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Information on EC 3.2.1.11 - dextranase
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3.2.1.11 dextranaseSpecify your search results
Word Map
- 3.2.1.11
- dextrans
- streptococcus
- glucans
-
dental
- plaque
- penicillium
- caries
- dextransucrase
- sobrinus
- leuconostoc
-
cariogenic
- isomaltose
-
water-insoluble
- mesenteroides
- synthesis
- sanguis
- isomaltotriose
- salivarius
- medicine
- lipomyces
-
glucosyltransferases
-
colon-specific
- mutanase
- downei
- funiculosum
- starkeyi
- biotechnology
- agriculture
- degradation
- nutrition
- food industry
- drug development
-
glucan-binding
- isomalto-oligosaccharides
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
1,6-alpha-D-glucan-6-glucanohydrolase, 6-alpha-D-glucan 6-glucanohydrolase, alpha-1,6-D-glucan 6-glucanohydrolase, alpha-1,6-D-glucan-6-glucanohydrolase, Alpha-1,6-glucan-6-glucanohydrolase, alpha-D-1,6-glucan-6-glucanohydrolase, alpha-dextranase, alpha-glucanase, AODex, Dex, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,6-alpha-D-glucan-6-glucanohydrolase
6-alpha-D-glucan 6-glucanohydrolase
alpha-1,6-D-glucan 6-glucanohydrolase
alpha-1,6-D-glucan-6-glucanohydrolase
Alpha-1,6-glucan-6-glucanohydrolase
alpha-D-1,6-glucan-6-glucanohydrolase
-
-
-
-
AODex
Dex
DexA
dextran hydrolase
-
-
-
-
dextranase
dextranase DL 2
-
-
-
-
DL 2
-
-
-
-
endo-dextranase
endodextranase
Fjoh_4430
LSD1
SmDex
Teth39_0264
TLDex
TPDex
additional information
Alpha-1,6-glucan-6-glucanohydrolase
-
-
-
-
endo-dextranase
-
-
-
-
endodextranase
-
-
-
-
additional information
the enzyme belongs to the glycoside hydrolase family (GH) 66
additional information
the enzyme belongs to the glycoside hydrolase family (GH) 66
-
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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 SOURCE
PATHWAYS
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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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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
isomaltose + isomaltotriose + D-glucose + low molecular-mass polysaccharides
dextran + H2O
isomaltotetraose
-
-
plus small amounts of cycloisomaltooligosaccharides with a degree of polymerization of 7â14
-
?
dextran + H2O
isomaltotetraose + cycloisomaltooligosaccharides
-
main products are isomaltotetraose and small amounts of cycloisomaltooligosaccharides with a degree of polymerization of 7-14
-
?
dextran T100 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
-
-
-
?
dextran T2000 + H2O
isomaltooligosaccharides
-
very high hydrolytic affinity, 100% activity with 3% (w/v) dextran T2000
-
-
?
dextran T2000 + H2O
isomaltotriose + isomaltotetraose + isomaltopentaose
-
-
main end-products
-
?
dextran T3 + H2O
isomaltose + isomaltotriose + D-glucose
-
65.17% activity compared to dextran T70
-
-
?
dextran T40 + H2O
isomaltose + isomaltotriose
88% activity compared to dextran T70
-
-
?
dextran T40 + H2O
isomaltose + isomaltotriose + D-glucose
-
98.5% activity compared to dextran T70
-
-
?
dextran T40 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
-
-
-
?
dextran T5 + H2O
isomaltose + isomaltotriose + D-glucose
-
65.54% activity compared to dextran T70
-
-
?
dextran T500 + H2O
isomaltose + isomaltotriose
96% activity compared to dextran T70
-
-
?
dextran T500 + H2O
isomaltose + isomaltotriose + D-glucose
-
99.62% activity compared to dextran T70
-
-
?
dextran T500 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
90.78% activity compared to dextran T250
-
-
?
dextran T60-90 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
90.19% activity compared to dextran T250
-
-
?
dextran T70 + H2O
isomaltooligosaccharides
-
96% of the activity with dextran T500
-
-
?
dextran T70 + H2O
isomaltose + isomaltotriose
100% activity
-
-
?
dextran T70 + H2O
isomaltose + isomaltotriose + D-glucose
-
100% activity
-
-
?
dextran T70 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
-
-
-
?
glucan + H2O
D-glucose + isomaltose + isomaltotriose + ?
-
from Streptococcus sobrinus K1-R
-
-
?
isomaltohexaose + H2O
D-glucose + isomaltose + isomaltotriose + isomaltotetraose + isomaltopentaose
-
-
-
?
Sephacryl S-300 + H2O
?
-
4.02% activity compared to dextran T250
-
-
?
(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
?
-
-
-
?
4-nitrophenyl alpha-isomaltopentoside + H2O
?
-
-
-
?
4-nitrophenyl alpha-isomaltotetraoside + 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
?
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
-
-
?
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 + isomaltose + isomaltooligosaccharides
-
-
-
?
dextran + H2O
D-glucose + isomaltose + isomaltooligosaccharides
-
-
-
?
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
-
-
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
isomaltooligosaccharides
-
the enzyme only has specificity to the alpha(1->6) glycosidic bond of dextran
-
-
?
dextran + H2O
isomaltooligosaccharides
-
the enzyme only has specificity to the alpha(1->6) glycosidic bond of dextran
-
-
?
dextran + H2O
isomaltose + isomaltotriose + D-glucose + isomaltooligosaccharides
with 4 mg/ml dextran, isomaltooligosaccharides with degrees of polymerization of 3 and 4 are present at the beginning of the reaction, and D-glucose and isomaltose are produced by the end of the reaction
-
-
?
dextran + H2O
isomaltose + isomaltotriose + D-glucose + isomaltooligosaccharides
with 4 mg/ml dextran, isomaltooligosaccharides with degrees of polymerization of 3 and 4 are present at the beginning of the reaction, and D-glucose and isomaltose are produced by the end of the reaction
-
-
?
dextran + H2O
isomaltose + isomaltotriose + D-glucose + low molecular-mass polysaccharides
-
the enzyme specially catalyzes the endohydrolysis of alpha-(1,6)-D-glycoside linkages at random sites of dextran
-
-
?
dextran + H2O
isomaltose + isomaltotriose + D-glucose + low molecular-mass polysaccharides
Penicillium cyclopium CICC-4022
-
the enzyme specially catalyzes the endohydrolysis of alpha-(1,6)-D-glycoside linkages at random sites of dextran
-
-
?
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
-
-
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 T10 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
88.64% activity compared to dextran T250
-
-
?
dextran T10 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
88.64% activity compared to dextran T250
-
-
?
dextran T20 + H2O
isomaltooligosaccharides
-
90% of the activity with dextran T500
-
-
?
dextran T20 + H2O
isomaltooligosaccharides
-
68.64% activity compared to dextran T2000
-
-
?
dextran T20 + H2O
isomaltose + isomaltotriose + D-glucose
-
90.64% activity compared to dextran T70
-
-
?
dextran T20 + H2O
isomaltose + isomaltotriose + D-glucose
Penicillium cyclopium CICC-4022
-
90.64% 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
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose + D-glucose
-
97% activity compared to dextran T70
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose + D-glucose
Penicillium cyclopium CICC-4022
-
97% activity compared to dextran T70
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
87.48% activity compared to dextran T250
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
87.48% activity compared to dextran T250
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
-
-
?
dextran T2000 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
-
-
?
dextran T250 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
100% activity
-
-
?
dextran T250 + H2O
isomaltose + isomaltotriose + isomaltooligosaccharides
-
100% activity
-
-
?
dextran T40 + H2O
isomaltooligosaccharides
-
91% of the activity with dextran T500
-
-
?
dextran T40 + H2O
isomaltooligosaccharides
-
72.96% activity compared to dextran T2000
-
-
?
pullulan + H2O
?
4% activity compared to dextran T70
-
-
?
soluble starch + H2O
?
Penicillium cyclopium CICC-4022
-
20.83% activity compared to dextran T70
-
-
?
additional information
?
-
-
no activity with starch, cellulose, glycol chitin, chitin, Sephadex G10, sucrose, and maltose
-
-
?
additional information
?
-
-
no activity with starch, cellulose, glycol chitin, chitin, Sephadex G10, sucrose, and maltose
-
-
?
additional information
?
-
-
the enzyme specifically cleaves the alpha-1,6 glycosidic bond. Poor substrate: starch. No substrate: pullulan
-
-
?
additional information
?
-
-
no activity toward Sepharose 6B, beta-cyclodextrin, chitosan, maltose, or sucrose
-
-
?
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
?
-
-
the enzyme has no effects on cellulose, sucrose, chitin, chitosan and beta-cyclodextrin
-
-
?
additional information
?
-
Penicillium cyclopium CICC-4022
-
the enzyme has no effects on cellulose, sucrose, chitin, chitosan and beta-cyclodextrin
-
-
?
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
?
-
no activity toward 4-nitrophenyl alpha-isomaltotrioside
-
-
?
additional information
?
-
-
no activity toward 4-nitrophenyl alpha-isomaltotrioside
-
-
?
additional information
?
-
no activity toward 4-nitrophenyl alpha-isomaltotrioside
-
-
?
additional information
?
-
-
enzyme influences glucan synthesis, linkage remodeling and branching
-
-
?
additional information
?
-
-
no activity towards beta-cyclodextrin, chitin, Sepharose 6B, chitosan, and sucrose. Low activity towards soluble starch
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
dextran + H2O
isomaltose + isomaltotriose + D-glucose + low molecular-mass polysaccharides
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
-
-
?
alternan + H2O
?
15% activity compared to dextran T70
-
-
?
alternan + H2O
?
15% activity compared to dextran T70
-
-
?
dextran + H2O
D-glucose + isomaltose + isomaltooligosaccharides
-
-
-
?
dextran + H2O
D-glucose + isomaltose + isomaltooligosaccharides
-
-
-
?
dextran + H2O
isomaltooligosaccharides
-
the enzyme only has specificity to the alpha(1->6) glycosidic bond of dextran
-
-
?
dextran + H2O
isomaltooligosaccharides
-
the enzyme only has specificity to the alpha(1->6) glycosidic bond of dextran
-
-
?
dextran + H2O
isomaltose + isomaltotriose + D-glucose + low molecular-mass polysaccharides
-
the enzyme specially catalyzes the endohydrolysis of alpha-(1,6)-D-glycoside linkages at random sites of dextran
-
-
?
dextran + H2O
isomaltose + isomaltotriose + D-glucose + low molecular-mass polysaccharides
Penicillium cyclopium CICC-4022
-
the enzyme specially catalyzes the endohydrolysis of alpha-(1,6)-D-glycoside linkages at random sites of dextran
-
-
?
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
?
-
AODex treatment of stale sugar cane juice results in a yield of square and light-colored sugar crystals
-
-
?
additional information
?
-
AODex treatment of stale sugar cane juice results in a yield of square and light-colored sugar crystals
-
-
?
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe2+
K+
Li+
Mg2+
Mn2+
Na+
Ni2+
additional information
Fe2+
stimulates activity of the dextransucrase-dextranase fusion protein
K+
stimulates activity of the dextransucrase-dextranase fusion protein
Li+
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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INHIBITOR
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
-
teeth rinsing product reagents, including carboxybenzene, ethanol, sodium fluoride, and xylitol have no effects on enzyme activity
-
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
-
Zn2+, Co2+, Ni2+, Fe3+ and EDTA show no obvious inhibition at 1 mM
-
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
-
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 Woodwardâs 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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alveolar Bone Loss
Effects of two dextranase preparations on dental caries and alveolar bone loss in hamsters.
Colonic Neoplasms
Colon specific enzyme responsive oligoester crosslinked dextran nanoparticles for controlled release of 5-fluorouracil.
Crohn Disease
Dextran and 5-aminosalicylic acid (5-ASA) conjugates: synthesis, characterisation and enzymic hydrolysis.
Dental Caries
Anti-Streptococcus mutans and anti-biofilm activities of dextranase and its encapsulation in alginate beads for application in toothpaste.
Dental Caries
Characterization of a marine-derived dextranase and its application to the prevention of dental caries.
Dental Caries
Effect of dextranase prepared from Spicaria violacea on dental caries in the hamster.
Dental Caries
Effects of two dextranase preparations on dental caries and alveolar bone loss in hamsters.
Dental Caries
Inhibition of rat dental caries by dextranase from a strain of Spicaria violacea.
Dental Caries
Optimization of Fungal Dextranase Production and Its Antibiofilm Activity, Encapsulation and Stability in Toothpaste.
Dental Caries
Renaturation of dextranase activity from culture supernatant fluids of Streptococcus sobrinus after sodium dodecylsulfate polyacrylamide gel electrophoresis.
Dental Caries
The development and application of dextranase in the prevention of dental caries.
Dental Caries
[Effects of dextranase, monofluorophosphate, and their combination on the reduction of dental caries and plaque in rats]
Dental Plaque
1. The effect of a dextranase mouthwash on dental plaque in young adults and children.
Dental Plaque
A novel dextranase gene from the marine bacterium Bacillus aquimaris S5 and its expression and characteristics.
Dental Plaque
Anti-Streptococcus mutans and anti-biofilm activities of dextranase and its encapsulation in alginate beads for application in toothpaste.
Dental Plaque
Effect of dextranase on the extracellular polysaccharide synthesis of Streptococcus mutans; chemical and scanning electron microscopy studies.
Dental Plaque
Effects of dextranase from Spicaria violaceae (IFO 6120) on the polysaccharides produced by oral streptococci and on human dental plaque.
Dental Plaque
Expression, purification and characterization of a cold-adapted dextranase from marine bacteria and its ability to remove dental plaque.
Dental Plaque
Immobilization of Dextranase on Nano-Hydroxyapatite as a Recyclable Catalyst.
Dental Plaque
In vitro adsorption of dextranase by dental plaque and buccal mucosa, and its oral retention after rinsing the mouth.
Dental Plaque
Metabolism of the polysaccharides of human dental plaque. I. Dextranase activity of streptococci, and the extracellular polysaccharides synthesized from sucrose.
Dental Plaque
Metabolism of the polysaccharides of human dental plaque: release of dextranase in batch cultures of Streptococcus mutans.
Dental Plaque
The effect of a bacterial dextranase on human dental plaque formation and gingivitis development.
Dental Plaque
The effect of dextranase on the release of reducing sugars from dental plaque.
Dental Plaque
The influence of mutanase and dextranase on the production and structure of glucans synthesized by streptococcal glucosyltransferases.
Dental Plaque
The influence of the probiotic Streptococcus salivarius M18 on indices of dental health in children: a randomised double-blind placebo-controlled trial.
Dental Plaque
The Marine Catenovulum agarivorans MNH15 and Dextranase: Removing Dental Plaque.
Dental Plaque
[Effects of dextranase from a strain of Spicaria species on the polysaccharides prepared from human dental plaque (author's transl)]
Dental Plaque
[In vitro and clinical effects of Chaetomium gracile dextranase on the release of reducing sugar and on the reduction of dental plaque]
Dental Plaque
[Scanning electron microscope study on the removal of artificial dental plaque treated with a bacteriolytic enzyme from Streptomyces globisporus--its synergistic effects with dextranase and lysozyme (author's transl)]
Dental Plaque
[The clinical effect of dextranase from spicaria violaceae on human dental plaque (author's transl)]
Dental Plaque
[The effect of dentifrice containing Chaetomium gracile dextranase on the reduction of dental plaque (2)--the time series analysis of variance]
Dental Plaque
[The in vitro effects of dextranase on dental plaque produced by Streptococcus mutans]
Endocarditis
Bacterial adherence in the pathogenesis of endocarditis. Interaction of bacterial dextran, platelets, and fibrin.
Endocarditis
Dextranase enhances antibiotic efficacy in experimental viridans streptococcal endocarditis.
Endocarditis
Enzymatic modification of glycocalyx in the treatment of experimental endocarditis due to viridans streptococci.
Gingivitis
The effect of a bacterial dextranase on human dental plaque formation and gingivitis development.
Hematuria
Enzymolysis of glomerular immune deposits in vivo with dextranase/protease ameliorates proteinuria, hematuria, and mesangial proliferation in murine experimental IgA nephropathy.
Periodontal Diseases
The retardation of spontaneous periodontal disease and the prevention of caries in hamsters with dextranase.
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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
9.1
Dextran
-
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
Km value 0.374 mg/ml, p-h 4.5, 37°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 1.77 g/l, pH 6.0, 50°C, dextran with molecular weight from 60000 to 90000 Da
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
-
additional information
additional information
-
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
11.9
3.02
purified recombinant enzyme SmDex95, the 95 kDa variant, pH 5.0, temperature not specified in the publication
43
8.21
purified recombinant enzyme SmDex90, the 90 kDa variant, pH 5.0, temperature not specified in the publication
90
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
additional information
-
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
additional information
-
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
4.5
4.5 - 5.5
4.6
5 - 6
5.2
5.3
5.4
5.4 - 5.8
5.5
5.8
6.5