Information on EC 2.4.1.19 - cyclomaltodextrin glucanotransferase and Organism(s) Paenibacillus macerans and UniProt Accession P31835

alpha-cyclodextrin + D-glucose

beta-cyclodextrin + maltooligosaccharide

-

immobilized enzyme

-

r

alpha-cyclodextrin + genistein

genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside

-

highest activity with alpha-cyclodextrin as glycosyl donor

-

?

alpha-cyclodextrin + glycosyl acceptor

beta-cyclodextrin + maltooligosaccharide

alpha-cyclodextrin + L-ascorbic acid

2-O-alpha-D-glucopyranosyl-L-ascorbic acid

-

highest activity

-

?

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

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 + genistein

genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside

-

-

?

beta-cyclodextrin + glycosyl acceptor

alpha-cyclodextrin + maltooligosaccharide

beta-cyclodextrin + L-ascorbic acid

2-O-alpha-D-glucopyranosyl-L-ascorbic acid

-

9% conversion rate

-

?

beta-cyclodextrin + maltohexaose

alpha-cyclodextrin + maltooligosaccharide

-

immobilized enzyme

-

r

beta-cyclodextrin + maltose

alpha-cyclodextrin + maltooligosaccharide

beta-cyclodextrin + maltotetraose

alpha-cyclodextrin + maltooligosaccharide

-

immobilized enzyme

-

r

beta-cyclodextrin + maltotriose

alpha-cyclodextrin + maltooligosaccharide

-

immobilized enzyme

-

r

beta-cyclodextrin + sucrose

alpha-cyclodextrin + maltooligosaccharide

-

immobilized enzyme

-

r

corn starch + L-ascorbic acid

2-O-alpha-D-glucopyranosyl-L-ascorbic acid

-

-

?

cyclohexaamylose + D-glucose

linear oligosaccharide

-

-

r

cyclohexaamylose + maltose

linear oligosaccharide

-

-

r

cyclohexaamylose + sucrose

linear oligosaccharide

-

-

r

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. 917, decrease, and the small and intermediate sizes, d.p. 28, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 48, decrease, and the small sizes, d.p. 2 and 3 become predominant

-

?

cyclomaltohexaose + methyl beta-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. 917, decrease, and the small and intermediate sizes, d.p. 28, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 48, 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 0.51.0 give a wide range of sizes from d.p. 217 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 917, decrease, and the small and intermediate sizes, d.p. 28, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 48, decrease, and the small sizes, d.p. 2 and 3 become predominant

-

?

cyclomaltohexaose + phenyl beta-D-glucopyranoside

maltodextrin glycoside

-

the reactions are optimized by using different ratios of the D-glucopyranosides to cyclomaltohexaose. The lower ratios of 0.51.0 give a wide range of sizes from d.p. 217 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 917, decrease, and the small and intermediate sizes, d.p. 28, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 48, decrease, and the small sizes, d.p. 2 and 3 become predominant

-

?

dextrin + L-ascorbic acid

2-O-alpha-D-glucopyranosyl-L-ascorbic acid

-

-

?

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

gamma-cyclodextrin + L-ascorbic acid

2-O-alpha-D-glucopyranosyl-L-ascorbic acid

-

-

?

genistein + alpha-cyclodextrin

genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside

-

highest activity with alpha-cyclodextrin as glycosyl donor

-

?

genistein + beta-cyclodextrin

genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside

-

-

?

genistein + D-glucose

genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside

-

very low activity with D-glucose als glysosyl donor

-

?

genistein + maltodextrin

alpha-cyclodextrins

less than 20% conversion ratio

-

?

genistein + maltodextrin

genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside

-

-

?

genistein + maltose

genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside

-

-

?

genistein + starch

genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside

-

-

?

genistein + sucrose

genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside

-

very low activity with sucrose als glysosyl donor

-

?

glycogen + acceptor

beta-cyclodextrin

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 + ?

-

-

?

linear alpha-(1,4)-glucan DP 29 + sucrose

alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin

-

-

?

linear alpha-(1,4)-glucan DP 38 + sucrose

alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin

-

-

?

linear alpha-(1,4)-glucan DP 44 + sucrose

alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin

-

-

?

linear alpha-(1,4)-glucan DP 53,116 + sucrose

alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin

-

-

?

linear alpha-(1,4)-glucan DP 65,166 + sucrose

alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin

-

-

?

maltodextrin + genistein

genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside

-

-

?

maltodextrin + glycosyl acceptor

alpha-cyclodextrin

-

-

?

maltodextrin + L-ascorbic acid

2-O-D-glucopyranosyl-L-ascorbic acid + ?

-

-

?

maltooligosaccharides + glycosyl acceptor

cyclodextrins

maltose + genistein

genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside

-

-

?

maltose + L-ascorbic acid

2-O-alpha-D-glucopyranosyl-L-ascorbic acid

-

-

?

potato starch + L-ascorbic acid

2-O-alpha-D-glucopyranosyl-L-ascorbic acid

-

-

?

rice starch + L-ascorbic acid

2-O-alpha-D-glucopyranosyl-L-ascorbic acid

-

-

?

soluble potato starch + sucrose

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

675462

-

?

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 + cellobiose

?

-

-

r

soluble starch + D-fructose

?

-

-

r

soluble starch + D-galactose

?

soluble starch + D-glucose

cyclodextrins

-

488848, 488849, 488854, 488861

-

?

soluble starch + D-maltose

cyclodextrins

-

488849, 488854, 488861

-

r

soluble starch + D-rhamnose

?

-

-

r

soluble starch + D-sorbose

?

-

488854, 488861

-

r

soluble starch + D-xylose

?

soluble starch + glycosyl acceptor

alpha-cyclodextrin

soluble starch + glycosyl acceptor

alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin

7 entries

soluble starch + glycosyl acceptor

beta-cyclodextrin

5 entries

soluble starch + glycosyl acceptor

cyclodextrin

-

-

?

soluble starch + glycosyl acceptor

cyclodextrins

soluble starch + glycosyl acceptor

cyclohexaamylose

-

-

r

soluble starch + glycosyl acceptor

gamma-cyclodextrin

soluble starch + glycosyl acceptor

Schardinger dextrins

-

488824, 488836

-

r

soluble starch + H2O

cyclodextrins

soluble starch + L-sorbose

?

-

-

r

soluble starch + maltotriose

cyclodextrins

-

-

r

soluble starch + myo-inositol

?

-

-

r

soluble starch + ribose

?

-

-

r

soluble starch + sucrose

?

-

488848, 488854, 488861

-

r

sophoricoside + maltodextrin

Glc-sophoricoside + Glc2-sophoricoside + Glc3-sophoricoside + Glc4-sophoricoside + Glc5-sophoricoside + Glc6-sophoricoside

more than 40% conversion ratio

-

?

starch

cyclodextrin

starch + genistein

genistein monoglucoside + genistein diglucoside + genistein triglucoside + genistein tetraglucoside

-

-

?

starch + glycosyl acceptor

alpha-cyclodextrin

-

736290

-

?

starch + glycosyl acceptor

cyclodextrins

starch + hesperidin

glycosyl hesperidin

-

-

r

starch + salicin

glycosyl salicin

-

-

r

starch + stevioside

glycosyl stevioside

additional information

?

-

18 entries

alpha-1,4-glucan + glycosyl acceptor

cyclodextrins

-

755771

-

?

soluble starch + glycosyl acceptor

cyclodextrins

-

736787

alpha-cyclodextrin is the main product

-

?

soluble starch + glycosyl acceptor

Schardinger dextrins

-

488824, 488836

-

r

starch + glycosyl acceptor

alpha-cyclodextrin

-

736290

-

?

starch + glycosyl acceptor

cyclodextrins

additional information

?

-

Ba2+

-

0.5 mM, 125% of initial activity

Ca2+

6 entries

CaCl2

-

5 mM, 20% activation of cross-linked enzyme crystals, 2% activation of soluble enzyme

Co2+

-

10 mM, 28% inhibition

Cu2+

-

10 mM, 20% inhibition

Fe2+

-

10 mM, 58% inhibition

FeCl2

-

5 mM, 110% activation of cross-linked enzyme crystals, inhibition of soluble enzyme

Hg2+

-

10 mM, complete inhibition

Mg2+

Zn2+

2-propanol

-

alpha-cyclodextrin

-

competitive product inhibition

beta-cyclodextrin

-

product inhibition

chloroform

-

ethanol

-

gamma-cyclodextrin

-

product inhibition

Hg2+

-

1 mM, 5% of initial activity

HgCl2

-

5 mM, 68% inhibition of cross-linked enzyme crystals, 40% of soluble enzyme

methanol

-

MgCl2

-

5 mM, 15% inhibition of cross-linked enzyme crystals, 22% of soluble enzyme

Ni2+

-

1 mM, 58% of initial activity

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

-

not inhibited by L-ascorbic acid

-

bromobenzene

-

increases the yield of beta-cyclodextrin

Ca2+

-

4 mM, 22% activation

cyclohexadec-8-ene-1-one

-

increases the yield of gamma-cyclodextrin

Cyclohexane

cyclotridecanone

-

increases the yield of gamma-cyclodextrin

Decanol

-

increases the yield of alpha-cyclodextrin

EDTA

-

10 mM, 105% of initial activity

ethanol

Isopropanol

-

increases the yield of beta-cyclodextrin

488855, 488861

n-butanol

-

increases the yield of alpha-cyclodextrin

Octanol

-

increases the yield of alpha-cyclodextrin

pentadecane

-

increases the yield of beta-cyclodextrin

Toluene

Trichloroethylene

-

increases the yield of beta-cyclodextrin

488855, 488861

undecane

-

increases the yield of beta-cyclodextrin

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

704134

-

1.26 - 2.32

alpha-cyclodextrin

0.08 - 1.51

beta-cyclodextrin

0.25

gamma-cyclodextrin

-

cyclodextrin opening

25.5 - 51.7

L-ascorbic acid

14 entries

0.47 - 0.64

maltodextrin

13 entries

0.58 - 2.1

starch

additional information

5 entries

-

0.000086 - 0.000133

L-ascorbic acid

8 entries

0.004 - 768

maltodextrin

16 entries

0.063

sophoricoside

0.442 - 1.66

starch

additional information

-

-

0.01255

alpha-cyclodextrin

-

at pH 6.5 and 50°C

0.00034

beta-cyclodextrin

-

at pH 6.5 and 50°C

0.00055

gamma-cyclodextrin

-

at pH 6.5 and 50°C

additional information

-

Ki-value for starch: 0.01 mg/ml (soluble enzyme), 0.0055 mg/ml (enzyme immobilized on alginate)

-

0.01

-

gamma-cyclodextrin, opening

0.02

-

beta-cyclodextrin, opening

1.1

-

gamma-cyclization, wild-type enzyme

1.24

-

gamma-cyclodextrin, opening

1.42

-

alpha-cyclodextrin, opening

1027

-

14.4

-

beta-cyclodextrin-forming activity, recombinant wild-type enzyme

190.4

-

alpha-cyclization, wild-type enzyme

2.4

-

maltotriose, disproportionation

21.7

-

beta-cyclodextrin-forming activity, recombinant mutant K47R

32.2

-

beta-cyclization, wild-type enzyme

35.9

-

beta-cyclodextrin-forming activity, recombinant mutant K47H

37.4

-

alpha-cyclodextrin, coupling

45.9

-

alpha-cyclodextrin-forming activity, recombinant mutant K47L

46.4

-

alpha-cyclodextrin-forming activity, recombinant mutant K47S

47.4

-

alpha-cyclodextrin-forming activity, recombinant mutant K47T

51.4

-

beta-cyclodextrin-forming activity, recombinant mutant K47T

51.5

-

beta-cyclodextrin-forming activity, recombinant mutant K47S

53.1

-

beta-cyclodextrin-forming activity, recombinant mutant K47L

62.9

-

alpha-cyclodextrin-forming activity, recombinant mutant K47H

77.3

-

alpha-cyclodextrin-forming activity, recombinant mutant K47R

81.55

-

488824

85.1

-

alpha-cyclodextrin-forming activity, recombinant wild-type enzyme

additional information

6 entries

5

-

5 - 5.7

5.2

-

assay at

5.4 - 5.8

-

5.5

5.7

recombinant enzyme, cgtM gene product

5.9

-

6

6 - 7

-

for the product of genistein monoglucoside, the enzyme's yield reaches the highest level at pH 6.5, while the most genistein diglucoside is obtained at pH 7.0

6.1 - 6.2

6.5

6.5 - 7

-

for the product of genistein monoglucoside, its yield reaches the highest level at pH 6.5, while the most genistein diglucoside is obtained at pH 7.0

7

7.5

-

additional information

-

the enzymes are more active in glycine/NaOH buffer compared with Na2HPO4/NaH2PO4 buffer at the same pH

4 - 6

-

4 - 8.5

4 - 9.5

-

loss of cyclization activity above and below

5 - 7

-

pH 5.0: about 70% of maximal activity, pH 9.0: about 70% of maximal activity, native enzyme

5 - 8

23

-

assay at

703063

30 - 37

-

36

37

40

40 - 60

-

immobilized enzyme

45

-

recombinant enzyme

50

-

native enzyme

55

60

7 entries

60 - 70

-

cross-linked enzyme crystals

28 - 44

-

30 - 70

40 - 50

-

more than 95% of maximum activity, recombinant enzyme

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

50 - 80

-

-

488863, 671505, 685767, 688329

SwissProt

commercial preparation

-

culture medium

-

674104

extracellular

-

671505

extracellular

-

488827, 488829, 488842, 488855, 673390, 674104, 701863

intracellular

-

5622

488824, 488855

additional information

-

no alpha-CGTase activity in the soluble cytoplasmic fraction, very low activity in the periplasmic fraction

-

701863

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

P31835 pBLAST

CDGT2_PAEMA

713

1

76857

Swiss-Prot

Show Sequence

-

139000

-

ATCC 8514, intracelluar enzyme

139300

-

sedimentation and diffusion data

488824

145000

-

ATCC 8514, extracelluar enzyme

35000

38000

65000

66000

67000

68000

72000

-

1 * 72000, SDS-PAGE

74000

74010

strain IFO3490, amino acid composition deduced from nucleotide sequence

75000

76000

-

x * 76000, about, His-tagged wild-type and mutant enzymes, SDS-PAGE

?

dimer

monomer

additional information

-

-

488828, 488839, 488855

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

S5ZJ19

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

-

A156V

the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme

A156V/A166Y

the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme

A156V/L174P

the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme

A156V/L174P/A166Y

the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme

A166Y

the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme

A166Y/L174P

the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme

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

L174P

the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme

Q265K

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

735512

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

735512

Y167H

Y195I

-

the mutation drastically alters the cyclodextrin specificity of the enzyme by switching toward the synthesis of both beta- and gamma-cyclodextrins

Y195S

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

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

additional information

4 - 10

-

488830

5.5

-

the half-life at pH 5.5 is 29.8 h

735493

6 - 9.5

-

719222

6.5 - 8.5

-

stable at 50°C

488839

8 - 10

-

488825, 488855

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

40

40 - 50

-

immobilized enzyme is stable at 40°C, heat inactivation above 50°C

45

-

half-life about 1.25 h

50

50 - 55

-

thermal stability of immobilized enzyme on chitosan increases from 50°C to 55°C

488840

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

58 - 60

-

undergoes rapid inactivation

60

70

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

-

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 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 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

-

675462

the temperature stability of the immobilized and crosslinked imprinted CGTase at 60°C is considerably higher than that of the native enzyme

-

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

-

stable in presence, but not active, relative residual activity 96%

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

-

relative residual activity 92%

chloroform

-

stable in presence, but not active

cyclohexane

-

relative residual activity 91%

Ethanol

-

stable in presence, but not active, relative residual activity 99%

hexane

-

n-hexane, relative residual activity 90%

Methanol

-

stable in presence, but not active, relative residual activity 98%

p-xylene

-

p-xylene, relative residual activity 100%

toluene

-

relative residual activity 100%

-

-

488824, 488825, 488828, 488829, 488834, 488835, 488839, 488848, 488849, 488852, 488855, 488861, 673390, 674104, 736787

ammonium sulfate precipitation and Ni-NTA agarose column chromatography

-

mutant Y167H with ammonium sulfate precipitation and Ni-NTA agarose column chromatography

S5ZJ19

Ni-NTA agarose column chromatography

Ni-NTA agarose column chromatography and Sephacryl-100 gel filtration

-

recombinant enzyme

-

recombinant enzyme, cgtM gene product

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 and recombinant enzymes

-

488857

-

488863

DNA and amino acid sequence determination and analysis, phylogenetic tree

685767

-

cloned and overexpressed in Bacillus subtilis

-

cloned and overexpressed in Escherichia coli

-

488857

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

-

660447

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

-

673388

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

-

704134

expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)

-

mutant Y167H is expressed in Escherichia coli BL21(DE3) cells

S5ZJ19

mutant Y195I is expressed in Escherichia coli BL21(DE3) cells

-

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

-

701863

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

subcloning in Escherichia coli strain JM109, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)

-

when the enzyme expression is induced at 25°C for 32 h, and then the temperature is shifted to 30°C, the extracellular enzyme activity at 90 h is 45% higher than that observed when induction is performed at a constant temperature of 25°C

-

755771

synthesis

food industry

cyclodextrins are frequently utilized chemical substances in the food, pharmaceutical, cosmetics, and chemical industries. An enzymatic process for cyclodextrin production is developed by utilizing sucrose as raw material instead of corn starch. Cyclodextrin glucanotransferase from Paenibacillus macerans is applied to produce the cyclodextrins from linear alpha-(1,4)-glucans, which are obtained by Neisseria polysaccharea amylosucrase treatment on sucrose. The greatest cyclodextrin yield (21.1%, w/w) is achieved from a one-pot dual enzyme reaction at 40°C for 24 h. The maximum level of cyclodextrin production (15.1 mg/ml) is achieved with 0.5 M sucrose in a simultaneous mode of dual enzyme reaction, whereas the reaction with 0.1 M sucrose is the most efficient with regard to conversion yield. Dual enzyme synthesis of cyclodextrins is successfully carried out with no need of starch material. Efficient bioconversion process that does not require the high temperature necessary for starch liquefaction by thermostable alpha-amylase in conventional industrial processing

industry

nutrition

pharmacology

synthesis

DePinto, J.A.; Campbell, L.L.

Purification and properties of the amylase of Bacillus macerans

Biochemistry

7

114-120

1968

Bacillus subtilis, Paenibacillus macerans, Homo sapiens, Sus scrofa

5758537

Kitahata, S.; Tsuyama, N.; Okada, S.

Purification and some properties of cyclodextrin glycosyltransferase from a strain of Bacillus species

Agric. Biol. Chem.

38

387-393

1974

Paenibacillus macerans, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) 5

-

488826

Nakamura, N.; Horikoshi, K.

Purification and properties of neutral-cyclodextrin glycosyl-transferase of an alkalophilic Bacillus sp.

Agric. Biol. Chem.

40

1785-1791

1976

Geobacillus stearothermophilus, Niallia circulans, Priestia megaterium, Paenibacillus macerans, Bacillus sp. (in: Bacteria)

-

488827

Bender, H.

Cyclodextrin glucanotransferase from Klebsiella pneumoniae. 1. Formation, purification and properties of the enzyme from Klebsiella pneumoniae M 5 al

Arch. Microbiol.

111

271-282

1977

Priestia megaterium, Paenibacillus macerans, Klebsiella oxytoca, Klebsiella pneumoniae, Priestia megaterium No5, Klebsiella pneumoniae M5

319771

488828

Kobayashi, S.; Kainuma, K.; Suzuki, S.

Purification and some properties of Bacillus macerans cycloamylose (cyclodextrin) glucanotransferase

Carbohydr. Res.

61

229-238

1978

Paenibacillus macerans

25712

Stavn, A.; Granum, P.E.

Purification and physiocochemical properties of an extra-cellular cycloamylose (cyclodextrin) glucanotransferase from Bacillus macerans

Carbohydr. Res.

75

243-250

1979

Paenibacillus macerans

39676

Ivony, K.; Szajani, B.; Seres, G.

Immobilization of starch-degrading enzymes. I. A comparative study on soluble and immobilized cyclodextrin glycosyltransferase

J. Appl. Biochem.

5

158-164

1983

Paenibacillus macerans

-

488831

Kato, T.; Horikoshi, K.

Immobilzed cyclomaltodextrin glucanotransferase of an alkalophilic Bacillus sp. No. 38-2

Biotechnol. Bioeng.

26

595-598

1984

Geobacillus stearothermophilus, Niallia circulans, Priestia megaterium, Paenibacillus macerans, Bacillus sp. (in: Bacteria), Klebsiella pneumoniae

18553375

488833

Aoki, H.; Yao, D.; Misawa, M.

Production and characterization of a thermostable bacterial cyclodextrin glycosyltransferase

Prog. Biotechnol.

3

81-93

1987

Geobacillus stearothermophilus, Paenibacillus macerans, Bacillus sp. (in: Bacteria), Klebsiella oxytoca, Bacillus sp. (in: Bacteria) IT25

-

488834

Maekelae, M.; Mattsson, P.; Schinina, M.E.; Korpela, T.

Purification and properties of cyclomaltodextrin glucanotransferase from an alkalophilic Bacillus

Biotechnol. Appl. Biochem.

10

414-427

1988

Niallia circulans, Paenibacillus macerans, Bacillus sp. (in: Bacteria), Klebsiella pneumoniae, Bacillus sp. (in: Bacteria) 1011, Paenibacillus macerans IAM1243

-

488835

Pongsawasdi, P.; Yagisawa, M.

Purification and properties of cyclomaltodextrin glucanotransferase from Bacillus circulans

Agric. Biol. Chem.

52

1099-1103

1988

Niallia circulans, Priestia megaterium, Paenibacillus macerans, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) Ha3-3-2 / ATCC 39612, Niallia circulans C31

-

488836

Fujita, Y.; Tsubouchi, H.; Inagi, Y.; Tomita, K.; Ozaki, A.; Nakanishi, K.

Purification and properties of cyclodextrin glycosyltransferase from Bacillus sp. AL-6

J. Ferment. Bioeng.

70

150-154

1990

Niallia circulans, Priestia megaterium, Bacillus subtilis, Paenibacillus macerans, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) AL-6, Bacillus subtilis 313

-

Akimaru, K.; Yagi, T.; Yamamoto, S.

Purification and properties of Bacillus coagulans cyclomaltodextrin glucanotransferase

J. Ferment. Bioeng.

71

322-328

1991

Geobacillus stearothermophilus, Niallia circulans, Weizmannia coagulans, Priestia megaterium, Bacillus subtilis, Paenibacillus macerans, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Klebsiella oxytoca, Klebsiella pneumoniae, Geobacillus stearothermophilus TC-60, Bacillus subtilis 313

-

488840

Lee, S.H.; Shin, H.D.; Lee, Y.H.

Evaluation of immobilization methods for cyclodextrin glucanotransferase and characterization of its enzymic properties

J. Microbiol. Biotechnol.

1

54-62

1991

Paenibacillus macerans

-

488842

Bovetto, L.J.; Backer, D.P.; Villette, J.R.; Sicard, P.J.; Bouquelet, S.J.L.

Cyclomaltodextrin glucanotransferase from Bacillus circulans E 192. I. Purification and characterization of the enzyme

Biotechnol. Appl. Biochem.

15

48-58

1992

Geobacillus stearothermophilus, Alkalihalobacillus alcalophilus, Niallia circulans, Priestia megaterium, Paenibacillus macerans, Bacillus ohbensis, Klebsiella pneumoniae, Micrococcus sp., Niallia circulans E 192, Niallia circulans 8

1532314

488844

Fujiwara, S.; Kakihara, H.; Sakaguchi, K.; Imanaka, T.

Analysis of mutations in cyclodextrin glucanotransferase from Bacillus stearothermophilus which affect cyclization characteristics and thermostability

J. Bacteriol.

174

7478-7481

1992

Geobacillus stearothermophilus, Niallia circulans, Paenibacillus macerans, Klebsiella oxytoca, Geobacillus stearothermophilus NO2, Geobacillus stearothermophilus TC-91, Niallia circulans 8

1429471

Fujiwara, S.; Kakihara, H.; Woo, K.B.; Lejeune, A.; Kanemoto, M.; Sakaguchi, K.; Imanaka, T.

Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme

Appl. Environ. Microbiol.

58

4016-4025

1992

Bacillus licheniformis, Bacillus sp. (in: Bacteria), Bacillus subtilis, Bacillus subtilis NA-1, Geobacillus stearothermophilus, Geobacillus stearothermophilus (P31797), Geobacillus stearothermophilus NO2, Klebsiella oxytoca, Klebsiella pneumoniae, Niallia circulans, Niallia circulans 8, Paenibacillus macerans, Paenibacillus macerans (P04830), Paenibacillus macerans IAM1243, Priestia megaterium

1476442

488848

Shibuya, T.; Miwa, Y.; Nakano, M.; Yamauchi, T.; Chaen, H.; Sakai, S.; Kurimoto, M.

Enzymatic synthesis of a novel trisaccharide, glucosyl lactoside

Biosci. Biotechnol. Biochem.

57

56-60

1993

Geobacillus stearothermophilus, Niallia circulans, Paenibacillus macerans, Geobacillus stearothermophilus TC-91

7763423

488849

Tomita, K.; Kaneda, M.; Kawamura, K.; Nakanishi, K.

Purification and properties of a cyclodextrin glucanotransferase from Bacillus autolyticus 11149 and selective formation of beta-cyclodextrin

J. Ferment. Bioeng.

75

89-92

1993

Geobacillus stearothermophilus, Bacillus autolyticus, Niallia circulans, Paenibacillus macerans, Bacillus sp. (in: Bacteria), Klebsiella oxytoca, Bacillus sp. (in: Bacteria) AL-6, Bacillus autolyticus 11149

-

488851

Nakamura, A.; Haga, K.; Yamane, K.

Four aromatic residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: effects of replacements on substrate binding and cyclization characteristics

Biochemistry

33

9929-9936

1994

Geobacillus stearothermophilus, Niallia circulans, Bacillus licheniformis, Paenibacillus macerans, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Klebsiella pneumoniae, Bacillus sp. (in: Bacteria) 1011, Bacillus sp. (in: Bacteria) 17-1, Bacillus sp. (in: Bacteria) B1018

8061001

488852

Ferrarotti, S.A.; Rosso, A.M.; Marechal, M.A.; Krymkiewicz, N.; Marechal, L.R.

Isolation of two strains (S-R type) of Bacillus circulans and purification of a cyclomaltodextrin-glucanotransferase

Cell. Mol. Biol.

42

653-657

1996

Geobacillus stearothermophilus, Alkalihalobacillus alcalophilus, Niallia circulans, Weizmannia coagulans, Priestia megaterium, Bacillus subtilis, Lederbergia lentus, Paenibacillus macerans, Bacillus sp. (in: Bacteria), Klebsiella oxytoca, Niallia circulans DF9

8832095

Park, D.C.; Kim, T.K.; Lee, Y.H.

Characteristics of transglycosylation reaction of cyclodextrin glucanotransferase in the heterogeneous enzyme reaction system using extrusion starch as a glucosyl donor

Enzyme Microb. Technol.

22

217-222

1998

Geobacillus stearothermophilus, Priestia megaterium, Paenibacillus macerans, Priestia megaterium No5

-

Tonkova, A.

Bacterial cyclodextrin glucanotransferase

Enzyme Microb. Technol.

22

678-686

1998

Bacillus cereus, Bacillus cereus NCIMB 13123, Bacillus licheniformis, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) 1011, Bacillus sp. (in: Bacteria) AL-6, Bacillus sp. (in: Bacteria) INMIA 1919, Bacillus sp. (in: Bacteria) INMIA A7/1, Bacillus sp. (in: Bacteria) INMIA T4, Bacillus sp. (in: Bacteria) INMIA t6, Geobacillus stearothermophilus, Geobacillus stearothermophilus N2, Klebsiella oxytoca, Klebsiella pneumoniae, Lederbergia lentus, Lysinibacillus sphaericus, Lysinibacillus sphaericus ATCC 7055, Micrococcus luteus, Niallia circulans, Niallia circulans 8, Paenibacillus macerans, Paenibacillus macerans IAM1243, Priestia megaterium, Priestia megaterium No5, Salimicrobium halophilum, Salimicrobium halophilum INMIA-3849, Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes EM1, Weizmannia coagulans

-

488857

Jeang, C.L.; Wung, C.H.; Chang, B.Y.; Yeh, S.S.; Lour, D.W.

Characterization of the Bacillus macerans cyclodextrin glucanotransferase overexpressed in Escherichia coli

Proc. Natl. Sci. Counc. Repub. China B

23

62-68

1999

Paenibacillus macerans

10420654

488858

Tachibana, Y.; Kuramura, A.; Shirasaka, N.; Suzuki, Y.; Yamamoto, T.; Fujiwara, S.; Takagi, M.; Imanaka, T.

Purification and characterization of an extremely thermostable cyclomaltodextrin glucanotransferase from a newly isolated hyperthermophilic archaeon, a Thermococcus sp

Appl. Environ. Microbiol.

65

1991-1997

1999

Bacillus licheniformis (P14014), Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) (P31746), Bacillus sp. (in: Bacteria) 1011, Brevibacterium sp., Brevibacterium sp. 9605, Geobacillus stearothermophilus, Geobacillus stearothermophilus (P31797), Klebsiella oxytoca, Klebsiella pneumoniae, Paenibacillus macerans, Paenibacillus macerans (P04830), Thermoanaerobacter sp., Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes (P26827), Thermococcus sp., Thermococcus sp. B1001

10223990

Abelyan, V.A.; Balayan, A.M.; Manukyan, L.S.; Afyan, K.B.; Meliksetyan, V.S.; Andreasyan, N.A.; Markosyan, A.A.

Characteristics of cyclodextrin production using cyclodextrin glucanotransferases from various groups of microorganisms

Appl. Biochem. Microbiol.

38

616-624

2002

Geobacillus stearothermophilus, Alkalihalobacillus alcalophilus, Niallia circulans, Weizmannia coagulans, Salimicrobium halophilum, Bacillus licheniformis, Paenibacillus macerans, Thermoactinomyces vulgaris, Bacillus licheniformis B-4025, Paenibacillus macerans BIO-2m, Thermoactinomyces vulgaris Tac-3554, Geobacillus stearothermophilus B-4006, Salimicrobium halophilum BIO-12H BIO-13H, Niallia circulans BIO-3m, Bacillus licheniformis BIO-9m, Alkalihalobacillus alcalophilus BA-4229, Weizmannia coagulans BIO-13m, Alkalihalobacillus alcalophilus B-3103

12449789

488862

Lee, S.H.; Kim, Y.W.; Lee, S.; Auh, J.H.; Yoo, S.S.; Kim, T.J.; Kim, J.W.; Kim, S.T.; Rho, H.J.; Choi, J.H.; Kim, Y.B.; Park, K.H.

Modulation of cyclizing activity and thermostability of cyclodextrin glucanotransferase and its application as an antistaling enzyme

J. Agric. Food Chem.

50

1411-1415

2002

Geobacillus stearothermophilus, Bacillus licheniformis, Paenibacillus macerans, Klebsiella pneumoniae, Niallia circulans (P43379), Geobacillus stearothermophilus NO2, Niallia circulans 251 (P43379), Geobacillus stearothermophilus ET1

11879012

488863

Rashid, N.; Cornista, J.; Ezaki, S.; Fukui, T.; Atomi, H.; Imanaka, T.

Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain

J. Bacteriol.

184

777-784

2002

Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) 1011, Geobacillus stearothermophilus, Geobacillus stearothermophilus (P31797), Klebsiella oxytoca (P08704), Niallia circulans, Niallia circulans (P43379), Niallia circulans 251, Niallia circulans 251 (P43379), Paenibacillus macerans (P31835), Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes EM1, Thermococcus kodakarensis (Q8X268), Thermococcus sp., Thermococcus sp. (Q9UWN2), Thermococcus sp. B1001, Thermococcus sp. B1001 (Q9UWN2)

11790748

Doukyu, N.; Kuwahara, H.; Aono, R.

Isolation of Paenibacillus illinoisensis that produces cyclodextrin glucanotransferase resistant to organic solvents

Biosci. Biotechnol. Biochem.

67

334-340

2003

Niallia circulans, Priestia megaterium, Salimicrobium halophilum, Paenibacillus macerans, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Brevibacterium sp., Thermoanaerobacterium thermosulfurigenes, Paenibacillus illinoisensis, Paenibacillus illinoisensis ST-12K, Brevibacterium sp. 9605, Bacillus sp. (in: Bacteria) BE101, Niallia circulans 251

12728995

658396

Yoon, S.H.; Bruce Fulton, D.; Robyt, J.F.

Enzymatic synthesis of two salicin analogues by reaction of salicyl alcohol with Bacillus macerans cyclomaltodextrin glucanyltransferase and Leuconostoc mesenteroides B-742CB dextransucrase

Carbohydr. Res.

339

1517-1529

2004

Paenibacillus macerans

15178396

658398

Rimphanitchayakit, V.; Tonozuka, T.; Sakano, Y.

Construction of chimeric cyclodextrin glucanotransferases from Bacillus circulans A11 and Paenibacillus macerans IAM1243 and analysis of their product specificity

Carbohydr. Res.

340

2279-2289

2005

Paenibacillus macerans (O52766), Niallia circulans (Q9F5W3), Paenibacillus macerans IAM1243 (O52766), Paenibacillus macerans IAM1243, Niallia circulans A11 (Q9F5W3)

16084934

Kim, W.; Chae, H.; Park, C.; Lee, K.

Stability and activity of crosslinking enzyme crystals of cyclodextrin glucanotransferase isolated from Bacillus macerans

J. Mol. Catal. B

26

287-292

2003

Paenibacillus macerans

-

660447

Kim, S.G.; Kweon, D.H.; Lee, D.H.; Park, Y.C.; Seo, J.H.

Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli

Protein Expr. Purif.

41

426-432

2005

Paenibacillus macerans

15866731

Qi, Q.; She, X.; Endo, T.; Zimmermann, W.

Effect of the reaction temperature on the transglycosylation reactions catalyzed by the cyclodextrin glucanotransferase from Bacillus macerans for the synthesis of large-ring cyclodextrins

Tetrahedron

60

799-806

2004

Paenibacillus macerans

-

671505

Qi, Q.; Zimmermann, W.

Cyclodextrin glucanotransferase: from gene to applications

Appl. Microbiol. Biotechnol.

66

475-485

2005

Bacillus licheniformis (P14014), Bacillus ohbensis (P27036), Bacillus sp. (in: Bacteria) (O82984), Bacillus sp. (in: Bacteria) (P05618), Bacillus sp. (in: Bacteria) (P17692), Bacillus sp. (in: Bacteria) (P30921), Bacillus sp. (in: Bacteria) (P31747), Bacillus sp. (in: Bacteria) (Q59239), Bacillus sp. (in: Bacteria) 1011 (P05618), Bacillus sp. (in: Bacteria) 1018 (P17692), Bacillus sp. (in: Bacteria) 17.1 (P30921), Bacillus sp. (in: Bacteria) 38-2 (P30921), Bacillus sp. (in: Bacteria) 6.6.3 (P31747), Bacillus sp. (in: Bacteria) A2-5a (O82984), Bacillus sp. (in: Bacteria) KC201 (Q59239), Brevibacillus brevis (O30565), Brevibacillus brevis CD162 (O30565), Cytobacillus firmus, Cytobacillus firmus 290-3, Evansella clarkii (Q8L3E0), Evansella clarkii 7384 (Q8L3E0), Geobacillus stearothermophilus (P31797), Klebsiella oxytoca (P08704), Klebsiella oxytoca M5a1 (P08704), Niallia circulans (P30920), Niallia circulans (P43379), Niallia circulans (Q9F5W3), Niallia circulans 251 (P43379), Niallia circulans 8 (P30920), Niallia circulans A11 (Q9F5W3), Nostoc sp. (Q8RMG0), Nostoc sp. 9229 (Q8RMG0), Paenibacillus macerans (P31835), Salipaludibacillus agaradhaerens, Salipaludibacillus agaradhaerens (Q7X3T0), Salipaludibacillus agaradhaerens DSM 8721 (Q7X3T0), Salipaludibacillus agaradhaerens DSM 9948, Salipaludibacillus agaradhaerens LS-3C, Streptococcus pyogenes, Thermoanaerobacter sp., Thermoanaerobacterium thermosulfurigenes (P26827), Thermococcus kodakarensis (Q8X268), Thermococcus sp. (Q9UWN2), Thermococcus sp. B1001 (Q9UWN2), Xanthomonas axonopodis, Xanthomonas campestris

15630515

Yoon, S.H.; Robyt, J.F.

Optimized synthesis of specific sizes of maltodextrin glycosides by the coupling reactions of Bacillus macerans cyclomaltodextrin glucanyltransferase

Carbohydr. Res.

341

210-217

2006

Paenibacillus macerans

16325787

673388

Kim, S.; Kim, J.; Yu, H.; Lee, D.; Kweon, D.; Seo, J.

Application of poly-arginine fused minichaperone to renaturation of cyclodextrin glycosyltransferase expressed in recombinant Escherichia coli

Enzyme Microb. Technol.

39

459-465

2006

Paenibacillus macerans

-

Arya, S.K.; Srivastava, S.K.

Kinetics of immobilized cyclodextrin gluconotransferase produced by Bacillus macerans ATCC 8244

Enzyme Microb. Technol.

39

507-510

2006

Paenibacillus macerans

-

Kaulpiboon, J.; Pongsawasdi, P.; Zimmermann, W.

Molecular imprinting of cyclodextrin glycosyltransferases from Paenibacillus sp. A11 and Bacillus macerans with gamma-cyclodextrin

FEBS J.

274

1001-1010

2007

Paenibacillus macerans, Paenibacillus sp., Paenibacillus sp. A11

17250740

674104

Jeang, C.L.; Lin, D.G.; Hsieh, S.H.

Characterization of cyclodextrin glycosyltransferase of the same gene expressed from Bacillus macerans, Bacillus subtilis, and Escherichia coli

J. Agric. Food Chem.

53

6301-6304

2005

Bacillus subtilis, Paenibacillus macerans, Escherichia coli, Paenibacillus macerans IAM1243

16076110

675462

Rha, C.; Lee, D.; Kim, S.; Min, W.; Byun, S.; Kweon, D.; Han, N.S.; Seo, J.

Production of cyclodextrin by poly-lysine fused Bacillus macerans cyclodextrin glycosyltransferase immobilized on cation exchanger

J. Mol. Catal. B

34

39-43

2005

Paenibacillus macerans

-

685767

Vollu, R.E.; da Mota, F.F.; Gomes, E.A.; Seldin, L.

Cyclodextrin production and genetic characterization of cyclodextrin glucanotranferase of Paenibacillus graminis

Biotechnol. Lett.

30

929-935

2008

Paenibacillus graminis, Paenibacillus macerans (P31835), Paenibacillus macerans, Paenibacillus macerans LMD24.10 (P31835)

18246304

688329

Son, Y.J.; Rha, C.S.; Park, Y.C.; Shin, S.Y.; Lee, Y.S.; Seo, J.H.

Production of cyclodextrins in ultrafiltration membrane reactor containing cyclodextrin glycosyltransferase from Bacillus macerans

J. Microbiol. Biotechnol.

18

725-729

2008

Paenibacillus macerans (P31835), Paenibacillus macerans

18467867

Li, Z.; Zhang, J.; Wang, M.; Gu, Z.; Du, G.; Li, J.; Wu, J.; Chen, J.

Mutations at subsite -3 in cyclodextrin glycosyltransferase from Paenibacillus macerans enhancing alpha-cyclodextrin specificity

Appl. Microbiol. Biotechnol.

83

483-490

2009

Paenibacillus macerans

19190904

701863

Li, Z.; Gu, Z.; Wang, M.; Du, G.; Wu, J.; Chen, J.

Delayed supplementation of glycine enhances extracellular secretion of the recombinant alpha-cyclodextrin glycosyltransferase in Escherichia coli

Appl. Microbiol. Biotechnol.

85

553-561

2010

Paenibacillus macerans, Paenibacillus macerans JFB05-01

19655137

701867

Leemhuis, H.; Kelly, R.M.; Dijkhuizen, L.

Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications

Appl. Microbiol. Biotechnol.

85

823-835

2010

Alkalihalobacillus clausii, Alkalihalobacillus clausii E16, Anaerobranca gottschalkii, Bacillus licheniformis, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) B1018, Bacillus sp. (in: Bacteria) BL-31, Bacillus sp. (in: Bacteria) G1, Bacillus sp. (in: Bacteria) KC201, Bacillus sp. (in: Bacteria) TS1-1, Brevibacillus brevis, Brevibacillus brevis CD162, Cytobacillus firmus, Evansella clarkii, Evansella clarkii 7384, Geobacillus stearothermophilus, Geobacillus stearothermophilus ET1, Klebsiella pneumoniae, Klebsiella pneumoniae M5a1, Niallia circulans, Paenibacillus campinasensis, Paenibacillus campinasensis H69-3, Paenibacillus graminis, Paenibacillus graminis NC22.13, Paenibacillus illinoisensis, Paenibacillus illinoisensis ST-12 K, Paenibacillus macerans, Paenibacillus pabuli, Paenibacillus pabuli US132, Paenibacillus sp., Priestia megaterium, Salipaludibacillus agaradhaerens, Salipaludibacillus agaradhaerens LS-3C, Thermoanaerobacter sp., Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes EM1

19763564

Svensson, D.; Ulvenlund, S.; Adlercreutz, P.

Efficient synthesis of a long carbohydrate chain alkyl glycoside catalyzed by cyclodextrin glycosyltransferase (CGTase)

Biotechnol. Bioeng.

104

854-861

2009

Paenibacillus macerans, Thermoanaerobacter sp.

19609955

703063

Yoon, S.H.; Bruce Fulton, D.; Robyt, J.F.

Synthesis of dopamine and L-DOPA-alpha-glycosides by reaction with cyclomaltohexaose catalyzed by cyclomaltodextrin glucanyltransferase

Carbohydr. Res.

344

2349-2356

2009

Paenibacillus macerans

19793583

704134

Li, Z.F.; Li, B.; Liu, Z.G.; Wang, M.; Gu, Z.B.; Du, G.C.; Wu, J.; Chen, J.

Calcium leads to further increase in glycine-enhanced extracellular secretion of recombinant alpha-cyclodextrin glycosyltransferase in Escherichia coli

J. Agric. Food Chem.

57

6231-6237

2009

Paenibacillus macerans, Paenibacillus macerans JFB05-01

19548680

Li, Z.F.; Zhang, J.Y.; Sun, Q.; Wang, M.; Gu, Z.B.; Du, G.C.; Wu, J.; Chen, J.

Mutations of lysine 47 in cyclodextrin glycosyltransferase from Paenibacillus macerans enhance beta-cyclodextrin specificity

J. Agric. Food Chem.

57

8386-8391

2009

Paenibacillus macerans, Paenibacillus macerans JFB05-01

19715296

Han, R.; Liu, L.; Shin, H.D.; Chen, R.R.; Du, G.; Chen, J.

Site-saturation engineering of lysine 47 in cyclodextrin glycosyltransferase from Paenibacillus macerans to enhance substrate specificity towards maltodextrin for enzymatic synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid (AA-2G)

Appl. Microbiol. Biotechnol.

97

5851-5860

2013

Paenibacillus macerans (O52766), Paenibacillus macerans

23129181

Li, Z.; Li, B.; Gu, Z.; Du, G.; Wu, J.; Chen, J.

Extracellular expression and biochemical characterization of alpha-cyclodextrin glycosyltransferase from Paenibacillus macerans

Carbohydr. Res.

345

886-892

2010

Paenibacillus macerans, Paenibacillus macerans JBF05-01

20227067

Yue, Y.; Liu, S.; Li, H.; Song, B.; Xie, T.; Sun, Y.; Chao, Y.; Qian, S.

Crystallization and preliminary X-ray diffraction studies of Tyr167His mutant alpha-cyclodextrin glucanotransferase from Bacillus macerans

Acta Crystallogr. Sect. F

69

1186-1189

2013

Paenibacillus macerans (S5ZJ19), Paenibacillus macerans 602-1 (S5ZJ19)

24100578

Han, R.; Liu, L.; Shin, H.; Chen, R.; Li, J.; Du, G.; Chen, J.

Systems engineering of tyrosine 195, tyrosine 260, and glutamine 265 in cyclodextrin glycosyltransferase from Paenibacillus macerans to enhance maltodextrin specificity for 2-O-D-glucopyranosyl-L-ascorbic acid synthesis

Appl. Environ. Microbiol.

79

672-677

2013

Paenibacillus macerans, Paenibacillus macerans JFB05-01

23160123

735512

Wang, L.; Duan, X.; Wu, J.

Enhancing the alpha-cyclodextrin specificity of cyclodextrin glycosyltransferase from Paenibacillus macerans by mutagenesis masking the subsite -7

Appl. Environ. Microbiol.

82

2247-2255

2016

Paenibacillus macerans

26850297

736290

Li, C.; Ban, X.; Gu, Z.; Li, Z.

Calcium ion contribution to thermostability of cyclodextrin glycosyltransferase is closely related to calcium-binding site CaIII

J. Agric. Food Chem.

61

8836-8841

2013

Niallia circulans, Paenibacillus macerans

23968201

Xie, T.; Hou, Y.; Li, D.; Yue, Y.; Qian, S.; Chao, Y.

Structural basis of a mutant Y195I alpha-cyclodextrin glycosyltransferase with switched product specificity from alpha-cyclodextrin to beta-/gamma-cyclodextrin

J. Biotechnol.

182-183

92-96

2014

Paenibacillus macerans, Paenibacillus macerans 602-1

24637377

736787

Song, B.; Yue, Y.; Xie, T.; Qian, S.; Chao, Y.

Mutation of tyrosine167histidine at remote substrate binding subsite -6 in alpha-cyclodextrin glycosyltransferase enhancing alpha-cyclodextrin specificity by directed evolution

Mol. Biotechnol.

56

232-239

2014

Paenibacillus macerans, Paenibacillus macerans 602-1

24037411

755771

Li, Y.; Liu, J.; Wang, Y.; Liu, B.; Xie, X.; Jia, R.; Li, C.; Li, Z.

A two-stage temperature control strategy enhances extracellular secretion of recombinant alpha-cyclodextrin glucosyltransferase in Escherichia coli

AMB Express

7

165

2017

Paenibacillus macerans, Paenibacillus macerans JFB05-01

28831769

Han, R.; Ni, J.; Zhou, J.; Dong, J.; Xu, G.; Ni, Y.

Engineering of cyclodextrin glycosyltransferase reveals pH-regulated mechanism of enhanced long-chain glycosylated sophoricoside specificity

Appl. Environ. Microbiol.

86

e00004-20

2020

Paenibacillus macerans (P04830), Paenibacillus macerans

32005733

Tao, X.; Su, L.; Wu, J.

Current studies on the enzymatic preparation 2-O-alpha-D-glucopyranosyl-L-ascorbic acid with cyclodextrin glycosyltransferase

Crit. Rev. Biotechnol.

39

249-257

2019

Geobacillus stearothermophilus, Alkalihalobacillus alcalophilus, Niallia circulans, Paenibacillus macerans, Thermoanaerobacter sp., Paenibacillus sp., Anaerobranca gottschalkii, Paenibacillus sp. JK-12, Paenibacillus sp. JB-13, Bacillus sp. SK 13.002, Alkalihalobacillus alcalophilus 7-12, Niallia circulans 251

30563366

Koh, D.W.; Park, M.O.; Choi, S.W.; Lee, B.H.; Yoo, S.H.

Efficient biocatalytic production of cyclodextrins by combined action of amylosucrase and cyclodextrin glucanotransferase

J. Agric. Food Chem.

64

4371-4375

2016

Paenibacillus macerans, Paenibacillus macerans (P04830)

27169988

Han, R.; Ge, B.; Jiang, M.; Xu, G.; Dong, J.; Ni, Y.

High production of genistein diglucoside derivative using cyclodextrin glycosyltransferase from Paenibacillus macerans

J. Ind. Microbiol. Biotechnol.

44

1343-1354

2017

Paenibacillus macerans, Paenibacillus macerans CCTCC M203062

28660368