptor
p-nitrophenyl alpha-D-glucoside + p-nitrophenyl 4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside + p-nitrophenyl-(alpha-1,4-D-glucopyranosyl)2-D-glucose + p-nitrophenyl-(alpha-1,4-D-glucopyranosyl)3-D-glucose
-
E 192
product proportions 32:50:12 6
?
p-nitrophenyl-(glucose)6 + glycosyl acceptor
p-nitrophenyl alpha-D-glucoside + p-nitrophenyl 4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside + p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)3-D-glucose + ?
-
E 192
product proportions 18:53:21:8
?
potato starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
soluble starch
alpha-cyclodextrin
-
poly-lysine fused immobilization increases the Vmax of the immobilized CGTase by 40% without a change in Km. Maximum alpha-cyclodextrin productivity of 539.4 g/l*h is obtained with 2% soluble starch solution which is constantly fed at a flow rate of 4.0 ml/min in a continuous operation mode of a packed-bed reactor
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
starch + ascorbic acid
2-O-alpha-glucopyranosyl L-ascorbic acid
-
-
-
-
r
starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
alpha-cyclodextrin, beta-cyclodextrin and gamma-cyclodextrin in the ratio of 0.26:1.0:0.86
-
?
starch + glycosyl acceptor
cyclodextrin
-
the cyclodextrin product specificity can be changed into linear product specificity, by introducing a five-residue insertion mutation at the donor substrate binding subsites. The CGTase mutants remain clearly different from the maltogenic alpha-amylase, as they have much lower hydrolytic activities, they form linear products of variable sizes and they retain a low cyclodextrin forming activity, whereas maltogenic alpha-amylases produce primarily maltose. The five-residue insertion, concomitantly, strongly enhances the exo-specificity of CGTase
-
-
?
stevioside + beta-cyclodextrin
4'-O-alpha-D-glycosyl stevioside + 4''-O-alpha-D-maltosyl stevioside + ?
wheat starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + D-glucose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltose
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + D-glucose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltose
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + D-glucose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltose
Bacillus sp. 17. Jan
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + D-glucose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltose
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + maltose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltotriose
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + maltose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltotriose
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + maltose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltotriose
Bacillus sp. 17. Jan
-
strain 1011, disproportionation
-
-
?
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside + maltose
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltotetraoside + maltotriose
-
strain 1011, disproportionation
-
-
?
4,6-O-ethylidene-4-nitrophenyl-alpha-D-maltoheptaoside + maltose
?
-
maltose as donor and acceptor, overview
-
-
?
4,6-O-ethylidene-4-nitrophenyl-alpha-D-maltoheptaoside + maltose
?
-
maltose as donor and acceptor, overview
-
-
?
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
-
-
-
-
r
alpha-1,4-glucan + glycosyl acceptor
cyclohexaamylose + cycloheptaamylose + cyclooctaamylose
-
-
product ratio 1: 2.4: 1
r
alpha-1,4-glucan + glycosyl acceptor
cyclohexaamylose + cycloheptaamylose + cyclooctaamylose
-
-
product ratio 1: 2.4: 1
r
alpha-cyclodextrin + D-lactose
O-beta-D-galactopyranosyl-1,4-O-beta-D-glucopyranosyl alpha-D-glucopyranoside + glucose
-
-
oligosaccharide A
r
alpha-cyclodextrin + D-lactose
O-beta-D-galactopyranosyl-1,4-O-beta-D-glucopyranosyl alpha-D-glucopyranoside + glucose
-
-
oligosaccharide A
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
-
r
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
-
-
-
-
r
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
-
ATCC 21783
-
-
r
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
-
C31
-
-
-
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
-
C31
-
-
-
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
-
-
-
r
amylose
alpha-cyclodextrin
-
catalyzes the conversion of amylose to cyclodextrins, circular alpha-(1,4)-linked glucopyranose oligosaccharides of different ring sizes, the cyclodextrin containing 12 alpha-D-glucopyranose residues is preferentially synthesized by the enzyme. Interactions at oligosaccharide-binding subsites located close to the catalytic site apparently play a more important role in the determination of the size of the cyclodextrin formed
product identification by amperometric detection, overview
-
?
amylose
alpha-cyclodextrin
-
catalyzes the conversion of amylose to cyclodextrins, circular alpha-(1,4)-linked glucopyranose oligosaccharides of different ring sizes, the cyclodextrin containing 12 alpha-D-glucopyranose residues is preferentially synthesized by the enzyme. Interactions at oligosaccharide-binding subsites located close to the catalytic site apparently play a more important role in the determination of the size of the cyclodextrin formed
product identification by amperometric detection, overview
-
?
amylose + glycosyl acceptor
?
-
NO2, spiral amylose
-
-
r
beta-cyclodextrin + 4-nitrophenyl-beta-D-glucopyranose
?
-
beta-cyclodextrin as a glycosyl donor and 4-nitrophenyl-beta-D-glucopyranose as a glycosyl acceptor
-
-
?
beta-cyclodextrin + 4-nitrophenyl-beta-D-glucopyranose
?
-
beta-cyclodextrin as a glycosyl donor and 4-nitrophenyl-beta-D-glucopyranose as a glycosyl acceptor
-
-
?
beta-cyclodextrin + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
r
beta-cyclodextrin + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
r
beta-cyclodextrin + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
-
ATCC 21783
-
-
r
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + maltotriose
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + maltotriose
alpha-cyclodextrin + maltooligosaccharide
-
ATCC 21783
-
-
r
beta-cyclodextrin + maltotriose
alpha-cyclodextrin + maltooligosaccharide
-
immobilized enzyme
-
r
beta-cyclodextrin + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
beta-cyclodextrin + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
beta-cyclodextrin + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cycloamylose + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cycloamylose + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cycloamylose + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cycloamylose + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cycloamylose + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cycloamylose + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cyclodextrins + acceptor
linear maltooligosaccharide
-
strain 1011, cyclodextrin ring opening
-
r
cyclodextrins + acceptor
linear maltooligosaccharide
-
strain 1011, cyclodextrin ring opening
-
r
cyclodextrins + acceptor
linear maltooligosaccharide
Bacillus sp. 17. Jan
-
strain 1011, cyclodextrin ring opening
-
r
cyclodextrins + acceptor
linear maltooligosaccharide
-
strain 1011, cyclodextrin ring opening
-
r
cyclomaltohexaose + D-lactose
O-beta-D-galactopyranosyl-1,4-O-beta-D-glucopyranosyl alpha-D-glucopyranoside + maltooligosyl sugars
-
-
oligosaccharide A
r
cyclomaltohexaose + D-lactose
O-beta-D-galactopyranosyl-1,4-O-beta-D-glucopyranosyl alpha-D-glucopyranoside + maltooligosyl sugars
-
-
oligosaccharide A
r
dodecyl-beta-D-maltoside + alpha-cyclodextrin
dodecyl-beta-D-maltooctaoside + ?
-
the equilibrium lays to 80% on the side of dodecyl-beta-D-maltooctaoside production when the enzyme from Bacillus macerans is used as biocatalyst
-
-
r
dodecyl-beta-D-maltoside + alpha-cyclodextrin
dodecyl-beta-D-maltooctaoside + ?
-
-
-
-
r
Glucidex 2B + glycosyl acceptor
beta-cyclodextrin
-
E 192
-
r
glycogen + acceptor
beta-cyclodextrin
-
-
-
-
-
glycogen + acceptor
beta-cyclodextrin
-
-
-
-
r
linear maltooligosaccharide + acceptor
?
-
strain 1011, disproportionation reaction
-
-
r
linear maltooligosaccharide + acceptor
?
-
strain 1011, disproportionation reaction
-
-
r
linear maltooligosaccharide + acceptor
?
Bacillus sp. 17. Jan
-
strain 1011, disproportionation reaction
-
-
r
linear maltooligosaccharide + acceptor
?
-
strain 1011, disproportionation reaction
-
-
r
maltodextrin
beta-cyclodextrin
-
intramolecular transglycosylation
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
displays unusually high amylolytic activity in relation to the cyclization activity. Disproportionation activity of the CGTase is optimal with maltose as the acceptor substrate. Cyclization reaction and beta-cyclodextrin formation are significantly promoted in the presence of CaCl2. The salt allows the cyclization reaction to be performed at higher temperature
the product of cyclization reaction is predominantly beta-cyclodextrin along with alpha-cyclodextrin as a minor product. The CDs profile is influenced by the reaction conditions. At pH 10, alpha-cyclodextrin is replaced by gamma-cyclodextrin formation
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
displays unusually high amylolytic activity in relation to the cyclization activity. Disproportionation activity of the CGTase is optimal with maltose as the acceptor substrate. Cyclization reaction and beta-cyclodextrin formation are significantly promoted in the presence of CaCl2. The salt allows the cyclization reaction to be performed at higher temperature
the product of cyclization reaction is predominantly beta-cyclodextrin along with alpha-cyclodextrin as a minor product. The CDs profile is influenced by the reaction conditions. At pH 10, alpha-cyclodextrin is replaced by gamma-cyclodextrin formation
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
maltodextrin + L-ascorbic acid
2-O-D-glucopyranosyl-L-ascorbic acid + ?
-
-
-
-
?
maltodextrin + L-ascorbic acid
2-O-D-glucopyranosyl-L-ascorbic acid + ?
-
-
-
-
?
maltooligosaccharides + glycosyl acceptor
cyclodextrins
-
ATCC 21783
-
-
r
maltooligosaccharides + glycosyl acceptor
cyclodextrins
-
-
-
-
r
maltooligosaccharides + glycosyl acceptor
cyclodextrins
-
-
-
-
r
maltose + glycosyl acceptor
beta-cyclodextrin
-
E 192, poor substrate
-
r
maltose + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
maltotetraose + glycosyl acceptor
beta-cyclodextrin
-
ATCC 21783
-
r
maltotriose + glycosyl acceptor
beta-cyclodextrin
-
ATCC 21783
-
-
-
maltotriose + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
naringin + maltodextrin
?
cyclization reaction with naringin as acceptor and maltodextrin as donor
-
-
?
naringin + maltodextrin
?
cyclization reaction with naringin as acceptor and maltodextrin as donor
-
-
?
Paselli starch
beta-cyclodextrin
-
-
78% conversion, 1.9fold higher activity with Paselli starch than with soluble starch
-
?
Paselli starch
beta-cyclodextrin
-
-
78% conversion, 1.9fold higher activity with Paselli starch than with soluble starch
-
?
potato starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
Carboxydocella sp.
-
worst substrate
-
-
?
potato starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
worst substrate
-
-
?
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
AL-6
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
AL-6
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
Bacillus sp. AL-6
-
AL-6
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
Bacillus sp. INMIA 1919
-
AL-6
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
Bacillus sp. INMIA A7/1
-
AL-6
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
Bacillus sp. INMIA T4
-
AL-6
-
-
r
potato starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
Bacillus sp. INMIA t6
-
AL-6
-
-
r
raw corn starch
beta-cyclodextrin + gamma-cyclodextrin
-
-
ratio of beta- to gamma-cyclodextrin products is about 4:1
-
?
raw corn starch
beta-cyclodextrin + gamma-cyclodextrin
-
-
ratio of beta- to gamma-cyclodextrin products is about 4:1
-
?
raw starch
beta-cyclodextrin + gamma-cyclodextrin
-
-
sole products, beta- and gamma-cyclodextrin in a ratio of 80%:20%
-
?
raw starch
beta-cyclodextrin + gamma-cyclodextrin
-
-
sole products, beta- and gamma-cyclodextrin in a ratio of 80%:20%
-
?
rice starch + glycosyl acceptor
beta-cyclodextrin
-
highest activity
-
-
?
soluble potato starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
ratio for alpha- to beta- to gamma-cyclodextrin 1:1.3:0.5
-
?
soluble potato starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
ratio for alpha- to beta- to gamma-cyclodextrin 1:1.3:0.5
-
?
soluble potato starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
ratio of products is alpha-cyclodextrin to beta-cyclodextrin to gamma-cyclodextrin 1:0.6:0.3
-
?
soluble starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
at the initial stage of the reaction, alpha-cyclodextrin is the main product. Subsequently, the proportion of beta-cyclodextrin increases and becomes the main product after prolonged incubation. After 10 h or 40 h of incubation, the conversion rates of starch into cyclodextrins are 36.8% or 42.3%, respectively
-
?
soluble starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
at the initial stage of the reaction, alpha-cyclodextrin is the main product. Subsequently, the proportion of beta-cyclodextrin increases and becomes the main product after prolonged incubation. After 10 h or 40 h of incubation, the conversion rates of starch into cyclodextrins are 36.8% or 42.3%, respectively
-
?
soluble starch
beta-cyclodextrin
-
51.5% conversion
71% of total cyclodextrin formed
-
?
soluble starch
beta-cyclodextrin
-
51.5% conversion
71% of total cyclodextrin formed
-
?
soluble starch + D-galactose
?
-
less efficient acceptor
-
-
r
soluble starch + D-glucose
cyclodextrins
-
-
-
-
r
soluble starch + D-glucose
cyclodextrins
-
-
-
-
-
soluble starch + D-maltose
cyclodextrins
-
-
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + D-xylose
?
-
less efficient acceptor
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
strain ATCC 21783, pH 4.5-4.7, producing ratio 23.5: 1.0: 1.0, pH 7.0 0.2: 6.0: 1.0, product ratio 2.0:5.0:1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
21783, neutral CGTase, 0.4, 14 and 2.5%
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
strain 251, product proportions 9: 82: 9 with addition of tert-butanol, 15: 65: 20 without solvent
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
ATCC 21783
-
-
-
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
ATCC 21783
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
strain 251, product proportions 9: 82: 9 with addition of tert-butanol, 15: 65: 20 without solvent
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
potato starch, sweet potato starch, rice starch, corn starch, wheat starch
potato starch, 20 h at 50°C, ratio 8.1: 8.9: 1.0, various conditions, product proportions 1.0: 1.0: 0.3
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product proportions 0.2:9.2:0.6 from gelatinized tapioca starch, 0.2:8.6:1.2 from raw wheat starch
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product proportions 1: 67: 1.6
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product ratio 2.0:5.0:1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product proportions 1: 2.4: 1
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product proportions 1: 2.4: 1
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
producing ratio 0.0: 4.0: 1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
-
-
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
-
-
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
Bacillus sp. AL-6
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
Bacillus sp. BE101
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
Bacillus sp. INMIA 1919
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
Bacillus sp. INMIA A7/1
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
Bacillus sp. INMIA T4
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
Bacillus sp. INMIA t6
-
INMIA A/7
INMIA A/7, product proportions 1: 58.4: 7.4
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
producing ratio 0.0: 0.0: 1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
producing ratio 0.0: 0.0: 1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product proportions 4.2: 5.9: 1
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
producing ratio 5.5: 8.0: 1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product proportions 4.2: 5.9: 1
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
producing ratio 5.5: 8.0: 1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
ratio 12: 82: 6
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
ratio 12: 82: 6
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
-
-
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
IFO 3490, product proportions 2.7: 1: 1
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
potato starch, sweet potato starch, rice starch, corn starch, wheat starch
producing ratio 5.0: 2.0: 1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
-
-
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
IFO 3490, product proportions 2.7: 1: 1
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product ratios 43% alpha-cyclodextrin, 46% beta-cyclodextrin and 11% gamma-cyclodextrin
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
product ratios 43% alpha-cyclodextrin, 46% beta-cyclodextrin and 11% gamma-cyclodextrin
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
C31
product ratio 1: 10.5
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
C31
product ratio 1: 10.5
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
strain NO2
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
strain NO2
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
Carboxydocella sp.
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
Bacillus autolyticus
-
potato starch, small amounts of alpha- and gamma-cyclodextrin
-
-
-
soluble starch + glycosyl acceptor
beta-cyclodextrin
Bacillus autolyticus 11149
-
potato starch, small amounts of alpha- and gamma-cyclodextrin
-
-
-
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
E 192, waxy maize starch is the best substrate, wheat starch, corn starch, potato starch
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
E 192, waxy maize starch is the best substrate, wheat starch, corn starch, potato starch
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
E 192, waxy maize starch is the best substrate, wheat starch, corn starch, potato starch
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
INMIA T42, INMIA A7/1
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
Bacillus sp. Ha3-3-2/ATCC 39612
-
-
-
-
-
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
-
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
INMIA 3849
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
INMIA 3849
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
tapioca starch is the best substrate
production ratio of beta-cyclodextrin to gamma-cyclodextrin is 0.11/0.89 after 24 h at 60°C, without presence of any selective agents
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
Bacillus sp. AL-6
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
tapioca starch is the best substrate
production ratio of beta-cyclodextrin to gamma-cyclodextrin is 0.11/0.89 after 24 h at 60°C, without presence of any selective agents
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
Bacillus sp. INMIA 1919
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
Bacillus sp. INMIA A7/1
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
Bacillus sp. INMIA T4
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
Bacillus sp. INMIA t6
-
AL-6
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
beta-cyclodextrin is the main product
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
beta-cyclodextrin is the main product
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
tapioca starch, wheat starch
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
corn starch
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
corn starch
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
alpha-cyclodextrin is the main product
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
alpha-cyclodextrin is the main product
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cycloheptaamylose
-
No. 5 strain
-
r
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
strain no.313
-
-
r
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
strain no.313
-
-
r
soluble starch + glycosyl acceptor
gamma-cyclodextrin
-
-
-
-
-
soluble starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
-
alpha-cyclodextrin production is not observed at any pH examined. The enzyme produces gamma-cyclodextrin principally at any pH and the ratio of gamma-cyclodextrin to beta-cyclodextrin is always more than 1.7 and 4.7 with 1% and 10% substrate
-
?
soluble starch + glycosyl acceptor
gamma-cyclodextrin + beta-cyclodextrin
-
-
alpha-cyclodextrin production is not observed at any pH examined. The enzyme produces gamma-cyclodextrin principally at any pH and the ratio of gamma-cyclodextrin to beta-cyclodextrin is always more than 1.7 and 4.7 with 1% and 10% substrate
-
?
soluble starch + glycosyl acceptor
maltose + maltotriose + maltotetraose + maltopentaose
-
-
-
r
soluble starch + glycosyl acceptor
maltose + maltotriose + maltotetraose + maltopentaose
-
-
-
r
soluble starch + glycosyl acceptor
maltose + maltotriose + maltotetraose + maltopentaose
-
-
-
r
soluble starch + glycosyl acceptor
Schardinger beta-dextrin
-
ATCC 21783
-
-
-
soluble starch + glycosyl acceptor
Schardinger beta-dextrin
-
ATCC 21783
-
-
r
soluble starch + glycosyl acceptor
Schardinger dextrins
-
-
-
-
r
starch
beta-cyclodextrin + gamma-cyclodextrin
86% beta-cyclodextrin and 14% of gamma-cyclodextrin are produced after 24 h incubation at 60°C, without adding any selective agent, in 0.1 M phosphate buffer
-
-
?
starch
beta-cyclodextrin + gamma-cyclodextrin
86% beta-cyclodextrin and 14% of gamma-cyclodextrin are produced after 24 h incubation at 60°C, without adding any selective agent, in 0.1 M phosphate buffer
-
-
?
starch
beta-cyclodextrin + gamma-cyclodextrin
-
the maximum starch conversion to beta-cyclodextrin and gamma-cyclodextrin is 29% and 38%, for the immobilized and soluble enzyme, respectively
-
-
?
starch
cyclodextrin
-
enzymes from Escherichia coli, Bacillus macerans and Bacillus subtilis show similar production profile in cyclization reaction
-
-
?
starch
cyclodextrin
-
enzymes from Escherichia coli, Bacillus macerans and Bacillus subtilis show similar pruduction profile in cyclization reaction
-
-
?
starch
cyclodextrin
-
enzymes from Escherichia coli, Bacillus macerans and Bacillus subtilis show similar pruduction profile in cyclization reaction
-
-
?
starch
cyclodextrin
-
to manipulate the product specificity of the Paenibacillus sp. A11 and Bacillus macerans cyclodextrin glycosyltransferases towards the preferential formation of gamma-cyclodextrin (CD8), crosslinked imprinted protein of cyclodextrin glycosyltransferase is prepared by applying enzyme imprinting and immobilization methodologies. The native enzyme produces CD6:CD7:CD8:CD9 ratios of 43:36:21:0 at 40°C. The size of the synthesis products formed bythe crosslinked imprinted cyclodextrin glycosyltransferases is shifted towards CD8 and CD9, and the overall cyclodextrin yield is increased by 12% compared to the native enzymes
-
-
?
starch
cyclodextrin
-
enzymes from Escherichia coli, Bacillus macerans and Bacillus subtilis show similar pruduction profile in cyclization reaction
-
-
?
starch
cyclodextrin
-
to manipulate the product specificity of the Paenibacillus sp. A11 and Bacillus macerans cyclodextrin glycosyltransferases towards the preferential formation of gamma-cyclodextrin (CD8), crosslinked imprinted protein of cyclodextrin glycosyltransferase is prepared by applying enzyme imprinting and immobilization methodologies. The native enzyme produces CD6:CD7:CD8:CD9 ratios of 15:65:20:0 at 40°C. The size of the synthesis products formed by the crosslinked imprinted cyclodextrin glycosyltransferases is shifted towards CD8 and CD9, and the overall cyclodextrin yield is increased by 12% compared to the native enzymes
-
-
?
starch
cyclodextrin
-
to manipulate the product specificity of the Paenibacillus sp. A11 and Bacillus macerans cyclodextrin glycosyltransferases towards the preferential formation of gamma-cyclodextrin (CD8), crosslinked imprinted protein of cyclodextrin glycosyltransferase is prepared by applying enzyme imprinting and immobilization methodologies. The native enzyme produces CD6:CD7:CD8:CD9 ratios of 15:65:20:0 at 40°C. The size of the synthesis products formed by the crosslinked imprinted cyclodextrin glycosyltransferases is shifted towards CD8 and CD9, and the overall cyclodextrin yield is increased by 12% compared to the native enzymes
-
-
?
starch
cyclodextrin
-
in acetatebuffer, pH 6.0, 60°C, the CGTase produces pre dominantly beta-cyclodextrin from either raw or gelatinized sago (Cycas revoluta) starch. Changing the buffer from acetate to phosphate reduces the yield of beta-cyclodextrin from 2.48 to 1.42 mg/ml, production of both alpha- and beta-cyclodextrins are more pronounced. The decrease in the production of cyclodextrins in phosphate buffer is significant at both pH 6.0 and 7.0. Changing the buffer to Tris/HCl (pH 7.0) shows a significant increase in beta-cyclodextrin production
-
-
?
starch + glycosyl acceptor
cyclodextrins
-
-
the main product is alpha-cyclodextrin
-
?
starch + glycosyl acceptor
cyclodextrins
Bacillus sp. 602-1
-
-
the main product is alpha-cyclodextrin
-
?
starch + glycosyl acceptor
cyclodextrins
-
-
the main product is alpha-cyclodextrin
-
?
starch + glycosyl acceptor
cyclodextrins
-
-
the main product is alpha-cyclodextrin
-
?
starch + maltose
beta-cyclodextrin + gamma-cyclodextrin + maltooligosaccharides
-
-
-
-
-
starch + maltose
beta-cyclodextrin + gamma-cyclodextrin + maltooligosaccharides
-
-
-
-
?
starch + stevioside
glycosyl stevioside
-
extrusion starch, raw starch and liquefied starch as glucosyl donor
-
-
r
stevioside + beta-cyclodextrin
4'-O-alpha-D-glycosyl stevioside + 4''-O-alpha-D-maltosyl stevioside + ?
-
1,4-intermolecular transglycosylation, the substrate is an entkaurene diterpene glycoside, and is a constituent in Stevia rebaudiana leaves. It has therapeutic importance as substitute of sugar for diabetics. Enhancement of thre reaction under microwave assisted reaction, overview
formed to 66% and 24%, respectively, product identification by detailed NMR, LC-MS/MS studies
-
?
stevioside + beta-cyclodextrin
4'-O-alpha-D-glycosyl stevioside + 4''-O-alpha-D-maltosyl stevioside + ?
-
1,4-intermolecular transglycosylation, the substrate is an entkaurene diterpene glycoside, and is a constituent in Stevia rebaudiana leaves. It has therapeutic importance as substitute of sugar for diabetics. Enhancement of thre reaction under microwave assisted reaction, overview
formed to 66% and 24%, respectively, product identification by detailed NMR, LC-MS/MS studies
-
?
stevioside + maltodextrin
?
-
the enzyme from strain BL-12 is more suitable for transglycosylation than the cyclization reaction, and is specific for the intermolecular transglycosylation of stevioside with maltodextrin as the most suitable glycosyl donor
-
-
?
stevioside + maltodextrin
?
-
the enzyme from strain BL-12 is more suitable for transglycosylation than the cyclization reaction, and is specific for the intermolecular transglycosylation of stevioside with maltodextrin as the most suitable glycosyl donor
-
-
?
wheat starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
Carboxydocella sp.
-
best substrate, the enzyme is preferentially forming alpha- (50%) and beta-cyclodextrin (40%) in the cyclization reaction using wheat starch as substrate
-
-
?
wheat starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
best substrate, the enzyme is preferentially forming alpha- (50%) and beta-cyclodextrin (40%) in the cyclization reaction using wheat starch as substrate
-
-
?
additional information
?
-
-
increasing substrate concentrations (0.5%-20.0%) and glucans containing branching points (alpha-1,6-glycosidic linkages) shift the product pattern to: beta-cyclodextrin > alpha-cyclodextrin > gamma-cyclodextrin
-
-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Anaerobranca gottschalkii produces alpha-cyclodextrins
-
-
-
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch
-
-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus agaradhaerens produces beta-cyclodextrins
-
-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus agaradhaerens produces beta-cyclodextrins
-
-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
-
additional information
?
-
-
D-glucuronate is ineffective as acceptor
-
-
-
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
-
additional information
?
-
-
D-glucuronate is ineffective as acceptor
-
-
-
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
-
additional information
?
-
-
D-glucuronate is ineffective as acceptor
-
-
-
additional information
?
-
Bacillus autolyticus
-
sorbitol, mannitol, xylulose, galactose, fructose, lactose, glycerol and arabinose are not acceptors
-
-
-
additional information
?
-
Bacillus autolyticus 11149
-
sorbitol, mannitol, xylulose, galactose, fructose, lactose, glycerol and arabinose are not acceptors
-
-
-
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
-
additional information
?
-
-
ATCC 21783 contains 3 types of enzymes, acid, neutral and alcaline
-
-
-
additional information
?
-
-
no reaction with p-nitrophenyl-glucose and p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose, heptakis(2,6-di-O-methyl)-beta cyclodextrin is not transformed
-
-
-
additional information
?
-
beta-cyclodextrin-forming activity from partially hydrolyzed potato starch with an average degree of polymerization of 50. Disproportionation activity is determined using 4-nitrophenyl-beta-D-maltoheptaoside-4-6-O-ethylidene, i.e. pNPG7, as substrate
-
-
-
additional information
?
-
conversion of starch into beta- and gamma-cyclodextrins in a ratio 73:27
-
-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzymes from Bacillus circulans strans produce beta-cyclodextrins, except for strain DF 9R that also produces alpha-cyclodextrins
-
-
-
additional information
?
-
CGTase catalyzes the formation of cyclomaltooligosaccharides, cyclic molecules formed by alpha-(1,4)-linked D-glucopyranosyl units with an apolar central cavity and a hydrophilic outer surface. alpha-, beta-Cyclizing and amylolytic activities withpotato starch as substrate, enzyme structure-function relationship, overview
-
-
-
additional information
?
-
-
formation of alpha-, beta-, and gamma-cyclodextrins from starch and matotriose
-
-
-
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme from strain BC251 also shows hydrolytic activity on potato starch. Substrate binding structure of the strain BC251 enzyme, overview
-
-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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beta-cyclodextrin-forming activity from partially hydrolyzed potato starch with an average degree of polymerization of 50. Disproportionation activity is determined using 4-nitrophenyl-beta-D-maltoheptaoside-4-6-O-ethylidene, i.e. pNPG7, as substrate
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additional information
?
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no reaction with p-nitrophenyl-glucose and p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose, heptakis(2,6-di-O-methyl)-beta cyclodextrin is not transformed
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additional information
?
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mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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additional information
?
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formation of alpha-, beta-, and gamma-cyclodextrins from starch and matotriose
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additional information
?
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CGTase catalyzes the formation of cyclomaltooligosaccharides, cyclic molecules formed by alpha-(1,4)-linked D-glucopyranosyl units with an apolar central cavity and a hydrophilic outer surface. alpha-, beta-Cyclizing and amylolytic activities withpotato starch as substrate, enzyme structure-function relationship, overview
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additional information
?
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no reaction with p-nitrophenyl-glucose and p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose, heptakis(2,6-di-O-methyl)-beta cyclodextrin is not transformed
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces 80% gamma-cyclodextrins with an overall conversion of starch into cyclodextrins of 14%
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces 80% gamma-cyclodextrins with an overall conversion of starch into cyclodextrins of 14%
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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additional information
?
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-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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additional information
?
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the enzyme shows cyclization activity on different raw and hydrolyzed starches, hydrolyzed cornstarch gives the highest activity. The enzyme from strain 7b mainly forms beta-cyclodextrin, but also alpha- and gamma-cyclodextrins, from maltodextrin, influence of substrate concentration on CGTase activity, overview
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produce beta-cyclodextrins, except for strain 290-3 that also produces gamma-cyclodextrins
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additional information
?
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the extracelluar enzyme converts starch into non-reducing, cyclic malto-oligosacchrarides called cyclodextrins
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additional information
?
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assay method optimization, the optimum ratio of stevioside to beta-cyclodextrin for optimum transglycosylation is 1:2, overview
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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assay method optimization, the optimum ratio of stevioside to beta-cyclodextrin for optimum transglycosylation is 1:2, overview
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additional information
?
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the enzyme shows cyclization activity on different raw and hydrolyzed starches, hydrolyzed cornstarch gives the highest activity. The enzyme from strain 7b mainly forms beta-cyclodextrin, but also alpha- and gamma-cyclodextrins, from maltodextrin, influence of substrate concentration on CGTase activity, overview
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additional information
?
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mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus lichenifoormis produces alpha- and beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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additional information
?
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-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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additional information
?
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the enzyme preforms cyclization of different alpha-1,4-glucans, e.g. soluble potato starch, or amylopectin, and amylose, the enzyme forms preferably beta-cyclodextrins, the ratio of products is 27:68:5 for alpha, beta, and gamma cyclodextrins
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus megaterium produces beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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the enzyme produces alpha-, beta-, and gamma-cyclodextrins from starch
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additional information
?
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the enzyme produces alpha-, beta-, and gamma-cyclodextrins from starch, product ratios depend on the duration of the process. The enzyme also shows coupling activity and is able to degrade high concentrations of beta-cyclodextrin and to transform different types of cyclodextrins one into another. Native corn starch and soluble potato starch as substrates, product determination by thin layer chromatography
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus obhensis produces beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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the immobilized enzyme, of both strains, as membrane biocatalysts forms mainly beta- and gamma-cyclodextrins after 6 h enzyme reaction at pH 9.0 of the reaction mixture, 35-37% of the reaction products formed are gamma-cyclodextrins
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additional information
?
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isolation of alkaliphilic Bacillus strains and determination of their phylogenetic and phenotypic characteristics, overview
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additional information
?
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glycosyl donor specificity for intermolecular transglycosylation of stevioside, overview, cyclization reaction with soluble starch as substrate
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additional information
?
-
the enzyme from strain BL-31 is highly specific for the intermolecular transglycosylation of bioflavonoids, with high specificities for glycosyl acceptor bioflavonoids, including naringin, rutin, and hesperidin, and especially naringin
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additional information
?
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the enzyme produces cyclodextrins from starch, enzymes from strains 20RF and 8SB Bacillus strains form only two types of cyclodextrins, beta and gamma
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additional information
?
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
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additional information
?
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reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview
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additional information
?
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substrate is soluble starch, formation of beta-cyclodextrins
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additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
substrates bind across the enzyme's surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
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additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
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additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
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-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
substrates bind across the enzyme's surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
glycosyl donor specificity for intermolecular transglycosylation of stevioside, overview, cyclization reaction with soluble starch as substrate
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-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
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-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
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-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
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-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
substrates bind across the enzyme's surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
the enzyme from strain BL-31 is highly specific for the intermolecular transglycosylation of bioflavonoids, with high specificities for glycosyl acceptor bioflavonoids, including naringin, rutin, and hesperidin, and especially naringin
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
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-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
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-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
-
-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
substrates bind across the enzyme's surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
substrate is soluble starch, formation of beta-cyclodextrins
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-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
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-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
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-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
-
-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
substrates bind across the enzyme's surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
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-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
-
-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
substrates bind across the enzyme's surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
when the coupling reaction is measured utilizing beta-cyclodextrin as substrate, CGTase from Escherichia coli displays a 14fold greater catalytic activity as compared to CGTase from Bacillus macerans or CGTase from Bacillis subtilis. The coupling activity of CGTase from Escherichia coli is not significantly different from that of CGTase from Bacillus macerans or CGTase from Bacillus subtilis when alpha-cyclodextrin is used as the substrate
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additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Brevibacillus brevis produces beta-cyclodextrins
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-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Brevibacillus brevis produces beta-cyclodextrins
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-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
when the coupling reaction is measured utilizing beta-cyclodextrin as substrate, CGTase from Escherichia coli displays a 14fold greater catalytic activity as compared to CGTase from Bacillus macerans or CGTase from Bacillis subtilis. The coupling activity of CGTase from Escherichia coli is not significantly different from that of CGTase from Bacillus macerans or CGTase from Bacillus subtilis when alpha-cyclodextrin is used as the substrate
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-
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additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
-
additional information
?
-
-
disaccharides are not substrates, except maltose
-
-
-
additional information
?
-
-
isomaltose, sucrose, melibiose, phenyl-alpha-D-glucoside, cellobiose and lactose are not acceptors, L-ascorbic acid-2-O-phosphate and, L-ascorbic acid-2-O-sulfate are not substrates
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additional information
?
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CGTase catalyzes the transfer of dextrin units from cyclodextrins or longer dextrins to polyols, such as glycerol, sugars, and flavonoids
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additional information
?
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CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces alpha- and beta-cyclodextrins
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Geobacillus stearothermophilus produces beta-cyclodextrins
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additional information
?
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CGTase transfers glycosyl residues from dextrin, maltosides with an alkyl side chain of C4, C8, C12, to the maltosides of butanol, octanol, and lauryl alcohol generating maltosides with 3-4 glucose units, substrate specificity, overview. Product identification with TLC, NMR, and ESI mass spectrometry
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additional information
?
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reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces alpha- and beta-cyclodextrins
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Geobacillus stearothermophilus produces beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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cyclization is the predominant activity, followed by hydrolysis and to a lesser extent coupling and disproportionation activities
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additional information
?
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cyclization is the predominant activity, followed by hydrolysis and to a lesser extent coupling and disproportionation activities
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additional information
?
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CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Klebsiella pneumoniae produces alpha-cyclodextrins
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additional information
?
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reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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additional information
?
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reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Klebsiella pneumoniae produces alpha-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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in addition to the intramolecular transglycosylation and cyclization producing beta-cyclodextrins, using maltodextrin and starch as substrates, the CGTase shows disproportionation and coupling activities, intermolecular transglycosylation reactions. The enzyme produces alpha-, beta-, and gamma-cyclodextrins in the ratio of 0.40:1:0.45. Activity with different starch types, overview
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additional information
?
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CGTase can hydrolyze glucan chains, e.g. starch, in a manner similar to alpha-amylases, but differs in its ability to form cyclodextrins as reaction products. Cyclodextrins are formed from starch molecules through intramolecular transglycosylation, i.e. cyclization, and can be made up of 6 to 8 glucan residues, alpha-, beta-, and gamma-cyclodextrin, respectively. The enzyme is multifunctional
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additional information
?
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cyclization with maltodextrin as substrate
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus campinasensis produces beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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CGTase can hydrolyze glucan chains, e.g. starch, in a manner similar to alpha-amylases, but differs in its ability to form cyclodextrins as reaction products. Cyclodextrins are formed from starch molecules through intramolecular transglycosylation, i.e. cyclization, and can be made up of 6 to 8 glucan residues, alpha-, beta-, and gamma-cyclodextrin, respectively. The enzyme is multifunctional
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additional information
?
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cyclization with maltodextrin as substrate
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus campinasensis produces beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus graminis produces alpha- and beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus graminis produces alpha- and beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus illinoisensis produces beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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the native enzyme does not convert king oyster mushroom powder and enoki mushroom powder, while recombinant enzyme converts king oyster mushroom powder and enoki mushroom powder to beta-cyclodextrin
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus illinoisensis produces beta-cyclodextrins
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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the native enzyme does not convert king oyster mushroom powder and enoki mushroom powder, while recombinant enzyme converts king oyster mushroom powder and enoki mushroom powder to beta-cyclodextrin
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additional information
?
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mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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additional information
?
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D-galactose, D-ribose, D-mannose, D-arabinose and D-fructose do not contribute as glucosyl acceptor
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additional information
?
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when the coupling reaction is measured utilizing beta-cyclodextrin as substrate, CGTase from Escherichia coli displays a 14fold greater catalytic activity as compared to CGTase from Bacillus macerans or CGTase from Bacillis subtilis. The coupling activity of CGTase from Escherichia coli is not significantly different from that of CGTase from Bacillus macerans or CGTase from Bacillus subtilis when alpha-cyclodextrin is used as the substrate
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additional information
?
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CGTase produces alpha-, beta-, and gamma-cyclodextrins from soluble starch, overview
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additional information
?
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CGTase is an extracellular enzyme capable of converting starch or starch derivatives into cyclodextrins through an intramolecular transglycosylation reaction. Cyclodextrins are cyclic, nonreducing oligoglucopyranose molecules linked via alpha(1,4)-glycosidic bonds
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus macerans produces alpha-cyclodextrins
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additional information
?
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Asp372 and Tyr89 at subsite -3 play important roles in cyclodextrin product specificity of CGTase. Comparison of alpha-, beta- and gamma-cyclization specificity of wild-type and mutant enzymes, overview
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additional information
?
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CGTases function according to an alpha-retaining double displacement mechanism with a covalent glycosyl-enzyme intermediate. Efficient synthesis of a long carbohydrate chain alkyl glycoside catalyzed by CGTase
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additional information
?
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
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synthesis of 3-O-alpha-D-glucopyranosyl dopamine and 4-O-alpha-D-glucopyranosyl dopamine, and of 3-O-alpha-D-glucopyranosyl L-DOPA and 4-O-alpha-D-glucopyranosyl L-DOPA by reaction with cyclomaltohexaose catalyze by the CGTase using dopamine-HCl or imidazolium-HCl and glucose or maltose as substrates, maltodextrin chains attached to dopamine, overview. Determination of the reaction products by MALDI-TOF MS and NMR, molecular structure of the dopamine-glycosides, overview
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additional information
?
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the enzyme performs formation of alpha-, beta- and gamma-cyclodextrin. Lys47 is important for the alpha-cyclization reaction. Enhancement of beta-cyclodextrin specificity might be due to weakening or removal of hydrogen-bonding interactions between the side chain of residue 47 and the bent intermediate specific for alpha-cyclodextrin formation
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additional information
?
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the enzyme shows alpha-cyclodextrin forming activity with soluble starch
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additional information
?
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mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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additional information
?
-
-
when the coupling reaction is measured utilizing beta-cyclodextrin as substrate, CGTase from Escherichia coli displays a 14fold greater catalytic activity as compared to CGTase from Bacillus macerans or CGTase from Bacillis subtilis. The coupling activity of CGTase from Escherichia coli is not significantly different from that of CGTase from Bacillus macerans or CGTase from Bacillus subtilis when alpha-cyclodextrin is used as the substrate
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additional information
?
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CGTase is an extracellular enzyme capable of converting starch or starch derivatives into cyclodextrins through an intramolecular transglycosylation reaction. Cyclodextrins are cyclic, nonreducing oligoglucopyranose molecules linked via alpha(1,4)-glycosidic bonds
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additional information
?
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the enzyme shows alpha-cyclodextrin forming activity with soluble starch
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additional information
?
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the enzyme performs formation of alpha-, beta- and gamma-cyclodextrin. Lys47 is important for the alpha-cyclization reaction. Enhancement of beta-cyclodextrin specificity might be due to weakening or removal of hydrogen-bonding interactions between the side chain of residue 47 and the bent intermediate specific for alpha-cyclodextrin formation
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additional information
?
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production of beta-cyclodextrin from potato starch
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additional information
?
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the main amino acid residues of cyclization activity are Lys47, Tyr89, Asn94, Phe183, Asn193, Leu194, Tyr195, Asp196, Phe259, Phe283, and Asp371
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additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus pabuli produces beta-cyclodextrins
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additional information
?
-
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substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus pabuli produces beta-cyclodextrins
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-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
-
production of beta-cyclodextrin from potato starch
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-
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additional information
?
-
the main amino acid residues of cyclization activity are Lys47, Tyr89, Asn94, Phe183, Asn193, Leu194, Tyr195, Asp196, Phe259, Phe283, and Asp371
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additional information
?
-
-
the main amino acid residues of cyclization activity are Lys47, Tyr89, Asn94, Phe183, Asn193, Leu194, Tyr195, Asp196, Phe259, Phe283, and Asp371
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additional information
?
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soluble potato starch, cellobiose, and cyclodextrins as substrates, cyclodextrin product spectrum of native and recombinant enzymes, overview
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additional information
?
-
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus sp. strains produce alpha- and beta-cyclodextrins
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-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
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additional information
?
-
-
reversible cyclization reaction with alpha-1,4-glucans, e.g. starch, the major final product of PFCGT cyclization is beta-cyclodextrin, and thus the enzyme is a beta-CGTase
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additional information
?
-
reversible cyclization reaction with alpha-1,4-glucans, e.g. starch, the major final product of PFCGT cyclization is beta-cyclodextrin, and thus the enzyme is a beta-CGTase
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additional information
?
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-
cyclization activity forming cyclodextrins from starch
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additional information
?
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-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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-
additional information
?
-
-
D-glucuronate is ineffective as acceptor
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-
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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-
-
additional information
?
-
-
D-glucuronate is ineffective as acceptor
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-
-
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
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-
-
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzymes from Thermoanaerobacter sp. strains produce alpha- and beta-cyclodextrins
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-
-
additional information
?
-
-
CGTases function according to an alpha-retaining double displacement mechanism with a covalent glycosyl-enzyme intermediate. Synthesis of a long carbohydrate chain alkyl glycoside catalyzed by CGTase
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-
-
additional information
?
-
-
cyclodextrin glycosyltransferase produces a mixture of alpha-, beta-, and gamma-cyclodextrins from starch
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-
-
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows high also shows hydrolytic activity on potato starch
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-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
the enzyme primarily catalyses the formation of cyclic alpha-1,4-linked cyclodextrins from starch. This enzyme also possesses unusually high hydrolytic activity as a side reaction, thought to be due to partial retention of ancestral enzyme function. Product formation, alpha-, beta-, and gamma-cyclodextrins, of wild-type and mutant enzymes, substrate-binding subsites of CGTase, and sugar binding structure, overview
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-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Thermoanaerobacterium thermosulfurigenes produces alpha- and beta-cyclodextrins
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-
-
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows high hydrolytic activity on potato starch
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-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
the enzyme primarily catalyses the formation of cyclic alpha-1,4-linked cyclodextrins from starch. This enzyme also possesses unusually high hydrolytic activity as a side reaction, thought to be due to partial retention of ancestral enzyme function. Product formation, alpha-, beta-, and gamma-cyclodextrins, of wild-type and mutant enzymes, substrate-binding subsites of CGTase, and sugar binding structure, overview
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-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows high hydrolytic activity on potato starch
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-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Thermoanaerobacterium thermosulfurigenes produces alpha- and beta-cyclodextrins
-
-
-
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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-
-
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch
-
-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
potato starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
soluble starch + glycosyl acceptor
Schardinger dextrins
-
-
-
-
r
wheat starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
potato starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
Carboxydocella sp.
-
worst substrate
-
-
?
potato starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
worst substrate
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
Carboxydocella sp.
-
-
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
-
-
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
beta-cyclodextrin is the main product
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
beta-cyclodextrin is the main product
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
alpha-cyclodextrin is the main product
-
?
soluble starch + glycosyl acceptor
cyclodextrins
-
-
alpha-cyclodextrin is the main product
-
?
starch + glycosyl acceptor
cyclodextrins
-
-
the main product is alpha-cyclodextrin
-
?
starch + glycosyl acceptor
cyclodextrins
Bacillus sp. 602-1
-
-
the main product is alpha-cyclodextrin
-
?
starch + glycosyl acceptor
cyclodextrins
-
-
the main product is alpha-cyclodextrin
-
?
starch + glycosyl acceptor
cyclodextrins
-
-
the main product is alpha-cyclodextrin
-
?
wheat starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
Carboxydocella sp.
-
best substrate, the enzyme is preferentially forming alpha- (50%) and beta-cyclodextrin (40%) in the cyclization reaction using wheat starch as substrate
-
-
?
wheat starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
best substrate, the enzyme is preferentially forming alpha- (50%) and beta-cyclodextrin (40%) in the cyclization reaction using wheat starch as substrate
-
-
?
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Anaerobranca gottschalkii produces alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus agaradhaerens produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus agaradhaerens produces beta-cyclodextrins
-
-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzymes from Bacillus circulans strans produce beta-cyclodextrins, except for strain DF 9R that also produces alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces 80% gamma-cyclodextrins with an overall conversion of starch into cyclodextrins of 14%
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces 80% gamma-cyclodextrins with an overall conversion of starch into cyclodextrins of 14%
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produce beta-cyclodextrins, except for strain 290-3 that also produces gamma-cyclodextrins
-
-
-
additional information
?
-
-
the extracelluar enzyme converts starch into non-reducing, cyclic malto-oligosacchrarides called cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus lichenifoormis produces alpha- and beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus megaterium produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus obhensis produces beta-cyclodextrins
-
-
-
additional information
?
-
-
isolation of alkaliphilic Bacillus strains and determination of their phylogenetic and phenotypic characteristics, overview
-
-
-
additional information
?
-
P05618
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus strains produce beta-cyclodextrins, strain G-825-6 also produces alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain G-825-6 produces beta-cyclodextrins and alpha-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from the Bacillus strain produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Brevibacillus brevis produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Brevibacillus brevis produces beta-cyclodextrins
-
-
-
additional information
?
-
-
CGTase catalyzes the transfer of dextrin units from cyclodextrins or longer dextrins to polyols, such as glycerol, sugars, and flavonoids
-
-
-
additional information
?
-
P31797
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces alpha- and beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Geobacillus stearothermophilus produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces alpha- and beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Geobacillus stearothermophilus produces beta-cyclodextrins
-
-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Klebsiella pneumoniae produces alpha-cyclodextrins
-
-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Klebsiella pneumoniae produces alpha-cyclodextrins
-
-
-
additional information
?
-
-
CGTase can hydrolyze glucan chains, e.g. starch, in a manner similar to alpha-amylases, but differs in its ability to form cyclodextrins as reaction products. Cyclodextrins are formed from starch molecules through intramolecular transglycosylation, i.e. cyclization, and can be made up of 6 to 8 glucan residues, alpha-, beta-, and gamma-cyclodextrin, respectively. The enzyme is multifunctional
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus campinasensis produces beta-cyclodextrins
-
-
-
additional information
?
-
-
CGTase can hydrolyze glucan chains, e.g. starch, in a manner similar to alpha-amylases, but differs in its ability to form cyclodextrins as reaction products. Cyclodextrins are formed from starch molecules through intramolecular transglycosylation, i.e. cyclization, and can be made up of 6 to 8 glucan residues, alpha-, beta-, and gamma-cyclodextrin, respectively. The enzyme is multifunctional
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus campinasensis produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus graminis produces alpha- and beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus graminis produces alpha- and beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus illinoisensis produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus illinoisensis produces beta-cyclodextrins
-
-
-
additional information
?
-
-
CGTase is an extracellular enzyme capable of converting starch or starch derivatives into cyclodextrins through an intramolecular transglycosylation reaction. Cyclodextrins are cyclic, nonreducing oligoglucopyranose molecules linked via alpha(1,4)-glycosidic bonds
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus macerans produces alpha-cyclodextrins
-
-
-
additional information
?
-
-
CGTase is an extracellular enzyme capable of converting starch or starch derivatives into cyclodextrins through an intramolecular transglycosylation reaction. Cyclodextrins are cyclic, nonreducing oligoglucopyranose molecules linked via alpha(1,4)-glycosidic bonds
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus pabuli produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus pabuli produces beta-cyclodextrins
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Paenibacillus sp. strains produce alpha- and beta-cyclodextrins
-
-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzymes from Thermoanaerobacter sp. strains produce alpha- and beta-cyclodextrins
-
-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Thermoanaerobacterium thermosulfurigenes produces alpha- and beta-cyclodextrins
-
-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Thermoanaerobacterium thermosulfurigenes produces alpha- and beta-cyclodextrins
-
-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
CaCl2
Co2+
Cu2+
Fe2+
FeCl2
K+
Mg2+
Mn2+
Na+
Zn2+
additional information
Ca2+
-
the enzyme has three Ca2+ binding sites. Ca2+ has a small contribution to the enzyme's thermostability
Ca2+
-
contains 2 mol Ca2+ per mol of enzyme, increases heat stability, denaturation temperature shifted from 70°C to 88°C
Ca2+
-
thermal stability is remarkably increased by addition of calcium ions
Ca2+
-
synergistic promoting effects of glycine and Ca2+ on the extracellular secretion of the recombinant protein in Escherichia coli, optimal at 150 mM and 20 mM, respectively, overview
Ca2+
-
the enzyme has two Ca2+ binding sites. Ca2+ has a small contribution to the enzyme's thermostability
Ca2+
thermal stability is remarkably increased by addition of calcium ions
CaCl2
-
5 mM, 20% activation of cross-linked enzyme crystals, 2% activation of soluble enzyme
FeCl2
-
5 mM, 110% activation of cross-linked enzyme crystals, inhibition of soluble enzyme
additional information
-
enzyme activity is not affected by Ca2+, Na+, K+, Fe3+, ICH2COOH, and SDS at low concentration
additional information
-
Ni2+ and Na+ ions have weak effects on the enzyme activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cyclodextrins
-
the enzyme activity is strongly inhibited by the reaction products
-
acarbose
the acceptor substrate binding site near the active site of the enzyme is involved in inhibition by acarbose, mutants K232E, F283L, and A230V show increased resistance, overview
acarbose
-
pseudotetrasaccharide, competitive inhibitor of the cyclization reaction
ethanol
-
the enzyme keeps very good levels of alpha-cyclodextrin activity using starch or maltodextrin as substrates even at 20% ethanol (around 55-60%). The degradation of the alpha-cyclodextrin is strongly inhibited by ethanol, even at very low concentrations
HgCl2
-
5 mM, 68% inhibition of cross-linked enzyme crystals, 40% of soluble enzyme
MgCl2
-
5 mM, 15% inhibition of cross-linked enzyme crystals, 22% of soluble enzyme
starch
-
substrate inhibition at 0.01 and 0.0055 mg starch/ml for free and immobilized enzyme
ZnCl2
-
5 mM, 30% inhibition of cross-linked enzyme crystals, 80% of soluble enzyme
additional information
-
the enzyme shows substrate and product inhibition
-
additional information
-
no or poor inhibition by PMSF, sodium azide, sodium m-arsenite, and 2-mercaptoethanol
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
light
-
illumination of the enzyme with white, linearly polarized light and at constant 25°C increases the enzyme activity producing a mixture of alpha-, beta-, and gamma-cyclodextrins. At a high enzyme concentration of 0.64 U/cm3, regardless the illumination time, formation of beta-cyclodextrin predominates. The highest yield of beta-cyclodextrin is afforded after 1 h illumination, but 2 h illumination leads to a significant increase in the yield of gamma-cyclodextrin
-
NaCl
enzyme shows its maximum hydrolysis activity in a buffer with 1.5 M NaCl and retains up to 65% of its activity at 0.5 M NaCl
Triton X-100
Bacillus autolyticus
-
enhances specificity and yield of beta-cyclodextrin production
additional information
-
synergistic promoting effects of glycine and Ca2+ on the extracellular secretion of the recombinant protein in Escherichia coli, optimal at 150 mM and 20 mM, respectively, overview
-
cyclohexadec-8-ene-1-one
-
increases the yield of gamma-cyclodextrin
cyclohexadec-8-ene-1-one
-
increases the yield of gamma-cyclodextrin
ethanol
Bacillus autolyticus
-
enhances specificity and yield of beta-cyclodextrin production
ethanol
-
increases yield of cyclodextrins, relative activity 104%
Isopropanol
-
increases the yield of beta-cyclodextrin
Toluene
-
relative residual activity 102%, relative activity 104%
Trichloroethylene
-
increases the yield of beta-cyclodextrin
Trichloroethylene
-
increases the yield of beta-cyclodextrin
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
soluble potato starch
-
pH 6.4, 55°C, formation of beta-cyclodextrin
-
0.08
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
-
strain 1011, acceptor maltose, mutant F183L
0.12
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
-
strain 1011, acceptor maltose, mutant F283L
0.15
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
-
strain 1011, acceptor glucose, mutant F283L
0.16
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
-
strain 1011, acceptor maltose, wild-type
0.2
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
-
strain 1011, acceptor glucose, wild-type and mutant Y195F
0.22
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
-
strain 1011, acceptor maltose, mutant Y195F
0.23
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
-
strain 1011, acceptor glucose, mutant F183L
0.24
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
-
strain 1011, acceptor maltose, mutant F183L/F259L
0.31
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
-
strain 1011, acceptor maltose, mutant Y195L
0.34
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
-
strain 1011, acceptor glucose, mutant Y195L and F183L/F259L
0.48
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
-
strain 1011, acceptor maltose, mutant F259L
0.56
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
-
strain 1011, acceptor glucose, mutant F259L
0.15
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
-
pH 6.0, 60°C, wild-type enzyme
0.2
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
-
pH 6.0, 60°C, mutant W239R
0.24
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
-
pH 6.0, 60°C, mutant S77P
0.27
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
-
pH 6.0, 60°C, mutant W239L
38.3
L-ascorbic acid
wild-type, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin
44.7
L-ascorbic acid
mutant K47W, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin
46.1
L-ascorbic acid
mutant K47F, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin
46.9
L-ascorbic acid
mutant K47V, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin
51.07
L-ascorbic acid
-
mutant enzyme Y260R/Q265K/Y195S, at pH 5.5 and 37°C
51.7
L-ascorbic acid
mutant K47L, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin
0.47
maltodextrin
-
mutant enzyme Y260R/Q265K/Y195S, at pH 5.5 and 37°C
0.48
maltodextrin
mutant K47V, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin
0.49
maltodextrin
mutant K47L, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin
0.52
maltodextrin
mutant K47F, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin
0.55
maltodextrin
mutant K47W, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin
0.64
maltodextrin
wild-type, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin
0.263
starch
-
strain 1011, beta-cyclodextrin-forming activity, mutant F183L/F259L
additional information
additional information
-
Km-value for starch: 0.0025 mg/ml (soluble enzyme), 0.0045 mg/ml (enzyme immobilized on alginate)
-
additional information
additional information
-
kinetics of the four reaction steps, overview
-
additional information
additional information
-
kinetics of hydrolyzing activity with different substrates, e.g. cyclodextrins, overview
-
additional information
additional information
-
kinetics of His-tagged wild-type and mutant enzymes, overview
-
additional information
additional information
-
reaction kinetics
-
additional information
additional information
reaction kinetics
-
additional information
additional information
-
reaction kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
dynamics of beta-cyclodextrin production, kinetics, overview
-
additional information
additional information
-
Km value is 0.69 mg/ml for wild-type, 0.57 mg/ml for mutant Q179G, 0.54 mg/ml for mutant Q179l, substrate soluble potato starch, pH 6.4, 56°C
-
additional information
additional information
-
kinetic data fit to Hill equation and lead to coefficients of 1.485 and 1.257 for the recombinant and the native enzyme, respectively
-
additional information
additional information
-
Km value is 17.2 mg/ml for beta-cyclization activity using soluble starch, pH 7.0, 55°C
-
additional information
additional information
Km value is 17.2 mg/ml for beta-cyclization activity using soluble starch, pH 7.0, 55°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.833
p-nitrophenyl-(alpha-1,4-glucopyranosyl)4-D-glucose, p-nitrophenyl-(alpha-1,4-glucopyranosyl)5-D-glucose, p-nitrophenyl-(alpha-1,4-glucopyranosyl)6-D-glucose
Bacillus circulans
-
E 192
-
0.122
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
mutant strain F283L, acceptor glucose, wild-type
0.137
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
strain 1011, acceptor maltose, mutant F283L
0.345
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
mutant strain F259L, acceptor glucose, wild-type
0.423
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
strain 1011, acceptor maltose, mutant F259L
1.97
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
mutant strain Y195L, acceptor glucose, wild-type
2.2
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
strain 1011, acceptor maltose, mutant Y195L
2.32
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
mutant strain Y195F, acceptor glucose, wild-type
2.63
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
strain 1011, acceptor maltose, mutant F183L/F259L
3.2
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
strain 1011, acceptor maltose, mutant Y195F
3.38
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
strain 1011, acceptor maltose, wild-type
3.8
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
mutant strain F183L/F259L, acceptor glucose, wild-type
4.07
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
strain 1011, acceptor glucose, wild-type
5.55
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
strain 1011, acceptor maltose, mutant F183L
15.5
3-ketobutylidene-beta-2-chloro-4-nitrophenylmaltopentaoside
Bacillus sp.
-
mutant strain F183L, acceptor glucose, wild-type
558
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
Thermoanaerobacterium thermosulfurigenes
-
pH 6.0, 60°C, mutant S77P
644
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
Thermoanaerobacterium thermosulfurigenes
-
pH 6.0, 60°C, mutant W239R
1082
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
Thermoanaerobacterium thermosulfurigenes
-
pH 6.0, 60°C, mutant W239L
1244
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
Thermoanaerobacterium thermosulfurigenes
-
pH 6.0, 60°C, wild-type enzyme
0.000106
L-ascorbic acid
Paenibacillus macerans
-
mutant enzyme Q265K/Y195S, at pH 5.5 and 37°C
0.00011
L-ascorbic acid
Paenibacillus macerans
-
mutant enzyme Y260R/Q265K, at pH 5.5 and 37°C
0.000114
L-ascorbic acid
Paenibacillus macerans
-
mutant enzyme Y260R/Q265K/Y195S, at pH 5.5 and 37°C
0.000133
L-ascorbic acid
Paenibacillus macerans
-
mutant enzyme Y260R/Y195S, at pH 5.5 and 37°C
0.004
maltodextrin
Paenibacillus macerans
O52766
mutant K47W, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin; wild-type, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin
0.005
maltodextrin
Paenibacillus macerans
O52766
mutant K47F, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin; mutant K47V, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin
0.006
maltodextrin
Paenibacillus macerans
O52766
mutant K47L, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin
0.0124
maltodextrin
Paenibacillus macerans
-
mutant enzyme Y260R/Q265K/Y195S, at pH 5.5 and 37°C
127.5
soluble potato starch
Bacillus circulans
-
mutant Q179L, pH 6.4, 56°C, calculated as production of beta-cyclodextrin
-
246.2
soluble potato starch
Bacillus circulans
-
wild-type, pH 6.4, 56°C, calculated as production of beta-cyclodextrin
-
247.2
soluble potato starch
Bacillus circulans
-
mutant Q179G, pH 6.4, 56°C, calculated as production of beta-cyclodextrin
-
803
soluble potato starch
Bacillus circulans
-
pH 6.4, 55°C, formation of beta-cyclodextrin
-
2.6
soluble starch
Bacillus sp.
-
mutant NS182G, pH 6.0, 60°C, calculated as production of beta-cyclodextrin; mutant S182E, pH 6.0, 60°C, calculated as production of beta-cyclodextrin
-
3.13
soluble starch
Bacillus sp.
-
wild-type, pH 6.0, 60°C, calculated as production of beta-cyclodextrin
-
3.5
soluble starch
Bacillus sp.
-
mutant N28R, pH 6.0, 60°C, calculated as production of beta-cyclodextrin
-
0.00267
starch
Bacillus sp.
-
strain 1011, beta-cyclodextrin-forming activity, mutant F183L/F259L
48
starch
Bacillus circulans
P30920
pH 6.0, 60°C, beta-cyclization activity, mutant A230V/H140Q
329
starch
Bacillus circulans
P30920
pH 6.0, 60°C, beta-cyclization activity, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
730
soluble potato starch
Bacillus circulans
-
pH 6.4, 55°C, formation of beta-cyclodextrin
8845
additional information
additional information
Bacillus sp.
-
kcat/Km value for wild-type is 1.82 mg/ml, pH 6.0, 60°C
2
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Ki-value for starch: 0.01 mg/ml (soluble enzyme), 0.0055 mg/ml (enzyme immobilized on alginate)
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14.4
-
beta-cyclodextrin-forming activity, recombinant wild-type enzyme
85.1
-
alpha-cyclodextrin-forming activity, recombinant wild-type enzyme
255
2268
-
glycosyltransferase gene fused with thioredoxin, hexa-histidine and S-protein at the N-terminus and a proline-rich peptide at the C-terminus, pH 6.0, 40°C
additional information
additional information
Bacillus autolyticus
-
332.5 units/mg, 1 unit is the amount of enzyme which decreases 10% of the absorbance at 700 nm per min
additional information
-
strain C31, 6.623.4 units, 1 unit is the amount of enzyme which causes 10% reduction in the intensity of the blue colour of the starch-iodine complex
additional information
-
strain DF9, R-variation, 353 units, 1 unit is the amount which produces a difference of absorbance of 1.0 per minute; strain DF9, S-variation, 388 units, 1 unit is the amount which produces a difference of absorbance of 1.0 per minute
additional information
-
activities of free and immobilized enzymes, overview
additional information
-
No. 5 strain, 258 units, 1 unit is the amount of enzyme which gaves a linear increase of 1% transmission per min at 40°C
additional information
-
Ha3-3-2/ATCC 39612, 45.000, 1 unit is the activity producing a 10% reduction in the intensity of the blue colour (700 nm) from a 10 min reaction at 50°C and pH 8.5
additional information
-
fed-batch fermentation results in production of a CGTase activity up to 56 unit/ml with 65 g dry cells/l
additional information
-
enzyme activities in U/ml with different fermentation methods, overview
additional information
-
specific activity after dissolution and dialysis 28 units/mg protein, 1 unit is the amount of enzyme which gives a linear increase of 1% transmission per minute at 40°C, immobilized enzyme 230-450 units/g solid
additional information
-
comparison of alpha-, beta-and gamma-cyclization activity of wild-type and mutant enzymes, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 4.7
4.6
-
ATCC 21783 contains 3 isozymes, neutral, alkalic and acidic, possessing markedly different pH optima, 4.6, 7.0 and 9.5
5 - 5.7
5 - 5.7
5.2
5.5 - 5.8
5.5
5.5
5.7
5.9 - 6.5
-
the optimum pH for dextrinizing and cyclization activities of purified CGTases from both sources are similar around pH 6.5 and pH 5.9 respectively
6 - 7
6.1 - 6.2
6.5
6.5
6.8
7.2
7.5
8 - 9
8.5
9.5
-
ATCC 21783 contains 3 isozymes, neutral, alkalic and acidic, possessing markedly different pH optima, 4.6, 7.0 and 9.5
10
additional information
-
the enzymes are more active in glycine/NaOH buffer compared with Na2HPO4/NaH2PO4 buffer at the same pH
5
-
optimum pH for L-ascorbic acid-2-O-alpha-D-glucoside formation
5
-
free and glutaraldehyde-activated chitosan spheres-immobilized enzyme
5.5
-
enzyme immobilized on glyoxyl-agarose and free enzyme present similar pH/activities profiles, with two peaks at pH values of 5.5 and 7 and a minimum at pH 6.0-6.5 in both amylolytic and CGTase activities
7
-
ATCC 21783, purified enzyme, crude enzyme has 3 pH optima, 4.5-5.0, 7.0 and 8.0-9.0
7
-
ATCC 21783 contains 3 isozymes, neutral, alkalic and acidic, possessing markedly different pH optima, 4.6, 7.0 and 9.5
7
-
enzyme immobilized on glyoxyl-agarose and free enzyme present similar pH/activities profiles, with two peaks at pH values of 5.5 and 7 and a minimum at pH 6.0-6.5 in both amylolytic and CGTase activities
8
-
beta-cyclodextrin production shows increment up to pH 8.0 but decreases at pH values higher than 9
10
-
around, wild-type enzyme and mutant enzymes A223H, A223R and A223K, gamma-cyclodextrin-forming activity
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 9.5
4 - 9
-
enzyme immobilized on glyoxyl-agarose and free enzyme present similar pH/activities profiles, with two peaks at pH values of 5.5 and 7 and a minimum at pH 6.0-6.5 in both amylolytic and CGTase activities. Activities decrease after these two maximum values. The glyoxyl CGTase retains 30% of amylase activity at pH 4 and 50% at pH 9. The soluble enzyme retains 10% and 30%, respectively. In synthetic activities differences are not significant
4 - 8.5
-
pH 4.0: about 65% of maximal activity, pH 8.5: about 65% of maximal activity, wild-type enzyme
4 - 8.5
4 - 6
4.5 - 10
-
activity range, about 20% of maximal activity at pH 4.5, and 40% at pH 10.0
5 - 10
5 - 7
-
pH 5.0: about 25% of maximal activity, pH 7.0: about 60% of maximal activity, the enzyme does not show any activity at pH 4.0 and at pH 10.0
5 - 8
5 - 9
5 - 7
-
pH 5.0: about 70% of maximal activity, pH 9.0: about 70% of maximal activity, native enzyme
5 - 8
5 - 9
-
pH 5.0: about 50% of maximal activity, pH 9.0: about 55% of maximal activity, native enzyme
5 - 10
-
pH 5.0: about 70% of maximal activity, pH 10.0: about 50% of maximal activity
5 - 8
pH 5.0: about 40% of maximal activity, pH 8.0: about 50% of maximal activity
5 - 8
-
pH 5: soluble enzyme shows about 50% of maximal activity, soluble enzyme shows about 60% of maximal activity, pH 8: soluble enzyme shows 40% of maximal activity, immobilized enzyme shows about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30 - 37
36
37
40
40 - 60
45
45 - 50
50
50 - 55
55
60
60 - 65
65
70
75
80
80 - 85
85
-
at pH 6.0, glutaraldehyde-activated chitosan spheres-immobilized enzyme
90
-
maximal cyclization activity of enzyme immobilized on glyoxyl-agarose, substrate: dextrin
additional information
-
pT16 shows broader optimum temperatures for both dextrinizing and cyclization activities
70
-
optimum for L-ascorbic acid-2-O-alpha-D-glucoside formation
80 - 85
-
maximal cyclization activity of soluble enzyme, substrate: dextrin
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
-
about 65% activity at 20°C, around 95-100% activity at 30-50°C, about 50% activity at 60°C
30 - 70
30 - 70
35 - 80
-
activity range, about 35% of maximal activity at 35°C and 80°C
40 - 70
-
40°C: about 50% of maximal activity, 70°C: about 80% of maximal activity
40 - 75
-
40°C: about 40% of maximal activity, 75°C: about 15% of maximal activity, soluble enzyme
40 - 80
45 - 70
-
45°C: soluble enzyme shows about 50% of maximal activity, enzyme immobilized on glyoxyl-agarose shows about 60% of maximal activity, 70°C: soluble enzyme shows about 60% of maximal activity, enzyme immobilized on gyoxyl-agarose shows about 75% of maximal activity
50 - 70
50 - 90
50°C: about 45% of maximal activity, 90°C: about 35% of maximal activity
50 - 80
55 - 70
-
55°C: about 75% of maximal activity, 70°C: about 90% of maximal activity
55 - 80
-
55°C: about 60% of maximal activity, about 40% of maximal activity
60 - 100
-
60°C: about 55% of maximal activity, 100°C: about 50% of maximal activity, soluble enzyme and enzyme immobilized on glyoxyl-agarose, substrate: dextrin
30 - 70
-
30°C: about 45% of maximal activity, 70°C: about 80% of maximal activity, native enzyme
30 - 70
-
30°C: about 450% of maximal activity, 90°C: about 50% of maximal activity, native enzyme
40 - 80
-
40°C: about 60% of maximal activity, 80°C: about 45% of maximal activity,cross-linked enzyme crystals
40 - 80
-
40°C: immobilized enzyme shows about 55% of maximal activity, soluble enzyme about 65% of maximal activity, 80°C: immobilized enzyme shows about 50% loss of maximal activity, soluble enzyme shows about 70% of maximal activity
50 - 70
-
50°C: about 15% of maximal activity, 70°C: about 20% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
production of CGTase is examined in submerged and solid-state fermentations. CGTase activity is highest in submerged fermentations with the greatest production observed at 48-72 h
-
production of CGTase is examined in submerged and solid-state fermentations. CGTase activity is highest in submerged fermentations with the greatest production observed at 48-72 h
-
additional information
-
conditions used to produce cyclodextrins with cyclodextrin glycosyltransferase from Bacillus circulans DF 9R are optimized using experimental designs. The optimum conditions for cyclodextrin production are: 5% (w/v) cassava starch, 15 U of enzyme per gram of substrate, reaction temperature of 56°C and pH 6.4. After 4 h, the proportion of starch converted to cyclodextrin reaches 66% (w/w) and the weight ratio of alpha-cyclodextrin:beta-cyclodextrin:gamma-cyclodextrin is 1.00:0.70:0.16
additional information
-
conditions used to produce cyclodextrins with cyclodextrin glycosyltransferase from Bacillus circulans DF 9R are optimized using experimental designs. The optimum conditions for cyclodextrin production are: 5% (w/v) cassava starch, 15 U of enzyme per gram of substrate, reaction temperature of 56°C and pH 6.4. After 4 h, the proportion of starch converted to cyclodextrin reaches 66% (w/w) and the weight ratio of alpha-cyclodextrin:beta-cyclodextrin:gamma-cyclodextrin is 1.00:0.70:0.16
-
additional information
-
optimization of carbon and nitrogen concentration in the feed medium using central composite design in order to enhance the production of CGTase from Bacillus sp. TS1-1 by fed batch fermentation
additional information
-
optimal growth temperature of strains 20RF, 8SB and 24WE is 38-40°C
additional information
-
optimization of carbon and nitrogen concentration in the feed medium using central composite design in order to enhance the production of CGTase from Bacillus sp. TS1-1 by fed batch fermentation
-
additional information
-
optimal growth conditions for wild-type strain T16 and transfected strain pT16, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
-
-
additional information
-
no alpha-CGTase activity in the soluble cytoplasmic fraction, very low activity in the periplasmic fraction
-
additional information
-
no alpha-CGTase activity in the soluble cytoplasmic fraction, very low activity in the periplasmic fraction
-
-
additional information
the enzyme sequence contains a signal peptide of 34 residues
-
additional information
-
the enzyme sequence contains a signal peptide of 34 residues
-
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
38000
62000
65000
66000
66800
67000
68000
70000
71000
72000
74000
74010
strain IFO3490, amino acid composition deduced from nucleotide sequence
75000
75370
strain NO2, amino acid composition deduced from nucleotide sequence
76000
77000
78000
80000
82000
85000 - 88000
85000
88000
76000
-
x * 76000, about, His-tagged wild-type and mutant enzymes, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
?
-
x * 74000, SDS-PAGE; x * 74352, calculated from amino acid sequence
?
-
x * 74000, SDS-PAGE; x * 74352, calculated from amino acid sequence
-
?
-
x * 76000, about, His-tagged wild-type and mutant enzymes, SDS-PAGE
monomer
Bacillus autolyticus 11149
-
1 * 70000, SDS-PAGE
-
monomer
Bacillus sp. Ha3-3-2/ATCC 39612
-
1 * 68000, ATCC 39612/Ha3-3-2, SDS-PAGE
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
enzyme peptide mapping and sequencing, overview. Enzyme structure-function relationship, involving protein ethoxyformylation, overview
additional information
-
enzyme peptide mapping and sequencing, overview. Enzyme structure-function relationship, involving protein ethoxyformylation, overview
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method at 293 K. X-ray diffraction data are collected to 2.2 A. The crystal belongs to space group R3, with unit-cell parameters a = b = 211.6, c = 52.7 A
-
hanging-drop vapour-diffusion method, crystal structure of native and acarbose-complexed mutant CGTase F283L and F283Y
-
hanging drop vapor diffusion technique. Cross-linked enzyme crystals can be useful biocatalysts because they are stable at elevated temperature, in organic solvents, and in the presence of enzyme inactivation surfactant. They also maintain their activity against protein-digesting enzyme
-
mutant Y167H, hanging drop vapor diffusion method, using 15% (w/v) PEG 4000, 0.05 M Tris-HCl, 0.1 M sodium acetate buffer, 25 mM Na2HPO4, 150 mM NaCl, 10 mM imidazole pH 8.5
mutant Y195I, hanging drop vapor diffusion method, using 0.2 M sodium acetate trihydrate, 0.1 M Tris hydrochloride pH 9.0, 30% (w/v) polyethylene glycol 4000, at 22°C
-
purified recombinant mutant S77P CGTase in 10 mM sodium acetate, pH 5.5, large crystals from 17-20%-saturated ammonium sulfate at room temperature in 100 mM HEPES, pH 7.6, or 100 mM HEPES, pH 7.8, or 100 mM Tris/HCl, pH 8.0, like the wild-type enzyme, crystals are soaked in 25% v/v glycerol and directly flash-cooled, or soaked in 2% w/v acarbose, 4% w/v maltohexaose and 25% glycerol in 20% saturated ammonium sulfate for 25 min followed by flash-cooling, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
5.5 - 9
5.5 - 9.5
5.5 - 9
6 - 10
6 - 8
6 - 9
6 - 9.5
6 - 10
6 - 7
-
purified native enzyme, 50°C, 4 h, almost completely stable
702110
6 - 9
-
the enzyme is stable from pH 6.0 to 9.0 for 30 min with a gradual loss of activity at higher and lower pH values in the range of 6.0-9.0
737302
7 - 8
-
strain E 192, maximum stability, only 14% decrease in activity at pH 7.0
488842
7 - 10
7 - 9
8 - 10
additional information
4 - 10
-
after 1 h of incubation, the enzyme shows less than 20% activity at pH 4.0 and 5.0, about 35% at pH 6.0, 100% at pH 7.0, about 80% at pH 8.0, about 30% at pH 9.0, and about 20% activity at pH 10.0
735782
5.5 - 9
Bacillus autolyticus
-
stable for 12 h at 40°C, below 40°C stable for 1 h at pH 6.0
488849
8 - 10
-
purified native enzyme, 50°C, 4 h, 16.8% retaining activity
702110
additional information
-
the immobilized and the crosslinked imprinted CGTase shows higher stability in the ranges from pH 3 to 7 and from pH 9 to 11
673578
additional information
-
the immobilized and the crosslinked imprinted CGTase are more stable than the native enzyme in the pH ranges from 3 to 6 and 8 to 11
673578
additional information
-
the recombinant enzyme is more stable at higher temperature and lower pH
687470
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 80
-
enzyme is stable from 4-45°C, still has 85% actvity after 30 min at 60°C, 40% activity after 30 min at 70°C, loses almost all activity after 30 min at 80°C
20 - 60
-
the enzyme remains fully stable between 20 and 40°C for 30 min, while at 50°C activity decreases to about 65% and is lost at 60°C
25
-
if submitted to strong stirring, promoting the apparition of gas bubbles and shear forces, the enzyme becomes inactivated at 25°C. This inactivation does not occur if the enzyme is immobilized on any porous support
30
30 - 65
-
Bacillus sp. strain 8SB synthesises a thermostable alkaline beta-CGTase, stability of the enzymes from diverse strains is strain-dependent, overview
35 - 65
-
purified native enzyme, 80% remaining activity at 35-65°C, pH 8.0, after 4 h, thermal deactivation above 70°C
40 - 60
-
strain E 192, heat labile, rapid inactivation at temperatures above 45, remaining activity is 75% after 20 min at 40°C, 10% at 50°C and only 5% after 1 min at 60°C, protected by substrate and Ca2+ enzyme is stable for at least 24 h at pH 6.0, very stable at pH 7.0, 48 h without any loss of activity
40 - 90
-
after 1 h of incubation, the enzyme shows about 43% activity at 40°C, about 80% at 50°C, about 90% at 55°C, 100% at 60°C, about 78% at 70°C, about 35% at 80°C, and about 20% activity at 90°C
40
40 - 50
-
immobilized enzyme is stable at 40°C, heat inactivation above 50°C
40
45 - 55
-
stable up to 45°C, 13.4% activity at 50°C, no activity above 55°C
50
50 - 55
-
thermal stability of immobilized enzyme on chitosan increases from 50°C to 55°C
50 - 60
-
purified enzyme is quite stable at 50°C, but loses 80% of its activity at 60°C for 30 min
50 - 70
-
immobilized enzyme is more stable than soluble enzyme, inactivation of the soluble enzyme at 50°C is 1.6 times, at 60°C is 6.9 times and at 70°C is 24.3 times faster
50
55
58 - 60
60
60 - 80
-
the native enzyme shows a half-life of 93.45 min, 56.34 min, and 43.57 min at 60, 70, and 80°C, respectively
60
65
69
-
5 mM CaCl2 shifts the apparent melting point from 60°C to 69°C
70 - 80
70
75
80
80 - 110
85
85 - 100
extreme thermostability with addition of Ca2+, no loss of activity after 80 min at 85°C, half-life of 20 min at 100°C, recombinant enzyme half-life of 40 min at 100°C
90 - 100
-
extremely heat-stable, stable above 100°C in presence of starch
110
additional information
40
-
purified native enzyme, thermal stability at 40°C is elevated 10fold in the presence of 1% maltodextrin
40
-
purified recombinant enzymes, the wild-type enzyme shows a half-life of 8.0 h, the mutant enzymes of 6.0-7.9 h, overview
40
-
the recombinant wild-type enzyme has a half-life of 8.0 h, while the recombinant K47 mutants show half-lives of 4.8-7.2 h
55
-
half-life of soluble enzyme at pH 7 is 1.5 h. The immobilization of the enzyme on CNBr-agarose does not promote an increment in the stability of the enzyme at 55°C, although it prevents the effect of the stirred system
60
-
5 mM CaCl2 shifts the apparent melting point from 60°C to 69°C
60
-
ATCC 21783, stable up to; ATCC 21783, stable up to, Ca2+ addition increases thermal stability
60
-
half-life: 9.7 min for wild-type enzyme, 8 min for mutant enzyme T186Y, 35 min for mutant enzyme N188D, 11.6 min for mutant enzyme K192E and 56 min for mutant enzyme N188D/K192R
60
-
half-life 22 min for wild-type, 94 min for mutant S182G, 31 min for mutant S182E
60
-
half-life 22 min for wild-type, 57 min for mutant carrying B domain from Bacillus stearothermophilus ET1
60
-
the enzyme is thermally stable up to 60°C without substrate during 1 h in the presence of 10 mM CaCl2
60
-
pH 6.0, 30 min, native enzyme shows about 10% loss of activity. Immobilized and crosslinked imprinted CGTase are stable
60
-
pH 6.0, 30 min, native enzyme shows about 10% loss of activity. Iimmobilized and crosslinked imprinted CGTase are stable
60
purified enzyme, 20 min during the purification process, 1.5fold increased enzymatic activity
70 - 80
-
does not lose activity by heat treatment for 10 min at 70-75°C, pH 5.5-9.5 in presence of CaCl2, loses half of the activity by heating at 80°C for 10 min
70
-
30 min, about 50% loss of activity of wild-type enzyme, about 70% loss of activity of mutant enzymes DELTA154-160 and Y96M
70
-
pH 6.0, 30 min, native enzyme shows about 50% loss of activity. Immobilized and crosslinked imprinted CGTase show about 15% loss of activity
70
-
pH 6.0, 30 min, native enzyme is completely inactivated. Immobilized and crosslinked imprinted CGTase shows about 50% loss of activity
75
-
glycerol, sorbitol and sucrose effected thermostability, thermostability increases in 1,4-dioxane and n-octane, retains 81% of its initial activity after incubation for 90 min
80
-
15 min at 80°C, after incubation for 12 h reactivation to a little restactivity
80 - 110
above 80°C activity increases by heat treatment, enzyme is irreversibly unfolded above 110°C
additional information
-
thermal stability is improved in the presence of maltodextrin, starch or CaCl2
additional information
-
enzyme is more heat resistant after its pretreatment in pH 9.0 at high temperatures 65-70°C, than at pH 6.0 under the same reaction conditions
additional information
-
the recombinant enzyme is more stable at higher temperature and lower pH
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ stabilizes against thermal inactivation, 5 mM CaCl2 shifts the apparent melting point from 60°C to 69°C
-
cell membrane-immobilized purified enzyme retains, after 240 h repeated batch cultivation, 1.3-2.3fold increase of the CGTase yield compared to free cells at the end of the process, overview
-
cross-linked enzyme crystals are slightly more resistant to 2-butanol and acetonitrile than DMSO. In 15% solution of 2-butanol, over 100% of the activity is retained in CGTase-cross-linking enzyme crystals while 28% of the activity remains in the case of soluble CGTase
-
enzyme immobilized on alginate shows a high operational stability by retaining almost 75% of the initial activity after seventh use
-
high substrate concentrations stabilize against thermal inactivation
-
immobilization in strongly hydrophilic microenvironment markedly enhances conformational stability in a wide temperature and pH range
-
more than 80% of the initial immobilized and crosslinked imprinted CGTase activity is retained for up to five cycles of synthesis reactions
prolonged digestion with trypsin does not affect the catalytic properties
-
SDS, 1%, only 7% of the activity of soluble enzyme activity remains, cross-linked enzyme crystals exhibit strong activity
-
the dextran (MW 47000)-conjugated form of the enzyme retains about 70.28% of the original specific catalytic activity exhibited by the native enzyme
-
the immobilized and CD8-crosslinked imprinted CGTase shows 15% higher stability in phosphate buffer containing up to 50% ethanol or cyclohexane compared to the native enzyme
-
the immobilized and CD8-crosslinked imprinted CGTase shows 30% higher stability in phosphate buffer containing up to 50% ethanol or cyclohexane compared to the native enzyme
-
the operational half-life of the packed-bed enzyme reactor (enzyme immobilized onto a cation exchanger by ionic interaction, poly-lysine fused immobilization) is estimated 12 days at 25°C and pH 6.0
-
the temperature stability of the immobilized and crosslinked imprinted CGTase at 60°C is considerably higher than that of the native enzyme
thermostability at 60°C and pH 7 reveals that the enzyme adsorbed on ionic supports is slightly less stable than the CNBr-agarose immobilized enzyme. The enzyme immobilized on Eupergit presents a very similar stability to this preparation while the glyoxyl-agarose is much more stable than any other preparation (by around a 15-fold factor) the glyoxyl-agarose immobilized enzyme is much more stable than any other preparation in presence of ethanol
-
more than 80% of the initial immobilized and crosslinked imprinted CGTase activity is retained for up to five cycles of synthesis reactions
-
more than 80% of the initial immobilized and crosslinked imprinted CGTase activity is retained for up to five cycles of synthesis reactions
-
the temperature stability of the immobilized and crosslinked imprinted CGTase at 60°C is considerably higher than that of the native enzyme
-
the temperature stability of the immobilized and crosslinked imprinted CGTase at 60°C is considerably higher than that of the native enzyme
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-butanol
-
in 15% solution of 2-butanol, over 100% of the activity is retained in CGTase-cross-linking enzyme crystals while 28% of the activity remains in the case of soluble CGTase
2-propanol
acetonitrile
-
in 15% solution of 2-butanol, over 100% of the activity is retained in CGTase-cross-linking enzyme crystals while 60% of the activity remains in the case of soluble CGTase
benzene
chloroform
cyclohexane
Ethanol
hexane
Methanol
toluene
2-propanol
-
stable in presence, relative residual activity 82%
-
2-propanol
-
stable in presence, but not active, relative residual activity 96%
Ethanol
-
stable in presence, but not active, relative residual activity 99%
Methanol
-
stable in presence, but not active, relative residual activity 98%
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.05 M Tris-HCl, pH 7.0 or sodium acetate buffer, pH 6.5 for at least 6 months without loss of activity
-
three-months storage of enzyme at 4°C and illuminated with white, linearly polarized light does not reduce the enhanced enzyme activity
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetone precipitation, DEAE-cellulose column chromatography, and Sephadex G-100 gel filtration
-
from the alkalophilic strain 20RF; from the alkalophilic strain 8SB; from the alkalophilic strains 8SB and 20RF
-
mutant Y167H with ammonium sulfate precipitation and Ni-NTA agarose column chromatography
native CGTase 22.9fold to homogeneity by hydrophobic interaction chromatography and starch adsorption
native enzyme 11.4fold from strain BL-12 by ultrafiltration and beta-cyclodextrin polymer affinity chromatography
-
native enzyme 13.7fold from strain ATCC 21783 by ultrafiltration and consecutive starch adsorption
native enzyme 315fold by ammonium sulfate fractionation, beta-cyclodextrin affinity chromatography, and ultrafiltration
-
native enzyme 99fold and recombinant enzyme 7fold from Escherichia coli both by starch adsorption, and hydrophobic interaction or beta-cyclodextrin affinity chromatography
-
native enzyme about 200fold from strain H69-3 by gel filtration, and one or two different steps of anion exchange chromatography
-
native enzyme by adsorption on starch, ion exchange chromatography, and gel filtration
-
native extracellular enzyme 23.1fold from an alkalophilic strain by ultrafiltration and anion exchange chromatography to homogeneity
-
Ni-NTA agarose column chromatography and Sephacryl-100 gel filtration
-
recombiant enzyme 25fold from Escherichia coli, by heat treatment at 60°C, hydrophobic interaction chromatography and starch adsorption, overview
recombinant
recombinant enzyme
recombinant enzyme from Escherichia coli strain BL21(DE3) inclusion bodies
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
wild-type enzyme and mutant enzymes H59Q, Y96M, 90-PPI-92, and DELTA(154–160) expressed in Escherichia coli
-
-
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; strain IFO3490, vector plasmid pTB523, gene cgtM cloned in Bacillus subtilis NA-1, sequence determined, chimeric GTAse gene constructed by using cgt-1 from Bacillus stearothermophilus NO2
; strain NO2, vector plasmid pTB523, 3genes, cgt-1, cgt-5 and cgt-232 cloned in Bacillus subtilis NA-1, sequence determined, chimeric GTAse gene constructed by using cgt-1 and cgtM from Bacillus macerans IFO3490
ATCC21783 expressed in Bacillus subtilis; no. 38-2 cloned and sequenced; no. 8 cloned, sequenced and expressed in Escherichia coli
-
coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase in Escherichia coli. The optimal coexpression partner, human peptidyl-prolyl cis-trans isomerase, is applied to fed-batch cultures of recombinant Escherichia coli in an attempt to develop an industrialy viable process
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109
-
DNA and amino acid sequence determination and analysis, phylogenetic tree
expressed as inclusion body in recombinant Escherichia coli. The refolding yield of CGTase is enhanced by 71% by the immobilized poly-arginine fused minichaperone (MiniELR10) compared with a conventional refolding method. Minichaperone immobilized by poly-arginine fusion could assist refolding of heterologous proteins expressed as inclusion body
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli strain BL21(DE3), glycine, as a medium supplement, can enhance the extracellular secretion of recombinant alpha-CGTase by 11fold. Glycine supplementation exerts impaired cell growth inhibiting an increased enzyme production, but Ca2+ can remedy cell growth inhibition induced by glycine, thereby leading to further increase in the glycine-enhanced extracellular secretion of recombinant alpha-CGTase, effects on the bacterial cell membrane permeability, overview
-
expression in Saccharomyces cerevisiae strain EBY100, subcloning in Escherichia coli strain DH5 alpha
-
expression of cyclodextrin glycosyltransferase gene fused with thioredoxin, hexa-histidine and S-protein at the N-terminus and a proline-rich peptide at the C-terminus, in Escherichia coli
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression of wild-type and mutant enzymes in Bacillus subtilis strain DB104A
expression of wild-type and mutant enzymes in Bacillus subtilis strain DB104A, subcloning in Escherichia coli strain MC1061
-
gene cgt, expression in Escherichia coli strain JM109 and K12 N3406, enzyme secretion, batch fermentation method optimization via medium improvement, overview
-
gene cgtase, DNA and amino acid sequence determination and analysis, expression in Escherichia coli periplasmic fraction in different strains at low amounts, overview
gene pfcgt, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli
isolation of alkaliphilic Bacillus strains and determination of their phylogenetic and phenotypic characteristics, overview
-
mutant enzymes H59Q, Y96M, 90-PPI-92, and DELTA(154–160) are constructed and produced using a recombinant Escherichia coli with a secretive expression system extracellularly
-
no. 38-2 cloned and sequenced; no. 8 cloned, sequenced and expressed in Escherichia coli
-
nucleotide sequence determined
overexpression and extracellular secretion of the recombinant alpha-cyclodextrin glycosyltransferase in Escherichia coli strain BL21(DE3), promotable by glycine, when supplemented optimally at the middle of the exponential growth phase at 1%, the enzyme production is increased by 11fold, glycine supplementation at the beginning of cell growth achieves a 1.2fold activation, overview. Glycine increases the cell membrane permeability, mechanism, overview
-
pET-8c vector, gene cloned and expressed in Escherichia coli BL21(DE3)
phylogenetic analysis
phylogenetic analysis, expression in Bacillus subtilis strain DB104A
-
phylogenetic analysis, expression in Bacillus subtilis strain NA-1
phylogenetic analysis, expression in Escherichia coli strain BL21(DE3)
phylogenetic analysis, expression of the enzyme from strain BC8 in Escherichia coli strain JM103, and of the enzyme from strain BC251 in Bacillus subtilis strain DB104A
-
sp. 17-1, nucleotide sequence determined; sp. B1018, nucleotide sequence determined
-
strain 1011 cloned in Escherichia coli bacteriophage lambdaD69 and recloned in Escherichia coli plasmid pBR322
-
strain NO2, mutant CGTases constructed from cgt1 gene and expressed in Bacillus subtilis NA-1
-
subcloning in Escherichia coli strain JM109, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
the cyclodextrin glucanotransferase gene is cloned into plasmid pYD1, which allows regulated expression, secretion, and detection. The expression of CGTase with a-agglutinin at the N-terminal end on the extracellular surface of Saccharomyces cerevisiae is confirmed by immunofluorescence microscopy. This surface-anchored CGTase gives the yeast the ability to directly utilize starch as a sole carbon source and the ability to produce the anticipated products, cyclodextrins, as well as glucose and maltose. The resulting glucose and maltose, which are efficient acceptors in the CGTase coupling reaction, could be consumed by yeast fermentation and thus facilitated cyclodextrin production. On the other hand, ethanol produced by the yeast may form a complex with cyclodextrin and shift the equilibrium in favor of cyclodextrin production. The yeast with immobilized CGTase produces 24.07 mg/ml cyclodextrins when it is incubated in yeast medium supplemented with 4% starch
-
DNA and amino acid sequence determination and analysis, phylogenetic tree
-
DNA and amino acid sequence determination and analysis, phylogenetic tree
phylogenetic analysis, expression in Escherichia coli strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A230V
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
A315D
-
the mutation significantly changes the contribution of Ca2+ to the enzyme's thermostability
D577A
-
the mutation increases the beta-cyclization activity of the enzyme with 23% higher catalytic efficiency compared to the wild type. The mutation also increases the affinity for maltodextrin
D577E
-
the mutant displays an 11.2% increase in the beta-cyclization activity compared to the wild type enzyme
D577G
-
the mutation increases the beta-cyclization activity of the enzyme with 43.9% higher catalytic efficiency compared to the wild type. The mutation also increases the affinity for maltodextrin
D577H
-
the mutant displays a slight decrease in the beta-cyclization activity compared to the wild type enzyme
D577I
-
the mutation decreases the beta-cyclization activity of the enzyme
D577K
D577L
-
the mutation decreases the beta-cyclization activity of the enzyme
D577R
-
the mutant displays a 30.7% increase in the beta-cyclization activity compared to the wild type enzyme
D577V
-
the mutation decreases the beta-cyclization activity of the enzyme
F283L
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
H140Q
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
K192R
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 11.6 min for the mutant enzyme
K232E
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
N188D
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 35 min for the mutant enzyme
N188D/K192R
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 56 min for the mutant enzyme
Q179G
-
mutation to residue G which is conserved in all the corresponding enzymes except in that from Bacillus circulans Df 9R. Activity and kinetic parameters remain unchanged
Q179L
-
mutation results in a different ratio of cyclodextrin products with a ratio for alpha- to beta- to gamma-cyclodextrin 1:1.7:0.7, a lower catalytic efficiency, and a decreased ability to convert starch into cyclodextrins
T185S
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 14.8 min for the mutant enzyme
T186Y
-
decrease in half-life at 60°C from 9.7 min for the wild-type enzyme to 8 min for the mutant enzyme
A230V
-
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
-
F283L
-
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
-
H140Q
-
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
-
K232E
-
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
-
Q179G
-
mutation to residue G which is conserved in all the corresponding enzymes except in that from Bacillus circulans Df 9R. Activity and kinetic parameters remain unchanged
-
Q179L
-
mutation results in a different ratio of cyclodextrin products with a ratio for alpha- to beta- to gamma-cyclodextrin 1:1.7:0.7, a lower catalytic efficiency, and a decreased ability to convert starch into cyclodextrins
-
D577A
-
the mutation increases the beta-cyclization activity of the enzyme with 23% higher catalytic efficiency compared to the wild type. The mutation also increases the affinity for maltodextrin
-
D577E
-
the mutant displays an 11.2% increase in the beta-cyclization activity compared to the wild type enzyme
-
D577G
-
the mutation increases the beta-cyclization activity of the enzyme with 43.9% higher catalytic efficiency compared to the wild type. The mutation also increases the affinity for maltodextrin
-
D577H
-
the mutant displays a slight decrease in the beta-cyclization activity compared to the wild type enzyme
-
D577I
-
the mutation decreases the beta-cyclization activity of the enzyme
-
D577K
-
the mutant displays a 1.5% increase in the beta-cyclization activity compared to the wild type enzyme
-
D577L
-
the mutation decreases the beta-cyclization activity of the enzyme
-
D577R
-
the mutant displays a 30.7% increase in the beta-cyclization activity compared to the wild type enzyme
-
D577V
-
the mutation decreases the beta-cyclization activity of the enzyme
-
A223H
-
mutant snzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 2fold increases at pH 7.5. pH activity profiles of the mutant shows higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
A223K
-
mutant enzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 3fold increases at pH 7.5. pH activity profiles of the mutant show higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
A223R
-
mutant enzyme shows a 4fold increase in gamma-cycodextrin-forming activity at pH 7.5 and 1.5fold increase in activity at pH 10.0. Mutant enzyme shows higher activity in pH range pH 6-10.5
A223H
-
mutant snzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 2fold increases at pH 7.5. pH activity profiles of the mutant shows higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
-
A223K
-
mutant enzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 3fold increases at pH 7.5. pH activity profiles of the mutant show higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
-
A223R
-
mutant enzyme shows a 4fold increase in gamma-cycodextrin-forming activity at pH 7.5 and 1.5fold increase in activity at pH 10.0. Mutant enzyme shows higher activity in pH range pH 6-10.5
-
DELTA154–160
-
mutation increases cyclization activity around 1.5times without any significant reduction of coupling and hydrolyzing activities, conversion yield into cyclodextrins is 39% higher than that of wild-type enzyme without any recognizable change in cyclodextrin ratio. pH-Stability decreases drastically in acidic pH region. Decrease in thermal stability
Y96M
-
mutation increases cyclization activity around 1.5times without any significant reduction of coupling and hydrolyzing activities, conversion yield into cyclodextrins is 28.6% higher than that of wild-type enzyme without any recognizable change in cyclodextrin ratio. Decrease in thermal stability
F283L
H233Y
the mutant primarily produces maltoheptaose using beta-cyclodextrin via a hydrolysis reaction. The mutant enzyme also shows hydrolyzing activity against gamma-cyclodextrin but is unable to catalyze the hydrolysis of alpha-cyclodextrin
N132R
-
introduction of an ionic interaction at the first Ca2+ site, disruption of catalytic activity
N28R
-
introduction of an additional ionic interaction at the second Ca2+ site, mutant displays increased cyclization activity
S182E
-
mutation adjacent to the first Ca2+ site and the active site cleft. Mutant shows enhanced thermostability, and decreased catalytic activity
S182G
-
mutation adjacent to the first Ca2+ site and the active site cleft. Increase in half-life at 60°C to 94 min
Y195I
-
the mutant produces less alpha-cyclodextrin, slightly more beta-cyclodextrin, and 3-4times more gamma-cyclodextrin than the wild type enzyme
Y195L
-
strain 1011; strain 1011, CGTase, in which Tyr-195 is replaced by a leucine residue, main initial product changed to gamma-cyclodextrin, absolute production being much larger than that of the wild-type
Y93F
-
the substitution causes no alpha-cyclodextrin formation, but produces 6% more beta-cyclodextrin, 16% less gamma-cyclodextrin, and decreases its kcat and kcat/Km values
F283L
-
starch degrading activity is similar to that of wild-type enzyme between the acidic and neutral pH ranges but decreases to 10% at pH 10.0. The pH-value of half-maximal activity at basic pH side is shifted to 8.6 from 10.0 of the wild-type. 23%-67% decrease in KM-value for 3-ketobutylidene-beta-2-chloro-4-nitrophenylmalto-pentaoside in the disproportionation reaction. The turnover-number for the disproportionating reaction at various pH conditions decreases to 1.6% to 4.4% compared with those of wild-type enzyme
-
Y195L
-
strain 1011; strain 1011, CGTase, in which Tyr-195 is replaced by a leucine residue, main initial product changed to gamma-cyclodextrin, absolute production being much larger than that of the wild-type
-
Y195L
Bacillus sp. 17. Jan
-
strain 1011; strain 1011, CGTase, in which Tyr-195 is replaced by a leucine residue, main initial product changed to gamma-cyclodextrin, absolute production being much larger than that of the wild-type
-
Y195I
Bacillus sp. 602-1
-
the mutant produces less alpha-cyclodextrin, slightly more beta-cyclodextrin, and 3-4times more gamma-cyclodextrin than the wild type enzyme
-
Y93F
Bacillus sp. A2-5a
-
the substitution causes no alpha-cyclodextrin formation, but produces 6% more beta-cyclodextrin, 16% less gamma-cyclodextrin, and decreases its kcat and kcat/Km values
-
Y195L
-
strain 1011; strain 1011, CGTase, in which Tyr-195 is replaced by a leucine residue, main initial product changed to gamma-cyclodextrin, absolute production being much larger than that of the wild-type
-
N132R
-
introduction of an ionic interaction at the first Ca2+ site, disruption of catalytic activity
-
N28R
-
introduction of an additional ionic interaction at the second Ca2+ site, mutant displays increased cyclization activity
-
S182E
-
mutation adjacent to the first Ca2+ site and the active site cleft. Mutant shows enhanced thermostability, and decreased catalytic activity
-
S182G
-
mutation adjacent to the first Ca2+ site and the active site cleft. Increase in half-life at 60°C to 94 min
-
F191Y
D372K
-
site-directed mutagenesis, the mutant shows a great shift in substrate specificity towards the production of alpha-cyclodextrin
D372K/Y89R
-
site-directed mutagenesis, the mutant enzyme shows a 1.5fold increase in the production of alpha-cyclodextrin, with a concomitant 43% decrease in the production of beta-cyclodextrin compared to the wild-type CGTase
K47F
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, 30% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
K47H
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47L
K47R
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47S
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47T
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47V
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, 48% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
K47W
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, 24% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
Q265K
-
the mutant shows 15% cyclization (alpha-cyclodextrin-forming) and 236% hydrolysis (starch-degrading) activities compared to the wild type enzyme; the mutant with enhanced maltodextrin specificity produces higher 2-O-D-glucopyranosyl-L-ascorbic acid yields than the wild type enzyme. Compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
Q265K/Y195S
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 226% hydrolysis (starch-degrading) activities compared to the wild type enzyme
R146A/D147P
-
the double mutant exhibits a ratio of alpha-cyclodextrin to total cyclodextrin production of 75.1%, approximately one-fifth greater than that of the wild-type enzyme (63.2%), without loss of thermostability
R146P/D147A
-
the double mutant exhibits a ratio of alpha-cyclodextrin to total cyclodextrin production of 76.1%, approximately one-fifth greater than that of the wild-type enzyme (63.2%), without loss of thermostability
Y167H
Y195I
-
the mutation drastically alters the cyclodextrin specificity of the enzyme by switching toward the synthesis of both beta- and gamma-cyclodextrins
Y195S
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 200% hydrolysis (starch-degrading) activities compared to the wild type enzyme; the mutant with enhanced maltodextrin specificity produces higher 2-O-D-glucopyranosyl-L-ascorbic acid yields than the wild type enzyme. Compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
Y195S/Q265K
-
compared with the wild type enzyme, the mutant has no cyclization activity and 498% hydrolysis and disproportionation activity
Y195S/Y260R
-
compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
Y260R
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 226% hydrolysis (starch-degrading) activities compared to the wild type enzyme; the mutant with enhanced maltodextrin specificity produces higher 2-O-D-glucopyranosyl-L-ascorbic acid yields than the wild type enzyme. Compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
Y260R/Q265K
-
compared with the wild type enzyme, the mutant has 8% cyclization activity and 213% hydrolysis activity
Y260R/Q265K/Y195S
-
the mutant shows 12% cyclization (alpha-cyclodextrin-forming) and 557% hydrolysis (starch-degrading) activities compared to the wild type enzyme
Y260R/Y195S
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 492% hydrolysis (starch-degrading) activities compared to the wild type enzyme
Y89D
-
site-directed mutagenesis, the mutant shows a shift in substrate specificity towards the production of alpha-cyclodextrin
Y89K
-
site-directed mutagenesis, the mutant shows a shift in substrate specificity towards the production of alpha-cyclodextrin
Y89N
-
site-directed mutagenesis, the mutant shows a shift in substrate specificity towards the production of alpha-cyclodextrin
Y89R
-
site-directed mutagenesis, the mutant shows a great shift in substrate specificity towards the production of alpha-cyclodextrin
Y167H
-
the mutant shows enhanced alpha-cyclodextrin specificity; the mutations increases the alpha:beta ratio in cyclodextrin product mixture from 3.4 to 7.8 in comparison with the wild type enzyme
-
Y195I
-
the mutation drastically alters the cyclodextrin specificity of the enzyme by switching toward the synthesis of both beta- and gamma-cyclodextrins
-
K47H
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
K47L
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
K47R
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
K47S
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
K47T
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
Q265K
-
the mutant shows 15% cyclization (alpha-cyclodextrin-forming) and 236% hydrolysis (starch-degrading) activities compared to the wild type enzyme
-
Y195S
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 200% hydrolysis (starch-degrading) activities compared to the wild type enzyme; the mutant with enhanced maltodextrin specificity produces higher 2-O-D-glucopyranosyl-L-ascorbic acid yields than the wild type enzyme. Compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
-
Y260R
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 226% hydrolysis (starch-degrading) activities compared to the wild type enzyme; the mutant with enhanced maltodextrin specificity produces higher 2-O-D-glucopyranosyl-L-ascorbic acid yields than the wild type enzyme. Compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
-
synthesis
-
immobilization of enzyme on mesoporous silica microspheres produces high yields of immobilization, up to 83%, and activity recoveries, up to 73%. The soluble enzyme and its immobilized form show similar values for the optimal pH activity, while optimal reaction temperatures are 100°C and 80°C, respectively. The immobilized enzyme shows similar values for Km and thermal stabilities as the soluble form, while its Vmax is lower. The immobilized enzyme was tested in repeated batches in order to simulate recovery and reuse, keeping about 60% of the initial catalytic activity after 15 cycles
S77P
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, molecular modelling of the location and effect of S77P mutation on the Tabium CGTase active-site conformation
W239L
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
W239R
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
S77P
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, molecular modelling of the location and effect of S77P mutation on the Tabium CGTase active-site conformation
-
W239L
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
-
W239R
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
-
additional information
D577K
-
the mutation significantly changes the contribution of Ca2+ to the enzyme's thermostability
D577K
-
the mutant displays a 1.5% increase in the beta-cyclization activity compared to the wild type enzyme
F283L
-
starch degrading activity is similar to that of wild-type enzyme between the acidic and neutral pH ranges but decreases to 10% at pH 10.0. The pH-value of half-maximal activity at basic pH side is shifted to 8.6 from 10.0 of the wild-type. 23%-67% decrease in KM-value for 3-ketobutylidene-beta-2-chloro-4-nitrophenylmalto-pentaoside in the disproportionation reaction. The turnover-number for the disproportionating reaction at various pH conditions decreases to 1.6% to 4.4% compared with those of wild-type enzyme
K47L
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47L
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, highest titer of product among the mutants tested, 57% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
Y167H
-
the mutations increases the alpha:beta ratio in cyclodextrin product mixture from 3.4 to 7.8 in comparison with the wild type enzyme
additional information
construction of chimeric cyclodextrin glucanotransferases from Bacillus circulans A11 and Paenibacillus macerans IAM1243 and analysis of their product specificity
additional information
error-prone PCR mutagenesis for searching the sequence space of CGTase for acarbose-insensitive variants, overview
additional information
-
position 179 is involved in enzyme product specificity and must be occupied by Gly or by amino acid residues able to interact with the substrate through hydrogen bonds in a way that the cyclization process occurs efficiently
additional information
-
error-prone PCR mutagenesis for searching the sequence space of CGTase for acarbose-insensitive variants, overview
-
additional information
-
construction of chimeric cyclodextrin glucanotransferases from Bacillus circulans A11 and Paenibacillus macerans IAM1243 and analysis of their product specificity
-
additional information
-
position 179 is involved in enzyme product specificity and must be occupied by Gly or by amino acid residues able to interact with the substrate through hydrogen bonds in a way that the cyclization process occurs efficiently
-
additional information
-
2fold enhancement and optimization of cyclodextrin production by the enzyme in a membrane process, development of a process for simultaneous production and isolation of beta-cyclodextrin in the presence of complexing agents, e.g. trichloroethylene or toluene, overview
additional information
-
immobilization of the enzyme by three different techniques: on two types of polysulfone membranes; entrapped in agar-gel beads containing magnetite, and by nano-particles of silanized magnetite covalently bound on the cell surface. The enzyme immobilized on membrane shows highest enzyme activity and high stability, overview
additional information
-
enzyme production, method optimization by usage of fed-batch fermentation, CGTase activity and cell density are increased 360% and 510%, respectively, compared to those values achieved with batch fermentation, overview
additional information
-
replacement of B domain by corresponding domain from Thermococcus kodakarensis, Anaerobacter gottschalkii and Pyrococcus furiosus leads to complete loss of catalytic function. Replacement of B domain by corresponding domain from Bacillus stearothermophilus ET1 enzyme leads to a mutant protein with retained activity. The mutant has the wild-type temperature optimum of 60°C with increase in half-life to 57 min. Introduction of mutation F188Y to the mutant results in a half-life of 28 min at 60°C. Bith mutant strains display improved ability to form cyclodextrin and a faster turnover rate
additional information
-
replacement of B domain by corresponding domain from Thermococcus kodakarensis, Anaerobacter gottschalkii and Pyrococcus furiosus leads to complete loss of catalytic function. Replacement of B domain by corresponding domain from Bacillus stearothermophilus ET1 enzyme leads to a mutant protein with retained activity. The mutant has the wild-type temperature optimum of 60°C with increase in half-life to 57 min. Introduction of mutation F188Y to the mutant results in a half-life of 28 min at 60°C. Bith mutant strains display improved ability to form cyclodextrin and a faster turnover rate
-
additional information
construction of chimeric cyclodextrin glucanotransferases from Bacillus circulans A11 and Paenibacillus macerans IAM1243 and analysis of their product specificity
additional information
-
method development for production of alpha-, beta-, and gamma-cyclodextrins from soluble starch by Bacillus macerans Lys10-tagged cyclodextrin glycosyltransferase using a reactor with installed ultrafiltration membrane and immobilized enzyme in a repeated-batch process, overview
additional information
-
generation of a modified enzyme with increased alpha-cyclization specificity by mutations of Asp372 and Tyr89 at subsite -3 in the CGTase, obverview
additional information
-
construction of chimeric cyclodextrin glucanotransferases from Bacillus circulans A11 and Paenibacillus macerans IAM1243 and analysis of their product specificity
-
additional information
-
molecular imprinting of the CGTase with cyclomaltododecaose, CD12, as the template molecule followed by cross-linking of the derivatized protein stabilizes the enzyme, overview
additional information
-
expression of cyclodextrin glycosyltransferase gene fused with thioredoxin, hexa-histidine and S-protein at the N-terminus and a proline-rich peptide at the C-terminus, in Escherichia coli. The maximum specific activity for enzyme is 2.7fold higher than that of the non-fusion form, leading to a specific activity of 2268 units/mg protein at a 61% yield. The fusion enzyme is superior than its wild-type counterpart in terms of stability against high temperature and organic solvents. The fusion enzyme catalyzes the synthesis of cyclodextrins in 20% v/v dimethylformamide with a higher product yield of cyclodextrins CD7 and CD8 compared to that of the wild-type enzyme in the same buffer-solvent system
additional information
-
expression of cyclodextrin glycosyltransferase gene fused with thioredoxin, hexa-histidine and S-protein at the N-terminus and a proline-rich peptide at the C-terminus, in Escherichia coli. The maximum specific activity for enzyme is 2.7fold higher than that of the non-fusion form, leading to a specific activity of 2268 units/mg protein at a 61% yield. The fusion enzyme is superior than its wild-type counterpart in terms of stability against high temperature and organic solvents. The fusion enzyme catalyzes the synthesis of cyclodextrins in 20% v/v dimethylformamide with a higher product yield of cyclodextrins CD7 and CD8 compared to that of the wild-type enzyme in the same buffer-solvent system; molecular imprinting of the CGTase with cyclomaltododecaose, CD12, as the template molecule followed by cross-linking of the derivatized protein stabilizes the enzyme, overview
-
additional information
-
engineering of yeast cells to display the enzyme on the cell surface with reduced cyclodextrin formation activity and enhanced hydrolysis activity towards starch, integration of deltaCGTase into the chromosome, overview, optimzation of starch hydrolysis by the recombinant enzyme for for enhancing of bread-baking process, overview
additional information
-
immobilization of the heat stable enzyme using different supports and immobilization methods, encapsulation of the enzyme in a sol-gel matrix, effects on activity recovery, method optimizations, overview
additional information
-
engineering cyclodextrin glycosyltransferase into a starch hydrolase with a high exospecificity. the cyclodextrin product specificity can be changed into linear product specificity, by introducing a five-residue insertion mutation at the donor substrate binding subsites. The CGTase mutants remain clearly different from the maltogenic alpha-amylase, as they have much lower hydrolytic activities, they form linear products of variable sizes and they retain a low cyclodextrin forming activity, whereas maltogenic alpha-amylases produce primarily maltose. The five-residue insertion, concomitantly, strongly enhances the exo-specificity of CGTase
additional information
-
mutations in two residues, Ser-77 and Trp-239, on the outer region of the active site, lowers the hydrolytic activity up to 15fold with retention of cyclization activity
additional information
-
mutations in two residues, Ser-77 and Trp-239, on the outer region of the active site, lowers the hydrolytic activity up to 15fold with retention of cyclization activity
-
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant CGTase from inclusion bodies by solubilization in 6 M urea, refolded by dialysis and heated to 80°C for 20 min
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
food industry
industry
nutrition
pharmacology
synthesis
food industry
the enzyme can be used in the bread-baking process since its addition in the dough mix improved significantly the loaf volume and decreased the firmness of bread during storage
food industry
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the enzyme improves the sweetness and edulcorant quality of stevioside
food industry
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the enzyme can be used in the bread-baking process since its addition in the dough mix improved significantly the loaf volume and decreased the firmness of bread during storage
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food industry
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the enzyme improves the sweetness and edulcorant quality of stevioside
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
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nutrition
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important enzyme in food industry
nutrition
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used for producing linear oligosaccharides, serving as sweeteners
nutrition
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used for producing linear oligosaccharides, serving as sweeteners
nutrition
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used for producing linear oligosaccharides, serving as sweeteners
nutrition
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used for producing linear oligosaccharides, serving as sweeteners
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
nutrition
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used for producing linear oligosaccharides, serving as sweeteners
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
nutrition
-
application as antistaling agent, retards the deterioration process in bread
nutrition
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important enzyme in food industry
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
important enzyme in food industry; important enzyme in food industry; important enzyme in food industry
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nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
application as antistaling agent, retards the deterioration process in bread
-
nutrition
-
application as antistaling agent, retards the deterioration process in bread; important enzyme in food industry
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
important enzyme in food industry; important enzyme in food industry
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nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
-
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
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pharmacology
-
important enzyme in pharmaceutical industry
pharmacology
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important enzyme in pharmaceutical industry
pharmacology
-
important enzyme in pharmaceutical industry
pharmacology
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important enzyme in pharmaceutical industry; important enzyme in pharmaceutical industry; important enzyme in pharmaceutical industry
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pharmacology
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important enzyme in pharmaceutical industry; important enzyme in pharmaceutical industry
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synthesis
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application of immobilized enzyme is practically important for continous production of cyclodextrins, broad activity maximum is advantageous for industrial operations, immobilized enzyme is able to work at maximum efficiency at lower temperatures
synthesis
-
ATCC 21783, enzyme is becoming commercially important since cyclodextrins have found various practical applications
synthesis
-
industrial strain E 192, industrial production of cyclodextrins
synthesis
-
enzymatic synthesis of glycosides such as maltooligosyl sucrose, glycosyl stevioside and glycosyl ascorbic acid
synthesis
-
strain 1011, Y195L and Y195V CGTases acquired better characteristics for industrial use
synthesis
thermostable, useful for industrial utilization
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
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constructing proteins having new properties of industrial importance
synthesis
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constructing proteins having new properties of industrial importance
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
enzymatic synthesis of salicin prodrugs by the reaction of cyclomaltodextrin glucanyltransferase from Bacillus macerans with cyclomaltohexaose and salicyl alcohol which gives a salicin as a major product and the reaction of Leuconostoc mesenteroides B-742CB dextransucrase with sucrose and salicyl alcohol which gives a isosalicin as the major product
synthesis
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production of alpha-cyclodextrin. Cyclodextrins serve as molecular hosts, are used in the food industry for capturing and retaining flavors and are also used in the formulation of pharmaceuticals.
synthesis
-
potential industrial application of this CGTase in processes in which thermal stability is required. This enzyme could be used after starch gelatinization without cooling the solution to temperatures lower than 60°C
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
-
synthesis of cyclodextrins with multiple applications in the food, pharmaceutical, cosmetic, agricultural and chemical industries. Conditions used to produce cyclodextrins with cyclodextrin glycosyltransferase from Bacillus circulans DF 9R are optimized using experimental designs
synthesis
-
the CGTase-glyoxyl derivative allow the production of cyclodextrin at 85°C, giving twice the production rate compared to the free enzyme, 17.5% higher mass selectivity for beta-cyclodextrin and may help avoid microbial contamination. These characteristics are important considerations for the development of an industrial CD production continuous process
synthesis
the enzyme is of interest for industrial cyclodextrin production
synthesis
-
the enzyme is useful for production of alpha-, beta-, and gamma-cyclodextrins from soluble starch
synthesis
-
the enzyme is used for cyclodextrin production, generation of a modified enzyme with increased alpha-cyclization specificity, overview
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
synthesis
-
the enzyme as membrane biocatalyst is applied for a direct cyclodextrin production
synthesis
-
CGTase is an important industrial enzyme, unique in its capacity to convert starch and related substrates into cyclodextrins through cyclization, an intramolecular transglycosylation reaction
synthesis
-
efficient synthesis of a long carbohydrate chain alkyl glycoside catalyzed by CGTase, the equilibrium lays to 80% on the side of dodecyl-beta-D-maltooctaoside production when the enzyme from Bacillus macerans is used as biocatalyst, method evaluation, overview
synthesis
-
synthesis of a long carbohydrate chain alkyl glycoside catalyzed by CGTase, the equilibrium lays to 80% on the side of dodecyl-beta-D-maltooctaoside production when the enzyme from Bacillus macerans is used as biocatalyst, method evaluation, overview
synthesis
CGTases is used to catalyze cyclomaltooligosaccharides/cyclodextrins production in important industrial processes
synthesis
-
manipulation of the enzyme by molecular imprinting to preferentially produce large-ring cyclodextrins, overview
synthesis
-
enzyme achieves 50.7% conversion of raw corn starch into 81.6% beta- and 18.4% gamma-cyclodextrins after 24 h enzyme reaction at 60°C and pH 8.0
synthesis
-
enzyme achieves 47% conversion of an insoluble raw commercial corn starch into cyclodextrins with production of only beta- and gamma-cyclodextrins, in a ratio of 80%:20% in alkaline pH 9.0
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
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cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
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synthesis
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constructing proteins having new properties of industrial importance
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synthesis
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constructing proteins having new properties of industrial importance
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synthesis
Bacillus autolyticus 11149
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used in industrial applications
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synthesis
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the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
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synthesis
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; industrial strain E 192, industrial production of cyclodextrins; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
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synthesis
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the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
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synthesis
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constructing proteins having new properties of industrial importance
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synthesis
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CGTases is used to catalyze cyclomaltooligosaccharides/cyclodextrins production in important industrial processes; synthesis of cyclodextrins with multiple applications in the food, pharmaceutical, cosmetic, agricultural and chemical industries. Conditions used to produce cyclodextrins with cyclodextrin glycosyltransferase from Bacillus circulans DF 9R are optimized using experimental designs
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synthesis
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industrial strain E 192, industrial production of cyclodextrins
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synthesis
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cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
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cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
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synthesis
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constructing proteins having new properties of industrial importance
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synthesis
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the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
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synthesis
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constructing proteins having new properties of industrial importance
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synthesis
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constructing proteins having new properties of industrial importance
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synthesis
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enzyme achieves 47% conversion of an insoluble raw commercial corn starch into cyclodextrins with production of only beta- and gamma-cyclodextrins, in a ratio of 80%:20% in alkaline pH 9.0
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synthesis
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enzyme achieves 50.7% conversion of raw corn starch into 81.6% beta- and 18.4% gamma-cyclodextrins after 24 h enzyme reaction at 60°C and pH 8.0
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synthesis
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strain 1011, Y195L and Y195V CGTases acquired better characteristics for industrial use; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
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synthesis
Bacillus sp. 1018
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the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
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synthesis
Bacillus sp. 17.1
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the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
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synthesis
Bacillus sp. 17. Jan
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strain 1011, Y195L and Y195V CGTases acquired better characteristics for industrial use
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synthesis
Bacillus sp. 38.2
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the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
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synthesis
Bacillus sp. 6.6.3
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the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
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synthesis
Bacillus sp. A2-5a
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the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
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synthesis
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cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst; strain 1011, Y195L and Y195V CGTases acquired better characteristics for industrial use
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst; the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
constructing proteins having new properties of industrial importance
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
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synthesis
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enzymatic synthesis of glycosides such as maltooligosyl sucrose, glycosyl stevioside and glycosyl ascorbic acid
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synthesis
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the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst; potential industrial application of this CGTase in processes in which thermal stability is required. This enzyme could be used after starch gelatinization without cooling the solution to temperatures lower than 60°C
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synthesis
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cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
constructing proteins having new properties of industrial importance
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
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synthesis
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manipulation of the enzyme by molecular imprinting to preferentially produce large-ring cyclodextrins, overview
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synthesis
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constructing proteins having new properties of industrial importance
-
synthesis
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constructing proteins having new properties of industrial importance
-
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
-
synthesis
-
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
-
LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.19)
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