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Enzyme Nomenclature
Information on EC 3.2.1.11 - dextranase
for references in articles please use BRENDA:EC3.2.1.11
Word Map on EC 3.2.1.11
- 3.2.1.11
- dextrans
- streptococcus
- glucans
-
dental
- plaque
- penicillium
- caries
- sobrinus
- dextransucrase
- leuconostoc
-
water-insoluble
-
cariogenic
- mesenteroides
- isomaltose
- sanguis
- funiculosum
-
colon-specific
- minioluteum
- downei
-
glucosyltransferases
- medicine
- salivarius
- starkeyi
- mutanase
- synthesis
- lipomyces
-
ingbritt
-
sucrose-dependent
- isomaltotriose
- biotechnology
- drug development
- degradation
-
glucan-binding
- agriculture
- chaetomium
- nutrition
- food industry
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
3.2.1.11
-
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RECOMMENDED NAME
GeneOntology No.
dextranase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in dextran
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
6-alpha-D-glucan 6-glucanohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9025-70-1
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
aerobic bacterium SRI 2125
commentary isolated from the hot environs of a raw sugar factory
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-
aerobic bacterium SRI 2126
commentary isolated from the hot environs of a raw sugar factory
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-
aerobic bacterium SRI 2128
commentary isolated from the hot environs of a raw sugar factory
-
-
aerobic bacterium SRI 2140
commentary isolated from the hot environs of a raw sugar factory
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-
anaerobic thermophilic bacterium AB11A
gram-negative, thermophilic, anaerobic, isolated from the non-volcanic low-temperature field, the Great Artesian Basin in Queensland
-
-
Chaetomium erraticum
isolated from sugar-cane farm soil, gene aodex
UniProt
Streptococcus mutans Ingbritt
strain MT8148, serotype c, and strain MT8148, serotype f
SwissProt
strain SL1, serotype d, and strain 6715DP, serotype g
SwissProt
isolated from an active volcanic zone high-temperature field at the biothermal springs at Rotoruna, New Zealand
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-
isolated from an active volcanic zone high-temperature field at the biothermal springs at Rotoruna, New Zealand
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
dextranase hydrolyzes the alpha-1,6 glucosidic bond of dextran to release isomaltooligosaccharides, as endo-dextranase, produced by various microorganisms including bacteria, yeast, and fungi
physiological function
-
dextranase hydrolyzes the alpha-1,6 glucosidic bond of dextran to release isomaltooligosaccharides, as endo-dextranase, produced by various microorganisms including bacteria, yeast, and fungi
-
additional information
N-terminal variable region and C-terminal variable region of the enzyme are not essentially required for catalytic activity, but induce hindered substrate binding to the active site
additional information
-
N-terminal variable region and C-terminal variable region of the enzyme are not essentially required for catalytic activity, but induce hindered substrate binding to the active site
-
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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
(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-sindacene-3-propionic acid, succinimidyl ester)-quenched dextran + H2O
?
dextran + H2O
D-glucose + isomaltose + isomalto-oligosaccharides
-
-
-
-
?
dextran + H2O
isomaltotetraose
-
-
plus small amounts of cycloisomaltooligosaccharides with a degree of polymerization of 7–14
-
?
dextran + H2O
isomaltotetraose + cycloisomaltooligosaccharides
-
main products are isomaltotetraose and small amounts of cycloisomaltooligosaccharides with a degree of polymerization of 7-14
-
?
dextran T2000 + H2O
isomaltotriose + isomaltotetraose + isomaltopentaose
-
-
main end-products
-
?
dextran T40 + H2O
isomaltose + isomaltotriose
88% activity compared to dextran T70
-
-
?
dextran T500 + H2O
isomaltose + isomaltotriose
96% activity compared to dextran T70
-
-
?
dextran T70 + H2O
isomaltose + isomaltotriose
100% activity
-
-
?
glucan + H2O
D-glucose + isomaltose + isomaltotriose + ?
-
from Streptococcus sobrinus K1-R
-
-
?
(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-sindacene-3-propionic acid, succinimidyl ester)-quenched dextran + H2O
?
-
-
-
?
(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-sindacene-3-propionic acid, succinimidyl ester)-quenched dextran + H2O
?
-
-
-
?
alternan + H2O
?
15% activity compared to dextran T70
-
-
?
alternan + H2O
?
15% activity compared to dextran T70
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
-
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Q8VLP4
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Q8VLP4
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
-
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
-
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
blue-dextran + H2O
?
Asp-453 and Trp-793 residues are critical for enzyme activity
-
-
?
dextran + H2O
?
-
extent of hydrolysis of 5-aminosalicylic acid-dextran conjugates (secondary amines) by dextranase is in part controlled by the degree of oxidation and by the amount of conjugated 5-aminosalicylic acid. Less oxidised dextrans (12%) conjugating proportionally less 5-aminosalicylic acid are successfully hydrolysed by dextranase
-
-
?
dextran + H2O
?
-
extent of hydrolysis of 5-aminosalicylic acid-dextran conjugates (secondary amines) by dextranase is in part controlled by the degree of oxidation and by the amount of conjugated 5-aminosalicylic acid. Less oxidised dextrans (12%) conjugating proportionally less 5-aminosalicylic acid are successfully hydrolysed by dextranase
-
-
?
dextran + H2O
?
-
substrate dextran T-20 98.9%, dextran 20000 91.3%, dextran T-70 98.3%, dextran T-500 85.1%, dextran T-2000 86.7% relative activity, respectively
-
-
?
dextran + H2O
?
-
substrate dextran T-20 98.9%, dextran 20000 91.3%, dextran T-70 98.3%, dextran T-500 85.1%, dextran T-2000 86.7% relative activity, respectively
-
-
?
dextran + H2O
D-glucose + isomaltotriose + isomaltose + isomaltooligosaccharide
-
-
-
-
?
dextran + H2O
D-glucose + isomaltotriose + isomaltose + isomaltooligosaccharide
-
-
-
-
?
dextran + H2O
glucose + maltose + maltotriose + maltotetraose
-
-
final products
-
?
dextran + H2O
glucose + maltose + maltotriose + maltotetraose
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-
final products
-
?
dextran + H2O
isomalto-oligosaccharides
-
dextranase D1
isomaltobiose-isomaltodecaose
-
?
dextran + H2O
isomalto-oligosaccharides
-
dextranase D2
isomaltotetraose-isomaltodecaose
-
?
dextran + H2O
isomalto-oligosaccharides
-
dextranase D1
isomaltobiose-isomaltodecaose
-
?
dextran + H2O
isomalto-oligosaccharides
-
dextranase D2
isomaltotetraose-isomaltodecaose
-
?
dextran + H2O
malto-oligosaccharides
dextran of 5000 Da, 0.5%
-
-
?
dextran + H2O
malto-oligosaccharides
dextran of 5000 Da, 0.5%
-
-
?
dextran + H2O
oligosaccharides
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
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-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
maltose, maltotriose and other maltosaccharides
?
dextran + H2O
oligosaccharides
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
substrates are dextrans of 15-25 kDa and 410 kDa. Ten units of dextranase can reduce dextran content by 67% in 24 h and 56% in 72 h from sugarcane juice of cane variety CoS 86032
-
-
?
dextran + H2O
oligosaccharides
-
substrates are dextrans of 15-25 kDa and 410 kDa. Ten units of dextranase can reduce dextran content by 67% in 24 h and 56% in 72 h from sugarcane juice of cane variety CoS 86032
-
-
?
dextran + H2O
oligosaccharides
-
-
isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran + H2O
oligosaccharides
-
-
isomaltotriose, isomaltose, isomaltotetraose, glucose
?
dextran T10 + H2O
isomaltose + isomaltotriose
73% activity compared to dextran T70
-
-
?
dextran T10 + H2O
isomaltose + isomaltotriose
73% activity compared to dextran T70
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose
96% activity compared to dextran T70, the enzyme activity is very specific for alpha-(1-6)-glucosidic glucan
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose
96% activity compared to dextran T70, the enzyme activity is very specific for alpha-(1-6)-glucosidic glucan
-
-
?
pullulan + H2O
?
4% activity compared to dextran T70
-
-
?
additional information
?
-
no substrates: trehalose, kojibiose, nigerose, maltose, maltotriose, or soluble starch. The enzyme additionally catalyzes disproportionation of isomaltose to form isomaltooligosaccharides
-
-
-
additional information
?
-
-
no substrates: trehalose, kojibiose, nigerose, maltose, maltotriose, or soluble starch. The enzyme additionally catalyzes disproportionation of isomaltose to form isomaltooligosaccharides
-
-
-
additional information
?
-
no substrates: trehalose, kojibiose, nigerose, maltose, maltotriose, or soluble starch. The enzyme additionally catalyzes disproportionation of isomaltose to form isomaltooligosaccharides
-
-
-
additional information
?
-
glycosyl hydrolase family 66 enzymes may be classified into three types: dextranases showing only dextranolytic activity, dextranases catalyzing hydrolysis with low cyclization activity, and cycloisomaltooligosaccharide glucanotransferases showing cycloisomaltooligosaccharide-forming activity with low dextranolytic activity
-
-
-
additional information
?
-
no or very low activity on substrates isomaltose, isomaltotriose, isomaltotetraose
-
-
-
additional information
?
-
glycosyl hydrolase family 66 enzymes may be classified into three types: dextranases showing only dextranolytic activity, dextranases catalyzing hydrolysis with low cyclization activity, and cycloisomaltooligosaccharide glucanotransferases showing cycloisomaltooligosaccharide-forming activity with low dextranolytic activity
-
-
-
additional information
?
-
no or very low activity on substrates isomaltose, isomaltotriose, isomaltotetraose
-
-
-
additional information
?
-
-
dextrans with a maximum degree of oxidation (93%) giving maximum conjugation of 5-aminosalicylic acid are resistant to dextranase hydrolysis
-
-
-
additional information
?
-
-
dextrans with a maximum degree of oxidation (93%) giving maximum conjugation of 5-aminosalicylic acid are resistant to dextranase hydrolysis
-
-
-
additional information
?
-
AODex treatment of stale sugar cane juice results in a yield of square and light-colored sugar crystals
-
-
-
additional information
?
-
-
enzyme hydrolyzed alpha-1,6 glucosidic bonds but not alpha-1,4 glucosidic bonds
-
-
-
additional information
?
-
AODex treatment of stale sugar cane juice results in a yield of square and light-colored sugar crystals
-
-
-
additional information
?
-
-
enzyme hydrolyzed alpha-1,6 glucosidic bonds but not alpha-1,4 glucosidic bonds
-
-
-
additional information
?
-
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
-
additional information
?
-
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
-
additional information
?
-
-
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
-
additional information
?
-
no activity on blue dextran brain heart infusion agar plates
-
-
-
additional information
?
-
no activity on blue dextran brain heart infusion agar plates
-
-
-
additional information
?
-
-
no activity on blue dextran brain heart infusion agar plates
-
-
-
additional information
?
-
no activity on blue dextran brain heart infusion agar plates
-
-
-
additional information
?
-
no activity on blue dextran brain heart infusion agar plates
-
-
-
additional information
?
-
-
no activity on blue dextran brain heart infusion agar plates
-
-
-
additional information
?
-
-
enzyme influences glucan synthesis, linkage remodeling and branching
-
-
-
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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
dextran T40 + H2O
isomaltose + isomaltotriose
A8F6K5
88% activity compared to dextran T70
-
-
?
dextran T500 + H2O
isomaltose + isomaltotriose
A8F6K5
96% activity compared to dextran T70
-
-
?
dextran T70 + H2O
isomaltose + isomaltotriose
A8F6K5
100% activity
-
-
?
alternan + H2O
?
A8F6K5
15% activity compared to dextran T70
-
-
?
alternan + H2O
?
A8F6K5
15% activity compared to dextran T70
-
-
?
dextran T10 + H2O
isomaltose + isomaltotriose
A8F6K5
73% activity compared to dextran T70
-
-
?
dextran T10 + H2O
isomaltose + isomaltotriose
A8F6K5
73% activity compared to dextran T70
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose
A8F6K5
96% activity compared to dextran T70, the enzyme activity is very specific for alpha-(1-6)-glucosidic glucan
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose
A8F6K5
96% activity compared to dextran T70, the enzyme activity is very specific for alpha-(1-6)-glucosidic glucan
-
-
?
pullulan + H2O
?
A8F6K5
4% activity compared to dextran T70
-
-
?
additional information
?
-
A9UKG4
AODex treatment of stale sugar cane juice results in a yield of square and light-colored sugar crystals
-
-
-
additional information
?
-
A9UKG4
AODex treatment of stale sugar cane juice results in a yield of square and light-colored sugar crystals
-
-
-
additional information
?
-
A8F6K5
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
-
additional information
?
-
A8F6K5
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
-
additional information
?
-
-
the enzyme cannot hydrolyze maltose, maltotriose, kojibiose, nigerose, sucrose, methyl alpha-glucoside, trehalose, soluble starch, and panose
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe2+
stimulates activity of the dextransucrase-dextranase fusion protein
K+
Li+
stimulates activity of the dextransucrase-dextranase fusion protein
Mg2+
Ni2+
additional information
K+
stimulates activity of the dextransucrase-dextranase fusion protein
Mg2+
activity increases to 125% in the presence of 1 mM Mg2+
Ni2+
stimulates activity of the dextransucrase-dextranase fusion protein
Ni2+
activity increases to 125% in the presence of 1 mM Ni2+
additional information
-
no effects on enzyme activity by K+, Mg2+, and Ca2+ on both free and immobilized enzymes
additional information
Ca2+, Li+, K+, and Na+ (with chloride) do not show appreciable effects on activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aflatoxin B1
inhibits dextranase activities of CYP3A4-expressing cultures, maximum inhibition of 22% at 2 microg/ml. Only negligibly inhibits strain INVSC1 expressing dextranase
aflatoxin G1
substantially less inhibitory towards dextranase activities of CYP3A4-expressing cultures than aflatoxin B1, showing a maximum inhibition of about 12% at 2 microg/ml, whereas strain INVSC1 expressing dextranase is only marginally inhibited
Na+
-
85% inhibition of the free enzyme, 60% inhibition of the immobilized enzyme
T-2 toxin
100% inhibition at 10 microg/ml of dextranase activities of CYP3A4-expressing cultures and strain INVSC1
Ca2+
-
5 mM, isoform D-I 71% residual activity, isoform D-II 83% residual activity
Cu2+
-
93% inhibition of the free enzyme, 56.5% inhibition of the immobilized enzyme
Fe2+
-
41.5% inhibition of the free enzyme, 18% inhibition of the immobilized enzyme
Fe2+
-
5 mM, isoform D-I 47% residual activity, isoform D-II 38% residual activity
Hg2+
-
complete inhibition of the free enzyme and the immobilized enzyme
Mn2+
-
23% inhibition of the free enzyme, 6% inhibition of the immobilized enzyme
Mn2+
-
5 mM, isoform D-I 67% residual activity, isoform D-II 63% residual activity
Pb2+
-
5 mM, isoform D-I 23% residual activity, isoform D-II 10% residual activity
Zn2+
-
21% inhibition of the free enzyme, 8% inhibition of the immobilized enzyme
additional information
-
not inhibited by Mn2+, Co2+, Zn2+, Ni2+, PCMB and EDTA
-
additional information
Chaetomium erraticum
-
for successful adsorption, enzyme to bentonite ratios greater than 0.4 (w/w) have to be used as lower ratios lead to 90% enzyme inactivation due to bentonite contact
-
additional information
-
not inhibited by dithiothreitol, 2-mercaptoethanol and EDTA
-
additional information
-
stable to Cu2+, Fe3+, Mg2+, Zn2+, EDTA and iodoacetamide
-
additional information
-
not inhibited by Mn2+, Co2+, Al3+, Mg2+ and EDTA
-
additional information
-
degree of enzyme inactivation declines with increasing ratio dextranase per dextranase adsorbate bentonite, at a ratio below 0.5: (w/w) only one half of the initial activity is retained
-
additional information
no significant inhibition of dextranase activities of CYP3A4-expressing cultures and strain INVSC1 at concentrations of 2, 20, 200, and 2000 ng/ml by deoxynivalenol, fumonisin B1, and ochratoxin A
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Chaetomium erraticum
-
bentonite carriers exhibit high monolayer protein and activity loads at pH 4.0 and after pH-shift to 5.4. If dextranase is adsorbed at pH 4.1 and hydroxyapatite is washed several times with buffer at pH 5.4 reveals highest activity yield so far (28%). Other selected carriers used are hydroxyapatite and Streamline DEAE. In general, immobilization yields are low and in case of DEAE the rather high particle size is problematic. Porous Eupergit differs only moderately in activity using low molecular weight substrate, whereas macroporous Eupergit reveals enhanced activity for high molecular weight substrates. Activation of the carbohydrate moiety of dextranase by metaperiodate results in active silica gels, whereas the activation of alginate via Woodward’s reagent K exhibits extremely low activities
-
additional information
-
highest immobilization efficiency at 200 mg Eupergit C with a ratio of activity of immobilized enzyme to the activity of soluble enzyme of 90%, higher amounts of Eupergit C yield lower immobilization efficiency. Immobilization duration increases immobilization efficiency
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.05
Dextran
-
pH not specified in the publication, temperature not specified in the publication
3.2
Dextran
-
isoform D-I, calculated as released reducing sugar, 40°C, pH 5.0
3.3
Dextran
-
isoform D-II, calculated as released reducing sugar, 40°C, pH 5.0
5.9
Dextran
-
isoform D-II, calculated as released reducing sugar, 40°C, pH 4.0
7.1
Dextran
-
isoform D-I, calculated as released reducing sugar, 40°C, pH 6.0
7.14
Dextran
-
isoform D-I, calculated as released reducing sugar, 40°C, pH 4.0
8.3
Dextran
-
isoform D-II, calculated as released reducing sugar, 40°C, pH 3.0
9.1
Dextran
-
isoform D-I, calculated as released reducing sugar, 40°C, pH 3.0; isoform D-II, calculated as released reducing sugar, 40°C, pH 6.0
87.1
Dextran
Chaetomium erraticum
-
ultrasound/microwave irradiation shock treatment, pH 5.4, 40°C
0.0095
dextran T2000
in 40 mM sodium acetate buffer (pH4.3) at 55°C
-
additional information
Dextran
KF241867
Km value of native enzyme, 4.38 mg/ml, of immobilzed enzyme, 9.92 mg/ml, respectively, pH 7.0, 50°C
additional information
Dextran
Km value 0.374 mg/ml, p-h 4.5, 37°C
additional information
dextran 742CB
-
Km value is 2.9 mg/ml, pH 5.2, 70°C
-
additional information
dextran T2000
-
Km value is 6.4 mg/ml, pH 5.2, 70°C
-
additional information
dextran T500
-
Km value is 2.5 mg/ml, pH 5.2, 70°C
-
additional information
additional information
-
0.06 microgram/ml, dextran
-
additional information
additional information
-
0.26 g/l, dextran
-
additional information
additional information
Chaetomium erraticum
-
KM-values of soluble and adsorbed enzymes do not differ significantly
-
additional information
additional information
-
0.9 g (500 kDa dextran) per l; 1.3 g (500 kDa dextran) per l
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.7
Dextran
Chaetomium erraticum
-
ultrasound/microwave irradiation shock treatment, pH 5.4, 40°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
76.78
Dextran
Chaetomium erraticum
-
ultrasound/microwave irradiation shock treatment, pH 5.4, 40°C
additional information
dextran 742CB
-
Km value is 1.25ml per mg and s, pH 5.2, 70°C
-
additional information
dextran T2000
-
kcat_/Km value is 5.9 ml per mg and s, pH 5.2, 70°C
-
additional information
dextran T500
-
Km value is 3.3 ml per mg and s, pH 5.2, 70°C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.02
purified recombinant enzyme SmDex95, the 95 kDa variant, pH 5.0, temperature not specified in the publication
8.21
purified recombinant enzyme SmDex90, the 90 kDa variant, pH 5.0, temperature not specified in the publication
11.9
additional information
additional information
Chaetomium erraticum
-
6356.3 dextranase units/mg, one unitis the amount of enzyme that degrades dextran to produce reducing sugar equivalent to 1 mg maltose per h per g at 40°C and pH 5.4
additional information
-
60603.3 dextranase units/mg, concentrated dextranase 1, one dextranase unit is the amount of enzyme that degrades dextran to produce reducing sugar equivalent to 1 mg maltose per h per g at 40°C and pH 5.4; 8290.8 dextranase units/mg, concentrated dextranase 3, factory 2, amount of enzyme that degrades dextran to produce reducing sugar equivalent to 1 mg maltose per h per g at 40°C and pH 5.4; 8402.8 dextranase units/mg, concentrated dextranase 3, factory 1, amount of enzyme that degrades dextran to produce reducing sugar equivalent to 1 mg maltose per h per g at 40°C and pH 5.4
additional information
-
release of 78.5 mg of Remazol Blue R-250 dye/min at 50°C
additional information
activities of recombinant fusion protein and of wild-type dextranase in fermentation, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6
5.2
5.3
5.4
5.5
5.5
5.5
additional information
-
optimum pH for activity 4.5-5.5 is not affected by immobilization
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
-
approx. 50% of maximal activity at pH 6.3, complete loss of activity above pH 7.5
4 - 8
5 - 5.5
5 - 6.5
5 - 6.4
5.5 - 8.3
70-100% activity at pH 6.0-8.0, 50% activity at pH 5.5 and pH 8.3
5 - 6.4
great loss in activity below and above that values, recombinant wild-type dextranase and engineered fusion protein DSXR
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
35 - 40
-
dex1 from strain Dex40-8 and dex2 from strain Dex50-2,inactive above 50°C
37
40
40 - 45
43.3 - 54.4
45
50
55
60
65
70
additional information
-
ranges for both soluble or immobilized enzyme between 30-35°C
60
Chaetomium erraticum
-
optimum temperature under ultrasound/microwave irradiation shock treatment
60
-
enzyme retains more than 70% maximal activity after incubation at 57°C for 9.5 h in the absence of substrate
60
temperature optima of mutants are similar to that of the wild-type
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 60
over 80% activity retained within the range of 37-50°C, 50% of maximal activity at 25°C and 60°C
25 - 45
-
approx. 50% of maximal activity at 30°C, dramatic decrease in activity above 45°C
30 - 60
-
approx. 35% of maximal activity at 30°C, approx. 10% of maximal activity at 60°C
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pI VALUE
ORGANISM