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Information on EC 3.2.1.132 - chitosanase
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3.2.1.132 chitosanaseIUBMB Comments
A whole spectrum of chitosanases are now known (for more details, see {http://rbrzezinski.recherche.usherbrooke.ca/::http://rbrzezinski.recherche.usherbrooke.ca/}). They can hydrolyse various types of links in chitosan. The only constant property is the endohydrolysis of GlcN-GlcN links, which is common to all known chitosanases. One known chitosanase is limited to this link recognition , while the majority can also recognize GlcN-GlcNAc links or GlcNAc-GlcN links but not both. They also do not recognize GlcNAc-GlcNAc links in partly acetylated chitosan.
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Word Map
- 3.2.1.132
- chitosans
- chitooligosaccharides
-
deacetylation
- oligosaccharide
- glycoside
-
colloidal
- chitinases
-
glcn
-
endo-type
-
biocontrol
- paenibacillus
- circulans
- chitotetraose
-
chitosanolytic
- d-glucosamine
- food industry
-
chitinolytic
- chitotriose
- synthesis
- biotechnology
- glucanase
- analysis
- industry
- pharmacology
- coss
- medicine
- chitopentaose
-
chitooligomers
- lichenan
- microbacterium
- agriculture
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
+
=
+
+
=
+
Synonyms
chitosanase, csnts, endo-chitosanase, chitosanase ii, gscsn46a, family 46 chitosanase, chit a, chit b, csnw2, endochitosanase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
actase
AsChi
Cel8A
ChA
CHI
ChiN
Chit A
Chit B
chitosan N-acetylglucosaminohydrolase
chitosanase
chitosanase II
ChiX
CHO
Cho-GG
ChoK
Chs1
Csn
Csn1
Csn2
CsnA
CsnB
CSNMHKI
endo-chitosanase
GH-75 chitosanase
GsCsn46A
MH-K1 chitosanase
mschito
PgChP
SACTE_5457
SCO0677
TKU032 chitosanase
additional information
additional information
-
the chitosanase is related to the glycosyl hydrolase family 46 chitosanases
additional information
-
the enzyme belongs to the glycohydrolase family 8, GH8
additional information
the enzyme belongs to the glycoside hydrolase 3, GH3-like family of Anabaena variabilis ATCC 29413
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O = 2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranose + 2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
chitosan N-acetylglucosaminohydrolase
A whole spectrum of chitosanases are now known (for more details, see {http://rbrzezinski.recherche.usherbrooke.ca/::http://rbrzezinski.recherche.usherbrooke.ca/}). They can hydrolyse various types of links in chitosan. The only constant property is the endohydrolysis of GlcN-GlcN links, which is common to all known chitosanases. One known chitosanase is limited to this link recognition [4], while the majority can also recognize GlcN-GlcNAc links or GlcNAc-GlcN links but not both. They also do not recognize GlcNAc-GlcNAc links in partly acetylated chitosan.
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CAS REGISTRY NUMBER
COMMENTARY
51570-20-8
-
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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
(GlcN)7 + H2O
beta-D-GlcN-(1->4)-beta-D-GlcN + beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN + beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN + beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN
Pedobacter sp. PR-M6
-
-
-
-
?
4-methylumbelliferyl beta-chitotrioside + H2O
4-methylumbelliferone + chitotriose + chitobiose + 4-methylumbelliferyl N-acetyl-beta-D-glucosaminide
-
-
-
-
?
aminoethyl chitosan + H2O
aminoethyl low molecular weight chitosan + ?
-
average molecular weight of aminoethyl low molecular weight chitosan is 8.89 kDa
-
-
?
beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN + H2O
beta-D-GlcN-(1->4)-beta-D-GlcN + beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN
Pedobacter sp. PR-M6
-
-
-
-
?
beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN + H2O
beta-D-GlcN-(1->4)-beta-D-GlcN + beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN + beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN
Pedobacter sp. PR-M6
-
-
-
-
?
beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN + H2O
beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN + beta-D-GlcN-(1->4)-beta-D-GlcN + beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN
(GlcN)6 is mainly hydrolyzed into two molecules of (GlcN)3, accompanied by a very small proportion of (GlcN)2 and (GlcN)4
-
-
?
carboxymethyl chitin + H2O
?
-
isoform A shows 41.8% activity and isoform B 17.2% activity compared to chitosan
-
-
?
carboxymethyl chitosan + H2O
carboxymethyl low molecular weight chitosan + ?
-
average molecular weight of carboxymethyl low molecular weight chitosan is 11.2 kDa
-
-
?
chitohexaose + H2O
chitobiose + chitotriose + chitotetraose
-
-
mutant enzyme D57A produces smaller amounts of chitobiose and chitotetraose as compared to chitotriose than does the wild-type enzyme
-
?
chitohexaose + H2O
chitotriose + chitobiose + chitotetraose
-
-
triglucosamine is the main product
-
?
chitosan + H2O
beta-D-GlcN-(1->4)-beta-D-GlcN + ?
colloidal chitosan, endotype cleavage pattern and hydrolysis of chitosan to yield (GlcN)2 as the major product
-
-
?
chitosan + H2O
beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN + beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN + beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN
beta-D-GlcN-(1->4)-beta-D-GlcN-(1->4)-beta-D-GlcN, (GlcN)4 and (GlcN)5 are the major products
-
-
?
chitosan + H2O
chitobiose + chitooligosaccharides
-
chitodisaccharide is the main product (69.9% of the total product)
-
-
?
chitosan + H2O
chitobiose + chitotriose + chitotetraose + chitopentaose + chitohexaose + chitoheptaose
chitosan + H2O
chitotriose + chitotetraose + chitopentaose
-
-
major hydrolytic products
-
?
chitosan + H2O
chitotriose + chitotetraose + chitopentaose + chitohexaose
the main products of chitosan hydrolyzed by recombinant chitosanase are (GlcN)3-6
-
-
?
chitosan + H2O
GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcN
chitosan + H2O
glucosamine oligomer + N-acetyl-glucosamine oligomer
-
-
hydrolysates are oligomers with one to four glucosamine residues and some oligomers with longer chain length
-
?
chitosan + H2O
low molecular weight chitosan polymers + chitosan oligomers
Ficus sp.
-
most effectively hydrolyzes chitosan polymers that are 52-70% deacetylated
-
-
?
chitosan hexasaccharide + H2O
chitosan disaccharide + chitosan trisaccharide + chitosan tetrasaccharide
ethylene glycol chitosan + H2O
ethylene glycol low molecular weight chitosan + ?
-
average molecular weight of ethylene glycol low molecular weight chitosan is 11.2 kDa
-
-
?
GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN + H2O
GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN + GlcN-beta-(1->4)-GlcN + GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN
-
best substrate
GlcN-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4) is the main product
-
?
GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc + H2O
?
-
-
-
-
?
GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN + H2O
?
GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcN + H2O
GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcNbeta(1-4)GlcN + D-glucosamine
-
-
-
-
?
GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcN + H2O
GlcNbeta(1-4)GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcN
-
-
-
-
?
GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcN + H2O
GlcNbeta(1-4)GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcN
-
-
-
-
?
N-acetylated chitosan + H2O
?
activity is ca. 3fold less than toward chitosan
-
-
?
water-soluble chitosan + H2O
chitosan oligosaccharides
-
substrate 40-50% deacetylated, 7.6% of the activity with colloidal chitosan
-
-
?
beta-chitin + H2O
?
-
85% activity with chitin (beta-type) compared to chitosan (95% DD)
-
-
?
beta-chitin + H2O
?
Serratia marcescens TKU019
-
85% activity with chitin (beta-type) compared to chitosan (95% DD)
-
-
?
carboxylmethyl cellulose + H2O
?
-
61.9% activity compared to chitosan
-
-
?
carboxymethyl cellulose + H2O
?
-
55% activity compared to 50% deacetylated chitosan
-
-
?
carboxymethyl cellulose + H2O
?
-
5.3% of the activity with soluble chitosan
-
-
?
carboxymethyl cellulose + H2O
?
-
5.3% of the activity with soluble chitosan
-
-
?
carboxymethylcellulose + H2O
?
58% activity compared to chitosan
-
-
?
carboxymethylcellulose + H2O
?
58% activity compared to chitosan
-
-
?
chitin + H2O
?
-
isoform A shows 7.8% activity and isoform B 10.8% activity compared to chitosan
-
-
?
chitoheptaose + H2O
?
23.8% of the activity with chitosan
-
-
?
chitoheptaose + H2O
?
Bacillus sp. (in: Bacteria) KCTC 0377BP
23.8% of the activity with chitosan
-
-
?
chitohexaose + H2O
?
20.0% of the activity with chitosan
-
-
?
chitohexaose + H2O
?
-
ChiN hydrolyzes oligomers larger than chitopentaose
-
-
?
chitohexaose + H2O
?
-
ChiN hydrolyzes oligomers larger than chitopentaose
-
-
?
chitopentaose + H2O
?
16.8% of the activity with chitosan
-
-
?
chitopentaose + H2O
?
Bacillus sp. (in: Bacteria) KCTC 0377BP
16.8% of the activity with chitosan
-
-
?
chitosan + H2O
?
-
70-100% deacetylated chitosan, the activity of AsChi increases with the degree of deacetylation of chitosan. AsChi probably hydrolyzes chitosan in an endo-type fashion
-
-
?
chitosan + H2O
?
-
70-100% deacetylated chitosan, the activity of AsChi increases with the degree of deacetylation of chitosan. AsChi probably hydrolyzes chitosan in an endo-type fashion
-
-
?
chitosan + H2O
?
exhibits antifungal activity against Rhizopus oryzae IAM6252, which is known to produce chitosan probably as a cell wall component. Glu22 acts as an active center in the CtoA protein
-
-
?
chitosan + H2O
?
-
100% activity with 50% deacetylated chitosan, 89% activity with 70% deacetylated chitosan, 91% activity with 98% deacetylated chitosan
-
-
?
chitosan + H2O
?
-
the enzyme hydrolyzes 70% deacetylated chitosan faster than fully deacetylated chitosan
-
-
?
chitosan + H2O
?
-
the enzyme hydrolyzes 70% deacetylated chitosan faster than fully deacetylated chitosan
-
-
?
chitosan + H2O
?
-
100% activity with chitosan of 60% degrees of deacetylation
-
-
?
chitosan + H2O
?
-
100% activity with chitosan of 60% degrees of deacetylation
-
-
?
chitosan + H2O
?
-
-
-
-
?
chitosan + H2O
?
-
-
-
-
?
chitosan + H2O
?
the mutant enzymes E309R/N319E and N308V/E309R/N319E can accept N-acetyl-D-glucosamine units at their subsite (-2), which is impossible for the wild-type enzyme
-
-
?
chitosan + H2O
?
-
a chitosanase classification system is suggested which is based on specificities and preferences of subsites (-2) to (+2)
-
-
?
chitosan + H2O
?
-
the enzyme shows activity toward chitosan polymers which exhibit various degrees of deacetylation (21-94%). It hydrolyzes 70-84% deacetylated chitosan polymers most effectively. Substrate specificity analysis indicates that the enzyme catalyzes the hydrolysis of chitin and chitosan polymers and their derivatives
-
-
?
chitosan + H2O
?
-
Chitosan, or beta-1,4-linked glucosamine, is a deacetylated derivative of chitin. The chitosanase is specific for chitosan as substrate
-
-
?
chitosan + H2O
?
-
the chitosanase is specific for chitosan as substrate
-
-
?
chitosan + H2O
?
-
Chitosan, or beta-1,4-linked glucosamine, is a deacetylated derivative of chitin. The chitosanase is specific for chitosan as substrate
-
-
?
chitosan + H2O
?
-
the chitosanase is specific for chitosan as substrate
-
-
?
chitosan + H2O
?
-
activity increases with the degree of deacetylation of chitosan
-
-
?
chitosan + H2O
?
-
activity increases with the degree of deacetylation of chitosan
-
-
?
chitosan + H2O
?
-
the chitosanase is an endo-type enzyme, the preferred substrates of chitosanase are chitosan preparations with a high degree of deacetylation, substrate is chitosan 66-97% deacetylated
-
-
?
chitosan + H2O
?
a chitosanase classification system is suggested which is based on specificities and preferences of subsites (-2) to (+2)
-
-
?
chitosan + H2O
?
Niallia circulans MH-K1
a chitosanase classification system is suggested which is based on specificities and preferences of subsites (-2) to (+2)
-
-
?
chitosan + H2O
?
-
chitosanase is a glycosyl hydrolase that endolytically hydrolyzes beta-1,4-linkages between D -glucosamine residues in a partially acetylated chitosan
-
-
?
chitosan + H2O
?
-
excellent activity on colloidal chitosan (338.74%), followed by chitosan powder (185.38%)
-
-
?
chitosan + H2O
?
Paenibacillus mucilaginosus TKU032
-
excellent activity on colloidal chitosan (338.74%), followed by chitosan powder (185.38%)
-
-
?
chitosan + H2O
?
the enzyme liberates a mean of 0.6 mM D-glucosamine per microgram of protein in 4 h reaction
-
-
?
chitosan + H2O
?
the enzyme liberates a mean of 0.6 mM D-glucosamine per microgram of protein in 4 h reaction
-
-
?
chitosan + H2O
?
-
activity toward 94% deacetylated soluble chitosan, 85% deacetylated soluble chitosan, and 73% deacetylated soluble chitosan
-
-
?
chitosan + H2O
?
substrate recognition mechanismis for non-processive chitosanase is decribed
-
-
?
chitosan + H2O
?
-
activity toward 94% deacetylated soluble chitosan, 85% deacetylated soluble chitosan, and 73% deacetylated soluble chitosan
-
-
?
chitosan + H2O
?
-
activity decreases with the degree of deacetylation of chitosan. The enzyme hydrolyzes chitosan with 60-95% degree of deacetylation
-
-
?
chitosan + H2O
?
-
100% activity with chitosan (95% degree of deacetylation), 26% activity with chitosan (85% degree of deacetylation)
-
-
?
chitosan + H2O
?
-
activity decreases with the degree of deacetylation of chitosan. The enzyme hydrolyzes chitosan with 60-95% degree of deacetylation
-
-
?
chitosan + H2O
?
Serratia marcescens TKU019
-
100% activity with chitosan (95% degree of deacetylation), 26% activity with chitosan (85% degree of deacetylation)
-
-
?
chitosan + H2O
?
-
chitosan of approximately 100 kDa and degree of deacetylation 96%
-
-
?
chitosan + H2O
?
the wild type chitosanase shows a clear preference for chitosan with high degrees of N-deacetylation (84-97%)
-
-
?
chitosan + H2O
?
-
chitosan of approximately 100 kDa and degree of deacetylation 96%
-
-
?
chitosan + H2O
?
a chitosanase classification system is suggested which is based on specificities and preferences of subsites (-2) to (+2)
-
-
?
chitosan + H2O
?
chitosan 10B. The enzyme has both cellulase activity and chitosanase activity
-
-
?
chitosan + H2O
chitobiose + chitotriose + chitotetraose
-
activity increases with the degree of deacetylation of chitosan. The enzyme hydrolyzes chitosan with 62-100% degree of deacetylation. Hydrolysis of chitosan with 99% degree of deacetylation by ChiN releases chitobiose, chitotriose and chitotetraose
-
-
?
chitosan + H2O
chitobiose + chitotriose + chitotetraose
-
activity increases with the degree of deacetylation of chitosan. The enzyme hydrolyzes chitosan with 62-100% degree of deacetylation. Hydrolysis of chitosan with 99% degree of deacetylation by ChiN releases chitobiose, chitotriose and chitotetraose
-
-
?
chitosan + H2O
chitobiose + chitotriose + chitotetraose + chitopentaose + chitohexaose + chitoheptaose
the enzyme is an endo-type chitosanase, which cannot cleave the beta-1,4 linkage in (GlcN)2. The enzyme forms (GlcN)2 to (GlcN)7 as the main products after 30 min in the mild reaction condition. The hydrolytic products after 2 h incubation are mainly (GlcN)2, (GlcN)3, (GlcN)4 and a small quantity of (GlcN)5. There are only (GlcN)2 and (GlcN)3 detected after 6 h reaction
-
-
?
chitosan + H2O
chitobiose + chitotriose + chitotetraose + chitopentaose + chitohexaose + chitoheptaose
the enzyme is an endo-type chitosanase, which cannot cleave the beta-1,4 linkage in (GlcN)2. The enzyme forms (GlcN)2 to (GlcN)7 as the main products after 30 min in the mild reaction condition. The hydrolytic products after 2 h incubation are mainly (GlcN)2, (GlcN)3, (GlcN)4 and a small quantity of (GlcN)5. There are only (GlcN)2 and (GlcN)3 detected after 6 h reaction
-
-
?
chitosan + H2O
chitohexaose + chitopentaose + chitotetraose + chitotriose + chitobiose
-
high activity on 90% deacetylated colloidal chitosan
chitosan is hydrolyzed to chitohexaose and chitopentaose at the initial stage of the reaction, after incubation for 1 h, the amounts of chitobiose, chitotriose and chitotetraose in the hydrolysate is increased
-
?
chitosan + H2O
chitohexaose + chitopentaose + chitotetraose + chitotriose + chitobiose
Bacillus sp. (in: Bacteria) MET 1299
-
high activity on 90% deacetylated colloidal chitosan
chitosan is hydrolyzed to chitohexaose and chitopentaose at the initial stage of the reaction, after incubation for 1 h, the amounts of chitobiose, chitotriose and chitotetraose in the hydrolysate is increased
-
?
chitosan + H2O
chitopentaose + chitohexaose
-
85% deacetylated soluble chitosan is the most susceptible substrate
products after 24 h incunation at 70°C
-
?
chitosan + H2O
chitopentaose + chitohexaose
-
85% deacetylated soluble chitosan is the most susceptible substrate
products after 24 h incunation at 70°C
-
?
chitosan + H2O
chitopentaose + chitotetraose + chitotriose
about 99% deacetylated substrate
-
-
?
chitosan + H2O
chitopentaose + chitotetraose + chitotriose
about 99% deacetylated substrate
-
-
?
chitosan + H2O
chitosan oligomers
-
chitodimer and chitotrimer as main products, a monoacetyl chitodimer and a monoacetyl chitotrimer but no significant amount of monomer glucosamine or chitotetramer is identified
-
?
chitosan + H2O
chitosan oligomers
-
chitodimer and chitotrimer as main products, a monoacetyl chitodimer and a monoacetyl chitotrimer but no significant amount of monomer glucosamine or chitotetramer is identified
-
?
chitosan + H2O
chitosan oligosaccharides
the enzyme prefers to hydrolyze chitosan with high degree of deacetylation. The main products of chitiosan (92% deacetylation) are chitosan oligosaccharides with degree of polymerization (DP) ranging from 2 to 6. No activity with colloidal chitin, carboxymethylcellulose, microcrystalline cellulose, glucosan
-
-
?
chitosan + H2O
chitosan oligosaccharides
-
-
chitosan oligosaccharides comprise oligomers with degree of polymerization mainly from dimers to pentamers
-
?
chitosan + H2O
chitosan oligosaccharides
-
-
the enzyme produces various chitooligomers with different degrees of polymerisation from 3 to 8
-
?
chitosan + H2O
chitosan oligosaccharides
-
-
chitosan oligosaccharides comprise oligomers with degree of polymerization mainly from dimers to pentamers
-
?
chitosan + H2O
chitosan oligosaccharides
-
-
the enzyme produces various chitooligomers with different degrees of polymerisation from 3 to 8
-
?
chitosan + H2O
chitosan oligosaccharides
activity of the enzyme increases with an increase of the degrees of deacetylation of the chitosan substrate
-
-
?
chitosan + H2O
chitosan oligosaccharides
-
1 g of enzyme can hydrolyze about 100 kg of chitosan
-
-
?
chitosan + H2O
chitosan oligosaccharides
Bacillus sp. (in: Bacteria) KCTC 0377BP
activity of the enzyme increases with an increase of the degrees of deacetylation of the chitosan substrate
-
-
?
chitosan + H2O
chitosan oligosaccharides
-
substrate with 85% deacetylation
-
-
?
chitosan + H2O
chitosan oligosaccharides
-
substrate with 85% deacetylation
-
-
?
chitosan + H2O
chitosan oligosaccharides
-
substrate chitosan, 99% deacetylated, 67% of the activity with colloidal chitosan
-
-
?
chitosan + H2O
chitosan oligosaccharides
-
substrate colloidal chitosan, 85% deacetylated
-
-
?
chitosan + H2O
chitosan oligosaccharides
-
substrate chitosan, 99% deacetylated, 67% of the activity with colloidal chitosan
-
-
?
chitosan + H2O
chitosan oligosaccharides
-
substrate colloidal chitosan, 85% deacetylated
-
-
?
chitosan + H2O
chitosan oligosaccharides
-
substrate with average molecular weight of 220 kDA, 85% deacetylated
-
-
?
chitosan + H2O
chitosan oligosaccharides
-
-
products are a variety of oligomers
-
?
chitosan + H2O
chitosan oligosaccharides
-
substrate with average molecular weight of 220 kDA, 85% deacetylated
-
-
?
chitosan + H2O
chitosan-oligosaccharides
85% deacetylated chitin, transformants show a significant increase in chitosanase production by 2.1fold than control
-
-
?
chitosan + H2O
chitosan-oligosaccharides
catalyzes the hydrolysis of beta-1,4-glycosidic links
-
-
?
chitosan + H2O
chitotriose + chitotetraose
-
-
-
?
chitosan + H2O
D-glucosamine + ?
-
chitosan polymers with various degrees of deacetylation (10-94%) are susceptible to hydrolysis by both isoforms. Polymers with 50-70% deacetylation are most susceptible to hydrolysis by isoform A and polymers with 40-80% deacetylation are most susceptible to isoform B
-
-
?
chitosan + H2O
D-glucosamine + ?
-
hydrolysis of chitosan hexamer, chitosan substrates are 55-80% deacetylated
dimers and trimers
-
?
chitosan + H2O
GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcN
chitosan with 85% degree of deacetylation. Inserting two surface loops, the endo-type chitosanase Csn is converted into an exo-type chitosanase. The chimeric chitosanase has 3% of wild-type activity and GlcNbeta(1-4)GlcN is the dominant product, whereas a mixture of GlcNbeta(1-4)GlcN, GlcNbeta(1-4)GlcNbeta(1-4)GlcN and GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcN is obtained with the wild-type endo-chitosanase. Chimeric Csn catalyzes the hydrolysis of chitosan with a smaller rate of viscosity decrease than the wild-type
-
-
?
chitosan + H2O
GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcN
Niallia circulans MH-K1
chitosan with 85% degree of deacetylation. Inserting two surface loops, the endo-type chitosanase Csn is converted into an exo-type chitosanase. The chimeric chitosanase has 3% of wild-type activity and GlcNbeta(1-4)GlcN is the dominant product, whereas a mixture of GlcNbeta(1-4)GlcN, GlcNbeta(1-4)GlcNbeta(1-4)GlcN and GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcN is obtained with the wild-type endo-chitosanase. Chimeric Csn catalyzes the hydrolysis of chitosan with a smaller rate of viscosity decrease than the wild-type
-
-
?
chitosan heptasaccharide + H2O
chitosan pentasaccharide + chitosan disaccharide
-
-
-
-
?
chitosan heptasaccharide + H2O
chitosan pentasaccharide + chitosan disaccharide
-
-
-
-
?
chitosan heptasaccharide + H2O
chitosan tetrasaccharide + chitosan trisaccharide
-
-
-
-
?
chitosan heptasaccharide + H2O
chitosan tetrasaccharide + chitosan trisaccharide
-
-
-
-
?
chitosan hexasaccharide + H2O
chitosan disaccharide + chitosan trisaccharide + chitosan tetrasaccharide
-
-
-
-
?
chitosan hexasaccharide + H2O
chitosan disaccharide + chitosan trisaccharide + chitosan tetrasaccharide
-
-
-
-
?
chitosan hexasaccharide + H2O
chitosan tetrasaccharide + chitosan disaccharide
-
-
-
-
?
chitosan hexasaccharide + H2O
chitosan tetrasaccharide + chitosan disaccharide
-
-
-
-
?
chitosan pentasaccharide + H2O
?
-
92% deacetylated chitosan, development of a Remazol Brilliant Blue R dye-coupled, quantitative enzyme assay method, overview
-
-
?
chitosan pentasaccharide + H2O
chitosan disaccharide + chitosan trisaccharide
-
-
-
-
?
chitosan pentasaccharide + H2O
chitosan disaccharide + chitosan trisaccharide
-
hydrolysis of the chitosan oligosaccharide (GlcN)5 to (GlcN)2 and (GlcN)3
-
-
?
chitosan pentasaccharide + H2O
chitosan disaccharide + chitosan trisaccharide
-
hydrolysis of the chitosan oligosaccharide (GlcN)5 to (GlcN)2 and (GlcN)3
-
-
?
chitosan pentasaccharide + H2O
chitosan disaccharide + chitosan trisaccharide
hydrolysis of the chitosan oligosaccharide (GlcN)5 to (GlcN)2 and (GlcN)3
-
-
?
chitotetraose + H2O
?
15.0% of the activity with chitosan
-
-
?
chitotetraose + H2O
?
Bacillus sp. (in: Bacteria) KCTC 0377BP
15.0% of the activity with chitosan
-
-
?
colloidal chitin + H2O
?
-
52% activity compared to 50% deacetylated chitosan
-
-
?
colloidal chitin + H2O
?
-
5.1% of the activity with colloidal chitosan
-
-
?
colloidal chitosan + H2O
chitobiose + chitotriose + chitotetraose
85% deacetylated, Csn2 displays stronger hydrolysis capability against colloidal chitosan than soluble chitosan
-
-
?
colloidal chitosan + H2O
chitobiose + chitotriose + chitotetraose
85% deacetylated, Csn2 displays stronger hydrolysis capability against colloidal chitosan than soluble chitosan
-
-
?
Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-GlcN-beta-(1->4) + H2O
?
-
-
-
-
?
Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-GlcN-beta-(1->4) + H2O
?
-
-
-
-
?
GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN + H2O
?
-
-
-
-
?
GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN + H2O
?
-
-
-
-
?
glycol chitin + H2O
?
-
isoform A shows 29.7% activity and isoform B 14.1% activity compared to chitosan
-
-
?
glycol chitin + H2O
?
-
11% activity compared to colloidal chitosan
-
-
?
glycol chitin + H2O
?
-
11% activity compared to colloidal chitosan
-
-
?
glycol chitosan + H2O
?
weak activity against glycol chitosan, Csn2 displays 4% of the activity for colloidal chitosan
-
-
?
glycol chitosan + H2O
?
weak activity against glycol chitosan, Csn2 displays 4% of the activity for colloidal chitosan
-
-
?
glycol chitosan + H2O
?
activity is ca. 4fold higher than toward chitosan
-
-
?
glycol chitosan + H2O
?
-
hydrolysis of glycol chitosan with release of glucosamine
-
-
?
glycol chitosan + H2O
?
-
12% activity compared to colloidal chitosan
-
-
?
glycol chitosan + H2O
?
-
12% activity compared to colloidal chitosan
-
-
?
glycol chitosan + H2O
glycol chitosan oligosaccharides
-
substrate approximately 40% deacetylated, 38% of the activity with colloidal chitosan
-
-
?
glycol chitosan + H2O
glycol chitosan oligosaccharides
-
substrate approximately 40% deacetylated, 38% of the activity with colloidal chitosan
-
-
?
methylcellulose + H2O
?
14% activity compared to chitosan
-
-
?
soluble chitosan + H2O
?
-
activity decreases with the degree of deacetylation of chitosan. The enzyme hydrolyzes chitosan with 82-100% degree of deacetylation.
-
-
?
soluble chitosan + H2O
?
Bacillus sp. (in: Bacteria) TKU004
-
activity decreases with the degree of deacetylation of chitosan. The enzyme hydrolyzes chitosan with 82-100% degree of deacetylation.
-
-
?
soluble chitosan + H2O
?
85% deacetylated, Csn2 displays 14% of the activity for colloidal chitosan
-
-
?
soluble chitosan + H2O
?
85% deacetylated, Csn2 displays 14% of the activity for colloidal chitosan
-
-
?
chitohexaose + H2O
additional information
-
-
chitosanase I
-
?
chitopentaose + H2O
additional information
-
-
chitosanase I
-
?
chitopentaose + H2O
additional information
-
-
chitosanase I
-
?
chitosan + H2O
additional information
-
alpine bacterium
-
most effective with 70% deacetylated chitosan as substrate
-
-
?
chitosan + H2O
additional information
-
alpine bacterium YSK-28
-
most effective with 70% deacetylated chitosan as substrate
-
-
?
chitosan + H2O
additional information
-
-
enzyme is capable of cleaving between glucosamine and glucosamine or N-acetylglucosamine, but not cleaving between N-acetylglucosamine and glucosamine
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
the smallest of the substrates is a tetramer of glucosamine
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
most susceptible substrates are: chitohexaose and chitoheptaose
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
most susceptible substrate is: 100% deacetylated chitosan
-
-
?
chitosan + H2O
additional information
-
-
deacetylation degree from 70% to 100%
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: chitosan extracted from Mucor rouxii cell walls
mixture of dimer, trimer and higher molecular weight oligomers of glucosamine
?
chitosan + H2O
additional information
-
-
-
chitosanase I produced glucosamine, chitosanase II produced chitooligosaccharides
?
chitosan + H2O
additional information
-
-
-
chitosanase I produced glucosamine, chitosanase II produced chitooligosaccharides
?
chitosan + H2O
additional information
-
-
enzyme I prefers chitosan with 30% acetylation, but enzyme II mostly effects chitosan without acetylation
-
-
?
chitosan + H2O
additional information
-
-
enzyme I prefers chitosan with 30% acetylation, but enzyme II mostly effects chitosan without acetylation
-
-
?
chitosan + H2O
additional information
-
-
-
products from 100% deacetylated chitosan are chitobiose: 27.2%, chitotriose: 40.6% and chitotetraose: 32.2%
?
chitosan + H2O
additional information
-
-
-
products from 100% deacetylated chitosan are chitobiose: 27.2%, chitotriose: 40.6% and chitotetraose: 32.2%
?
chitosan + H2O
additional information
-
-
specificity
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
specificity
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
enzyme degrades soluble and colloidal chitosan
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: soluble chitosan
glucosamine oligomers with the degree of polymerization from 2 to 8 are produced during hydrolysis of soluble chitosan
?
chitosan + H2O
additional information
-
-
enzyme is absolutely specific towards the GlcN-GlcN bonds in partially N-acetylated chitosan and at least three GlcN residues are necessary to hydrolyze chitosan
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: glycol chitosan
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: glycol chitosan
glucosamine oligomers with the degree of polymerization from 2 to 8 are produced during hydrolysis of soluble chitosan
?
chitosan + H2O
additional information
-
-
enzyme degrades soluble and colloidal chitosan
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: glycol chitosan
-
-
?
chitosan + H2O
additional information
-
-
enzyme is absolutely specific towards the GlcN-GlcN bonds in partially N-acetylated chitosan and at least three GlcN residues are necessary to hydrolyze chitosan
-
-
?
chitosan + H2O
additional information
-
-
enzyme degrades soluble and colloidal chitosan
-
-
?
chitosan + H2O
additional information
-
Bacillus sp. (in: Bacteria) No. 7-M
-
enzyme is absolutely specific towards the GlcN-GlcN bonds in partially N-acetylated chitosan and at least three GlcN residues are necessary to hydrolyze chitosan
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: glycol chitosan
-
-
?
chitosan + H2O
additional information
-
-
degrades 60-94% deacetylated chitosan most effectively
end products of chitosan hydrolysis are chitobiose, chitotetraose and some chitooligosaccharides with a longer chain length
?
chitosan + H2O
additional information
-
-
degrades 60-94% deacetylated chitosan most effectively
end products of chitosan hydrolysis are chitobiose, chitotetraose and some chitooligosaccharides with a longer chain length
?
chitosan + H2O
additional information
-
-
most effective with 70-100% deacetylated chitosan as substrate
-
-
?
chitosan + H2O
additional information
-
-
most effective with 70-100% deacetylated chitosan as substrate
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: colloidal chitosan 80% deacetylated, not 100% deacetylated
GlcNAc4-6 and colloidal chitin are hydrolyzed to GlcNAc2
?
chitosan + H2O
additional information
-
-
hydrolysis of: colloidal chitosan 80% deacetylated, not 100% deacetylated
the main cleavage site with GlcNAc3-6 is the second linkage from the non-reducing end, based on the pattern of pNp-GlcNAc2-5
?
chitosan + H2O
additional information
-
-
hydrolysis of: colloidal chitosan 80% deacetylated, not 100% deacetylated
colloidal chitosan is hydrolyzed to GlcNAc2 and to similar partially N-acetylated chitooligosaccharides
?
chitosan + H2O
additional information
-
-
deacetylation degree from 70% to 100%
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: glycol chitosan
-
-
?
chitosan + H2O
additional information
-
-
the smallest of the substrates is a tetramer of glucosamine
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
substrates with less than 40% deacetylation are not affected by the enzyme
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
most susceptible substrate is: 80% deacetylated chitosan
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
hydrolysis of: glycol chitosan
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
Niallia circulans MH-K1
-
the smallest of the substrates is a tetramer of glucosamine
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
Niallia circulans MH-K1
-
substrates with less than 40% deacetylation are not affected by the enzyme
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
Niallia circulans MH-K1
-
most susceptible substrate is: 80% deacetylated chitosan
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
enzyme A is highly specific for chitosan, enzyme B and C possess comparable specific activities towards chitosan, chitin and cellulose
glucosamine oligomers, predominantly dimers and trimers
?
chitosan + H2O
additional information
-
-
high substrate specificity for highly deacetylated chitosan
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
high substrate specificity for highly deacetylated chitosan
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
-
chitosan of an average MW 36000 is reduced by the enzymatic catalysis to nearly one-fourth this size
?
chitosan + H2O
additional information
-
-
-
chitosan of an average MW 36000 is reduced by the enzymatic catalysis to nearly one-fourth this size
?
chitosan + H2O
additional information
-
-
hydrolysis of: soluble chitosan
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: colloidal chitosan 80% deacetylated, not 100% deacetylated
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: glycol chitosan
-
-
?
chitosan + H2O
additional information
-
-
-
diglucosamine and triglucosamine
?
chitosan + H2O
additional information
-
-
the smallest of the substrates is a tetramer of glucosamine
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
-
diglucosamine and triglucosamine
?
chitosan + H2O
additional information
-
-
most effective with 68-88% deacetylated chitosan as substrate
-
-
?
chitosan + H2O
additional information
-
-
polymers with 30% to 60% acetylation
with 60% acetylated chitosan as substrate a dimer is also found
?
chitosan + H2O
additional information
-
-
polymers with 30% to 60% acetylation
major oligomeric product from 30% acetylated chitosan is a trimer
?
chitosan + H2O
additional information
-
-
polymers with 30% to 60% acetylation
the products depend on the degree of acetylation of the polymer
?
chitosan + H2O
additional information
-
-
polymers containing equal proportions of acetylated and non-acetylated sugars are optimal for chitosanase activity
with 60% acetylated chitosan as substrate a dimer is also found
?
chitosan + H2O
additional information
-
-
polymers containing equal proportions of acetylated and non-acetylated sugars are optimal for chitosanase activity
major oligomeric product from 30% acetylated chitosan is a trimer
?
chitosan + H2O
additional information
-
-
polymers containing equal proportions of acetylated and non-acetylated sugars are optimal for chitosanase activity
the products depend on the degree of acetylation of the polymer
?
additional information
?
-
-
no activity with 50% deacetylated chitosan, 19% deacetylated colloidal chitin, carboxymethylcellulose sodium, and carboxymethyl chitosan
-
-
?
additional information
?
-
-
no activity with 50% deacetylated chitosan, 19% deacetylated colloidal chitin, carboxymethylcellulose sodium, and carboxymethyl chitosan
-
-
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
-
no activity with glucosamine dimer and trimer
-
-
?
additional information
?
-
-
degrades glucosamine tetramer to dimer and pentamer and to dimer and trimer
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze colloidal chitin or carboxymethylcellulose
-
-
?
additional information
?
-
-
the enzyme splits GlcN-GlcN and GlcNAc-GlcN bonds but not GlcNAc-GlcNAc or GlcN-GlcNAc bonds
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze colloidal chitin or carboxymethylcellulose
-
-
?
additional information
?
-
-
the enzyme splits GlcN-GlcN and GlcNAc-GlcN bonds but not GlcNAc-GlcNAc or GlcN-GlcNAc bonds
-
-
?
additional information
?
-
-
enzyme is able to catalyze the synthesis of small amounts of chitooctaose from a mixture of chitobiose to chitoheptaose oligomers, possible through transglycosylation. Pentamer and hexamer oligosaccharides are the main glycosyl acceptors
-
-
?
additional information
?
-
-
the chitosanase splits (GlcN)4GlcNOH into (GlcN)3 + (GlcN)1GlcNOH, and (GlcN)5GlcNOH into (GlcN)4 + (GlcN)1GlcNOH and (GlcN)3 + (GlcN)2GlcNOH. The heptamer (GlcN)6GlcNOH is split into (GlcN)1GlcNOH + (GlcN)5, thereafter hydrolyzed again into (GlcN)3 + (GlcN)2, or into (GlcN)4 + (GlcN)2GlcNOH, as well as (GlcN)3 + (GlcN)3GlcNOH, whereas (GlcN)1-3GlcNOH is not hydrolyzed. The monomers GlcN and GlcNOH are never detected from the enzyme reaction. Substrate specificity and product analysis, overview
-
-
?
additional information
?
-
-
the chitosanase splits (GlcN)4GlcNOH into (GlcN)3 + (GlcN)1GlcNOH, and (GlcN)5GlcNOH into (GlcN)4 + (GlcN)1GlcNOH and (GlcN)3 + (GlcN)2GlcNOH. The heptamer (GlcN)6GlcNOH is split into (GlcN)1GlcNOH + (GlcN)5, thereafter hydrolyzed again into (GlcN)3 + (GlcN)2, or into (GlcN)4 + (GlcN)2GlcNOH, as well as (GlcN)3 + (GlcN)3GlcNOH, whereas (GlcN)1-3GlcNOH is not hydrolyzed. The monomers GlcN and GlcNOH are never detected from the enzyme reaction. Substrate specificity and product analysis, overview
-
-
?
additional information
?
-
-
enzyme is able to catalyze the synthesis of small amounts of chitooctaose from a mixture of chitobiose to chitoheptaose oligomers, possible through transglycosylation. Pentamer and hexamer oligosaccharides are the main glycosyl acceptors
-
-
?
additional information
?
-
-
chitosan oligosaccharides, the enzymatic degradation products, show an inhibitory effect on growth of Pseudomonas aeruginosa, Salmonella typhimurium, Listeria monomcytogenens, Bacillus cereus, Escherichia coli, Staphylococcus aureus
-
-
?
additional information
?
-
-
no substrates: colloidal and glycol chitin
-
-
?
additional information
?
-
-
chitosan oligosaccharides, the enzymatic degradation products, show an inhibitory effect on growth of Pseudomonas aeruginosa, Salmonella typhimurium, Listeria monomcytogenens, Bacillus cereus, Escherichia coli, Staphylococcus aureus
-
-
?
additional information
?
-
-
no substrates: colloidal and glycol chitin
-
-
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
-
no activity with glycol chitin
-
-
?
additional information
?
-
-
no activity with powdered chitosan
-
-
?
additional information
?
-
-
no activity with methylcellulose
-
-
?
additional information
?
-
-
no activity with colloidal chitin
-
-
?
additional information
?
-
-
the enzyme is constitutively produced
-
-
?
additional information
?
-
-
no activity on colloidal chitin
-
-
?
additional information
?
-
no hydrolysis of chitobiose and chitotriose
-
-
?
additional information
?
-
-
no hydrolysis of chitobiose and chitotriose
-
-
?
additional information
?
-
-
the enzyme cannot hydrolyze colloidal chitin and crystalline cellulose
-
-
?
additional information
?
-
-
chitosanase has antioxidant activity. Squid pen powder is a carbon/nitrogen source for chitosanase production. Autoclave treatment of squid pen powder for 45 min remarkably promotes enzyme productivity, production of chitosanase is highest when 3% squid pen powder is used. No acitivity with chitosan (80% degree of deacetylation), chitosan (73% degree of deacetylation), chitosan (60% degree of deacetylation) and chitin (alpha-type)
-
-
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
-
no activity with glycol chitin
-
-
?
additional information
?
-
-
no activity with powdered chitosan
-
-
?
additional information
?
-
-
no activity with cellulose
-
-
?
additional information
?
-
-
no activity with methylcellulose
-
-
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) KCTC 0377BP
no hydrolysis of chitobiose and chitotriose
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) MET 1299
-
the enzyme is constitutively produced
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) MET 1299
-
no activity on colloidal chitin
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) No. 7-M
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) No. 7-M
-
no activity with glycol chitin
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) No. 7-M
-
no activity with powdered chitosan
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) No. 7-M
-
no activity with cellulose
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) No. 7-M
-
no activity with methylcellulose
-
-
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
-
the enzyme cannot hydrolyze colloidal chitin and crystalline cellulose
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) TKU004
-
chitosanase has antioxidant activity. Squid pen powder is a carbon/nitrogen source for chitosanase production. Autoclave treatment of squid pen powder for 45 min remarkably promotes enzyme productivity, production of chitosanase is highest when 3% squid pen powder is used. No acitivity with chitosan (80% degree of deacetylation), chitosan (73% degree of deacetylation), chitosan (60% degree of deacetylation) and chitin (alpha-type)
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze glycolchitosan, chitin, carboxymethyl cellulose, barley beta-glucan or phosphoric acid swollen cellulose (0.2% each)
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze glycolchitosan, chitin, carboxymethyl cellulose, barley beta-glucan or phosphoric acid swollen cellulose (0.2% each)
-
-
?
additional information
?
-
does not hydrolyze colloidal chitin and carboxylmethyl cellulose
-
-
?
additional information
?
-
does not hydrolyze colloidal chitin and carboxylmethyl cellulose
-
-
?
additional information
?
-
-
chitosanases hydrolyze the polysaccharide chitosan, which is composed of partially acetylated beta-(1,4)-linked glucosamine residues
-
-
?
additional information
?
-
-
the enzyme is specific for chitosan as substrate, no activity with colloidal chitin, insoluble cellulose, CM cellulose, beta-1,3-glucan, xylan, and arabinoxylan
-
-
?
additional information
?
-
-
at 37°C and pH 5.0, beta-1,4-glucanase activitiy is about 2.5fold higher than activity on colloidal chitosan
-
-
?
additional information
?
-
-
at 37°C and pH 5.0, beta-1,4-glucanase activitiy is about 2.5fold higher than activity on colloidal chitosan
-
-
?
additional information
?
-
-
The enzyme might be identical with a lipase that co-purifies with the chitosanase. No activity for colloidal chitin, Na-CMC and starch
-
-
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
Niallia circulans MH-K1
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
the enzyme is not active toward colloidal chitin or carboxymethyl cellulose
-
-
?
additional information
?
-
-
the enzyme is not active toward colloidal chitin or carboxymethyl cellulose
-
-
?
additional information
?
-
-
bacterial chitosanase of the GH-8 group possessing additional glucanase activity
-
-
?
additional information
?
-
-
the chitosanase from Paenibacillus fukuinensis exhibits both chitosanase and beta-1,4 glucanase activities. Glu302 is a proton acceptor for chitosanase activity, and Asn312 also participates in the hydrolysis of chitosan and cellulose
-
-
?
additional information
?
-
-
the chitosanase from Paenibacillus fukuinensis exhibits both chitosanase and beta-1,4 glucanase activities. Glu302 is a proton acceptor for chitosanase activity, and Asn312 also participates in the hydrolysis of chitosan and cellulose
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl-N-acetyl-beta-D-glucosaminide
-
-
?
additional information
?
-
Paenibacillus mucilaginosus TKU032
-
no activity with 4-nitrophenyl-N-acetyl-beta-D-glucosaminide
-
-
?
additional information
?
-
does not hydrolyze microcrystalline cellulose, chitin, xylan, laminarin, pustulan, pachyman, mannan, or beta-1,3-1,4-glucan
-
-
?
additional information
?
-
does not hydrolyze microcrystalline cellulose, chitin, xylan, laminarin, pustulan, pachyman, mannan, or beta-1,3-1,4-glucan
-
-
?
additional information
?
-
-
no substrate: carboxymethyl chitosan
-
-
?
additional information
?
-
-
no activity toward 82% deacetylated soluble chitosan, 73% deacetylated soluble chitosan, colloidal chitin, carboxymethyl cellulose, and xylan
-
-
?
additional information
?
-
-
no activity toward 82% deacetylated soluble chitosan, 73% deacetylated soluble chitosan, colloidal chitin, carboxymethyl cellulose, and xylan
-
-
?
additional information
?
-
-
no activity against colloidal chitin, chitin (a-type) and chitin (b-type). The enzyme has antioxidant activity
-
-
?
additional information
?
-
-
the enzyme shows no activity with chitosan (73% and 60% degrees of deacetylation), glycols chitosan, and alpha-chitin
-
-
?
additional information
?
-
-
no activity against colloidal chitin, chitin (a-type) and chitin (b-type). The enzyme has antioxidant activity
-
-
?
additional information
?
-
Serratia marcescens TKU019
-
the enzyme shows no activity with chitosan (73% and 60% degrees of deacetylation), glycols chitosan, and alpha-chitin
-
-
?
additional information
?
-
comparison of activities on chitosan by cellobiohydrolases, chitosanases, and lysozyme, oligomer pattern, overview. The different enzymes produce chito-oligosaccharides (COSs) with varying acetylation, NMR spectrometric analysis. The preferred cleavage site of enzyme CSN1 is between GlcN and GlcNAc
-
-
?
additional information
?
-
-
the enzyme cannot hydrolyze colloidal chitin, carboxylmethyl cellulose, diglucosamine, triglucosamine, or tetraglucosamine
-
-
?
additional information
?
-
-
the enzyme cannot hydrolyze colloidal chitin, carboxylmethyl cellulose, diglucosamine, triglucosamine, or tetraglucosamine
-
-
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
-
chitosan crosslinked with trimellitic anhydride, diisocyanatohexane, and dibromodecane show the same hydrolytic behaviour as uncrosslinked chitosan. Crosslinked chitosan species which are complexed with metals exhibits a significantly reduced extent of hydrolysis
-
-
?
additional information
?
-
the enzyme does not react with chitin. Oligosaccharides with degree of polymerization above 4 are not hydrolyzed
-
-
?
additional information
?
-
-
comparison of activities on chitosan by cellobiohydrolases, chitosanases, and lysozyme, oligomer pattern, overview. The different enzymes produce chito-oligosaccharides (COSs) with varying acetylation, NMR spectrometric analysis. The preferred cleavage site of enzyme CSN2 is between GlcN(Ac) and GlcN(Ac)
-
-
?
additional information
?
-
-
does not hydrolyze GlcNbeta(1-4)GlcN or GlcNbeta(1-4)GlcNbeta(1-4)GlcN
-
-
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
the enzyme does not react with chitin. Oligosaccharides with degree of polymerization above 4 are not hydrolyzed
-
-
?
additional information
?
-
-
the enzyme is not able to degrade chitin
-
-
?
additional information
?
-
-
the enzyme is not able to degrade chitin
-
-
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
-
slow cleavage of: pentamer of N-acetylglucosamine, glucosamine oligomers
-
-
?
additional information
?
-
-
no activity with trimers or tetramers of N-acetylglucosamine, carboxymethylcellulose, dextran, galactan, polygalacturonic acid, laminaran, mucoran, pectin, pullulan, salicin, xylan, 4-nitrophenyl-beta-D-acetylglucosamine, 4-nitrophenyl-beta-D-glucosamine
-
-
?
additional information
?
-
-
enzyme cleaves both glucosamine-glucosamine and N-acetylglucosamine-glucosamine linkages of chitosan. Enzyme additionally has cellulase activity for carboxymethylcellulose
-
-
?
additional information
?
-
catalytic residues Glu121 and Glu141 are important for the antifungal effect of the cho product
-
-
?
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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
chitosan + H2O
D-glucosamine + ?
-
chitosan polymers with various degrees of deacetylation (10-94%) are susceptible to hydrolysis by both isoforms. Polymers with 50-70% deacetylation are most susceptible to hydrolysis by isoform A and polymers with 40-80% deacetylation are most susceptible to isoform B
-
-
?
chitosan + H2O
?
-
100% activity with 50% deacetylated chitosan, 89% activity with 70% deacetylated chitosan, 91% activity with 98% deacetylated chitosan
-
-
?
chitosan + H2O
?
-
the enzyme hydrolyzes 70% deacetylated chitosan faster than fully deacetylated chitosan
-
-
?
chitosan + H2O
?
-
the enzyme hydrolyzes 70% deacetylated chitosan faster than fully deacetylated chitosan
-
-
?
chitosan + H2O
?
-
100% activity with chitosan of 60% degrees of deacetylation
-
-
?
chitosan + H2O
?
-
100% activity with chitosan of 60% degrees of deacetylation
-
-
?
chitosan + H2O
?
-
-
-
-
?
chitosan + H2O
?
-
-
-
-
?
chitosan + H2O
?
-
Chitosan, or beta-1,4-linked glucosamine, is a deacetylated derivative of chitin. The chitosanase is specific for chitosan as substrate
-
-
?
chitosan + H2O
?
-
Chitosan, or beta-1,4-linked glucosamine, is a deacetylated derivative of chitin. The chitosanase is specific for chitosan as substrate
-
-
?
chitosan + H2O
?
-
chitosanase is a glycosyl hydrolase that endolytically hydrolyzes beta-1,4-linkages between D -glucosamine residues in a partially acetylated chitosan
-
-
?
chitosan + H2O
?
the wild type chitosanase shows a clear preference for chitosan with high degrees of N-deacetylation (84-97%)
-
-
?
chitosan + H2O
chitosan oligomers
-
chitodimer and chitotrimer as main products, a monoacetyl chitodimer and a monoacetyl chitotrimer but no significant amount of monomer glucosamine or chitotetramer is identified
-
?
chitosan + H2O
chitosan oligomers
-
chitodimer and chitotrimer as main products, a monoacetyl chitodimer and a monoacetyl chitotrimer but no significant amount of monomer glucosamine or chitotetramer is identified
-
?
chitosan + H2O
chitosan oligosaccharides
-
-
chitosan oligosaccharides comprise oligomers with degree of polymerization mainly from dimers to pentamers
-
?
chitosan + H2O
chitosan oligosaccharides
-
-
the enzyme produces various chitooligomers with different degrees of polymerisation from 3 to 8
-
?
chitosan + H2O
chitosan oligosaccharides
-
-
chitosan oligosaccharides comprise oligomers with degree of polymerization mainly from dimers to pentamers
-
?
chitosan + H2O
chitosan oligosaccharides
-
-
the enzyme produces various chitooligomers with different degrees of polymerisation from 3 to 8
-
?
additional information
?
-
-
chitosan oligosaccharides, the enzymatic degradation products, show an inhibitory effect on growth of Pseudomonas aeruginosa, Salmonella typhimurium, Listeria monomcytogenens, Bacillus cereus, Escherichia coli, Staphylococcus aureus
-
-
?
additional information
?
-
-
chitosan oligosaccharides, the enzymatic degradation products, show an inhibitory effect on growth of Pseudomonas aeruginosa, Salmonella typhimurium, Listeria monomcytogenens, Bacillus cereus, Escherichia coli, Staphylococcus aureus
-
-
?
additional information
?
-
-
the enzyme is constitutively produced
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) MET 1299
-
the enzyme is constitutively produced
-
-
?
additional information
?
-
-
chitosanases hydrolyze the polysaccharide chitosan, which is composed of partially acetylated beta-(1,4)-linked glucosamine residues
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
-
activity increases about 2.5fold by the addition of 10 mM Co2+
Cu2+
K+
Mg2+
Mn2+
Na+
NaCl
-
addition of 0.001-0.5M NaCl increases the CsnM activity to 128% to 151%
Sr2+
Zn2+
additional information
Ca2+
-
chitosan degrading activity is enhanced by 15% in the presence of calcium ions (8 mM)
Ca2+
-
influences folding an stability of newly translocated protein, one weak Ca2+-binding site with a KA of 300 M-1
Mn2+
-
5 mM, 1.6fold activation of chitosanase A, 1.2fold activation of chitosanase B
Mn2+
-
activity increases about 1.4fold by the addition of 10 mM Mn2+
Mn2+
-
1 mM, 1.5fold activation of fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5), 1.9fold activation of wild-type enzyme
additional information
-
PMSF, K+, Na+, Pb2+, Mg2+, Ba2+ and Zn2+ have no effect on enzyme activity
additional information
-
not affected by Ca2+, Sr2+, Mn2+, Fe2+, Sn2+, and Zn2+
additional information
-
Ba2+ and Ca2+ show nearly no effect on relative enzymatic activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-Dinitro-1-fluorobenzene
-
isoform A shows 95% residual activity at 0.625 mM, isoform B shows 84% residual activity at 0.625 mM
2-Hydroxy-5-nitrobenzyl bromide
-
69% inhibition at 5 mM, 33% inhibition at 1 mM
Mo2+
-
94% inhibition of chitosanase I and 88% inhibition of chitosanase II
N-Acetylimidazole
-
isoform A shows 96% residual activity at 5 mM, isoform B shows 84% residual activity at 5 mM
phenylmethylsulfonyl fluoride
-
isoform B shows 86% residual activity at 2.5 mM
sulfhydryl reagents
-
glutathione or L-cysteine restores activity
Woodward's reagent K
-
N-ethyl-5-phenylisoazoline-3'-sulfonate, isoform A shows 95% residual activity at 50 mM, isoform B shows 1% residual activity at 50 mM
Ag+
-
isoform A shows 91% residual activity at 1 mM, isoform B shows 86% residual activity at 1 mM
Al3+
-
1 mM, 86.5% inhibition of fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5). 1 mM, 87% inhibition of wild-type enzyme
Ba2+
-
5 mM inhibits by 15%, in 50 mM phosphate buffer, pH 7, for 30 min at 37°C
Ca2+
-
5 mM inhibits by 10%, in 50 mM phosphate buffer, pH 7, for 30 min at 37°C
Cu2+
-
59% inhibition of chitosanase I and 48% inhibition of chitosanase II
Cu2+
-
5 mM, about 40% loss of activity of chitosanase A, about 30% loss of activity of chitosanase B
Cu2+
-
5 mM inhibits by 41%, in 50 mM phosphate buffer, pH 7, for 30 min at 37°C
Cu2+
1 mM completely inhibits, with colloidal chitosan as substrate
Cu2+
-
1 mM, complete inhibition of fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5) and of wild-type enzyme
EDTA
-
5 mM inhibits by 10%, in 50 mM phosphate buffer, pH 7, for 30 min at 37°C
Fe2+
-
5 mM, about 30% loss of activity of chitosanase A, about 25% loss of activity of chitosanase B
Fe2+
-
5 mM inhibits by 77%, in 50 mM phosphate buffer, pH 7, for 30 min at 37°C
Fe3+
-
1 mM, 11% inhibition of fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5). 1 mM, 13% inhibition of wild-type enzyme
Hg2+
-
81% inhibition of chitosanase I and 80% inhibition of chitosanase II
Hg2+
1 mM completely inhibits, with colloidal chitosan as substrate
Mg2+
-
5 mM inhibits by 14%, in 50 mM phosphate buffer, pH 7, for 30 min at 37°C
Mn2+
-
5 mM inhibits by 17%, in 50 mM phosphate buffer, pH 7, for 30 min at 37°C
N-bromosuccinimide
-
isoform A shows 12% residual activity at 2.5 mM, isoform B is completely inhibited at 2.5 mM
Ni2+
-
1 mM, 22% inhibition of fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5). 1 mM,10% inhibition of wild-type enzyme
SDS
-
2 mM of the anionic surfactant SDS completely inhibits at 25°C for 30 min
Triton X-100
-
0.5% nonionic surfactant of Triton X-100 inhibits by 56% at 25°C for 30 min
Tween 20
-
0.5% nonionic surfactant of Tween 20 inhibits by 16% at 25°C for 30 min
Tween 40
-
0.5% nonionic surfactant of Tween 40 inhibits by 29% at 25°C for 30 min
Zn2+
-
5 mM, about 30% loss of activity of chitosanase A, about 40% loss of activity of chitosanase B
Zn2+
-
5 mM inhibits by 18%, in 50 mM phosphate buffer, pH 7, for 30 min at 37°C
additional information
antifungal effect of CtoA against Rhizopus oryzae IAM6252 is drastically enhanced by the simultaneous addition of the family 19 chitinase ChiC from Streptomyces griseus
-
additional information
-
not inhibited by phenylmethylsulfonyl fluoride, TKUPSP018, TKUPSP073, TKUPSP011, TKUPSP035, TKUPSP080, and TKUPSP062
-
additional information
-
enzyme is not affected by presence of 1 M NaCl or 6 M urea
-
additional information
-
in the presence of 2% Tween 20, Tween 40, Triton X-100 (non-ionic surfactant), and 2 mM SDS (anionic surfactant), the enzyme retains almost original activity
-
additional information
-
the enzyme is very stable under incubation with EDTA, EGTA, o-phenanthroline, N-ethylmaleimide, monoiodoacetate and EDAC (5 mM each), beta-mercaptoethanol and dithiothreitol (2 mM each), N-bromosuccinimide (1 mM) and p-chloromercuribenzoate (0.1 mM)
-
additional information
-
not inhibited by diethyl dicarbonate, 1,2-cyclohexanedione, and p-hydroxymercuribenzoate
-
additional information
-
ethanol, isopropanol and dimethyl sulfoxide (5 mM -100 mM) have no effect in activity
-
additional information
1 mM Mg2+, Ca2+, Fe3+, Zn2+, Ba2+ and Pb2+ have little or no effect on activity
-
additional information
-
5 mM Ba2+, Mg2+ and Ca2+ have little effect on activity at 37°C for 30 min. After keeping at 25°C for 10 days, the chitosanase is inactivated in the presence of 25% (v/v) ethanol and ethyl ether
-
additional information
-
not influenced by 5 mM phenylmethylsulfonyl fluoride, 0.5 mM SDS, 0.5-2% (v/v) Tween 20, 0.5-2% (v/v) Tween 40, and 0.5-2% (v/v) Triton X-100
-
additional information
extent of growth inhibition is dependent on chitosan concentration, average molecular mass, the pH of the medium and salt composition. Growth inhibition can be suppressed by the expression of CsnN174 in Escherichia coli JM109
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tween 20
-
2% nonionic surfactant of Tween 20 activates by 38% at 25°C for 30 min
Triton X-100
-
2% nonionic surfactant of Triton X-100 activates by 51% at 25°C for 30 min
Tween 40
-
2% nonionic surfactant of Tween 40 activates by 6% at 25°C for 30 min
additional information
-
chitosanase is activated after keeping at 4°C for 10 days, in the presence of 25% (v/v) toluene, acetonitrile, and butanol
-
additional information
-
direct interaction of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine liposomes with membrane of Streptomyces griseus cell under heat stress at 41°C increases chitosanase production and release to 2.2times higher than that at 37°C without the 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine liposomes. Lipid mimicking cell membrane liposome under heat at 41°C in the presence of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine liposomes is 17% of initially-entrapped chitosanase while it is only 1% in the absence of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine liposomes, even under a heat stress at 41°C
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
Molecular mechanism of the alternative expression of the Chlorella virus CVK2 chitosanase gene.
Aspergillosis
Analysis of the major proteins secreted by the human opportunistic pathogen Aspergillus fumigatus under in vitro conditions.
Infections
Analysis of the major proteins secreted by the human opportunistic pathogen Aspergillus fumigatus under in vitro conditions.
Infections
CAZyme content of Pochonia chlamydosporia reflects that chitin and chitosan modification are involved in nematode parasitism.
Infections
Chitosanase purified from bacterial isolate Bacillus licheniformis of ruined vegetables displays broad spectrum biofilm inhibition.
Infections
Molecular mechanism of the alternative expression of the Chlorella virus CVK2 chitosanase gene.
Mycoses
Preparation of Active Chitooligosaccharides with a Novel Chitosanase AqCoA and Their Application in Fungal Disease Protection.
Neoplasms
Structural insights into the substrate-binding mechanism for a novel chitosanase.
Virus Diseases
Molecular mechanism of the alternative expression of the Chlorella virus CVK2 chitosanase gene.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcN
-
at pH 5.7 and 37°C
4.8
chitosan
40°C, pH not specified in the publication, mutant enzyme A207C/L286C, calculated as micromol reducing sugar liberated from chitosan
4.9
chitosan
40°C, pH not specified in the publication, wild-type enzyme, calculated as micromol reducing sugar liberated from chitosan
additional information
chitosan
-
Km-value: 0.089 mg/ml, 50°C, pH 4.5
additional information
chitosan
Km-value: 1.19 mg/ml, wild-type enzyme, pH 5.0, 50°C
additional information
chitosan
Km-value: 1.579 g/ml, mutant enzyme D318N, pH 5.0, 50°C
additional information
chitosan
Km-value: 1.97 mg/ml, 30°C, pH 5.5
additional information
chitosan
Km-value: 12.33 mg/ml, mutant enzyme D318E, pH 5.0, 50°C
additional information
chitosan
Km-value: 12.67 mg/ml, mutant enzyme D318K, pH 5.0, 50°C
additional information
chitosan
Km-value: 18.5 mg/ml, mutant enzyme D318A, pH 5.0, 50°C
additional information
chitosan
-
KM-value: 31.5 g/l, fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module AoCBM35 from Amycolatopsis orientalis (CsnA-CBM35), pH 5.6, 55°C
additional information
chitosan
-
KM-value: 42 g/l, fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module PfCBM32-2 from Paenibacillus fukuinensis (CsnA-CBM32-2), pH 5.6, 55°C
additional information
chitosan
-
KM-value: 43 g/l, fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5), pH 5.6, 55°C
additional information
chitosan
Km-value: 5 mg/ml, mutant enzyme D318R, pH 5.0, 50°C
additional information
chitosan
-
KM-value: 69 g/l, wild-type enzyme, pH 5.6, 55°C
additional information
chitosan
Km-value: 7.1 mg/ml, pH 6.0, 55°C
additional information
additional information
-
KM is 5.2 mg/ml for PSC-I, 4 mg/ml for PSC-II and 5.6 mg/ml for PSC-III
-
additional information
additional information
-
KM is 8.13 mg/ml for chitosanase A and 8.65 mg/ml for chitosanase B
-
additional information
additional information
-
2.0% glycol chitosan
-
additional information
additional information
-
0.52 mg/ml with 20.2% acetylated chitosan as substrate
-
additional information
additional information
-
0.688 mg/ml chitosan, at pH 5.5
-
additional information
additional information
-
0.688 mg/ml chitosan, at pH 5.5
-
additional information
additional information
-
0.18% carboxymethylcellulose
-
additional information
additional information
-
1.4 mg/ml: 5% or 30% acetylated chitosan
-
additional information
additional information
-
1.4 mg/ml: 5% or 30% acetylated chitosan
-
additional information
additional information
-
25 mg/ml with colloidal chitosane as substrate
-
additional information
additional information
-
Km: 3.3% soluble chitosan
-
additional information
additional information
-
KM-value for colloidal chitosan is 37.5 g/L
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
at pH 5.6, 22°C, Km value 0.8 mg per ml, isoform A
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0167
chitosan
mutant D40G/T45D, assayed as the amount of D-glucosamine released from chitosan
0.024
chitosan
mutant E36A/D40G, assayed as the amount of D-glucosamine released from chitosan
0.0368
chitosan
mutant T45E, assayed as the amount of D-glucosamine released from chitosan
0.0683
chitosan
mutant E36Q/D40G, assayed as the amount of D-glucosamine released from chitosan
0.44
chitosan
mutant D40G, assayed as the amount of D-glucosamine released from chitosan
0.9
chitosan
mutant enzyme R42K, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
1.6
chitosan
mutant enzyme R42E at 37°C in 50 mM sodium acetate buffer (pH 5.5)
2.5
chitosan
40°C, pH not specified in the publication, wild-type enzyme, calculated as micromol reducing sugar liberated from chitosan
4.9
chitosan
40°C, pH not specified in the publication, mutant enzyme A207C/L286C, calculated as micromol reducing sugar liberated from chitosan
6.827
chitosan
mutant E36N, assayed as the amount of D-glucosamine released from chitosan
8.34
chitosan
mutant E36D, assayed as the amount of D-glucosamine released from chitosan
10
chitosan
chitosan with less than 75% deacetylation, at pH 6.0 and 45°C
10.48
chitosan
mutant T45S, assayed as the amount of D-glucosamine released from chitosan
10.7
chitosan
wild type enzyme, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
11.2
chitosan
chitosan with more than 90% deacetylation, at pH 6.0 and 45°C
11.47
chitosan
mutant E36A, assayed as the amount of D-glucosamine released from chitosan
11.66
chitosan
mutant E36Q, assayed as the amount of D-glucosamine released from chitosan
12.4
chitosan
wild-type, assayed as the amount of D-glucosamine released from chitosan
20800
chitosan
-
fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module AoCBM35 from Amycolatopsis orientalis (CsnA-CBM35), pH 5.6, 55°C
30100
chitosan
-
fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module PfCBM32-2 from Paenibacillus fukuinensis (CsnA-CBM32-2), pH 5.6, 55°C
64400
chitosan
-
fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5), pH 5.6, 55°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.52
chitosan
40°C, pH not specified in the publication, wild-type enzyme, calculated as micromol reducing sugar liberated from chitosan
1.03
chitosan
40°C, pH not specified in the publication, mutant enzyme A207C/L286C, calculated as micromol reducing sugar liberated from chitosan
additional information
chitosan
Km-value: 10800 mg/s*ml, mutant enzyme D318A, pH 5.0, 50°C
additional information
chitosan
Km-value: 1630 mg/s*ml, mutant enzyme D318E, pH 5.0, 50°C
additional information
chitosan
Km-value: 1710 mg/s*ml, mutant enzyme D318K, pH 5.0, 50°C
additional information
chitosan
Km-value: 3880 mg/s*ml, mutant enzyme D318R, pH 5.0, 50°C
additional information
chitosan
Km-value: 424000 mg/s*ml, wild-type enzyme, pH 5.0, 50°C
additional information
chitosan
Km-value: 599000 mg/s*ml, mutant enzyme D318N, pH 5.0, 50°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0012
mutant enzyme D40G/R42E, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
0.002
0.018
mutant enzyme D40G/R42K, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
0.06
0.9
mutant enzyme R42E at 37°C in 50 mM sodium acetate buffer (pH 5.5)
1.4
mutant enzyme R42K, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
1.6
10
102.3
105
154.8
160
163.8
-
after Mono-S cation exchange chromatography with 0.06 to 0.08 M KCl
2.76
200
319
35.61
38.8
42.7
5.84
51.8
52.9
59.8
61.4
additional information
1.6
mutant enzyme D40G, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
52.9
wild type enzyme, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
additional information
-
between 270-290 U/mg, recombinant chitosanase
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
4.5 - 6
4.5 - 6.5
5 - 7
5.3
5.5
5.5 - 6
5.6
5.8
6.2
6.5
7.5
additional information
-
broader pH activity profile for YM20, in contrast to the pH activity profile of YM18, which shows the same pH optimum as the wild-type enzyme at pH 5.5
5
optimum pH for wild-type enzyme and mutant enzymes D318R and D318K
5.6
-
wild-type enzyme, fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5), fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module PfCBM32-2 from Paenibacillus fukuinensis (CsnA-CBM32-2) and fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module AoCBM35 from Amycolatopsis orientalis (CsnA-CBM35)
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
-
both purified isoforms A and B retain approximately 70-100% relative activity between pH 3.0 and 6.0 but rapidly lose activity above pH 6.0
3.8 - 6.5
the enzyme keeps at least 80% of activity between pH 3.8 and 6.5
4 - 6
4 - 7
-
20% of maximal activity at pH 4.0, 10% at pH 7.0, pH profile, overview
4 - 7.5
4 - 8
4 - 9
-
pH 4.0: about 75% of maximal activity, pH 9.0: about 50% of maximal activity
4.5 - 6.5
4.5 - 7
pH 4.5: about 50% of maximal activity, pH 7.0: about 50% of maximal activity
4.6 - 6
pH 4.6: about 60% of maximal activity, pH 6.0: about 50% of maximal activity
5 - 11
-
about 55% activity at pH 3.0, about 57% activity at pH 5.0, about 80% activity at pH 6.0, 100% activity at pH 9.0, about 75% activity at pH 10.0-11.0
5 - 6.3
-
pH 5.0: about 70% of maximal activity, pH 6.3: about 60% of maximal activity
7
-
above, complete loss of activity due to partial denaturation of enzyme and chitosan substrate insolubilization
additional information
-
study on the interaction of pH value with activity. Reaction rate decreases by 50% from pH 5.5 to 6.0
4 - 6
-
pH 4.0: about 45% of maximal activity, pH 6.0: about 25% of maximal activity
4 - 7.5
more than 50% activity between pH 4.0 and 7.5, more than 90% activity between pH 4.5 and 7.0
4 - 7.5
pH 4.0: about 50% of maximal activity, pH 7.5: about 40% of maximal activity
4 - 8
-
the recombinant enzyme is inactive above pH 8.0 and shows 90% of maximal activity at pH 4.0
4.5 - 6.5
pH 4.5: about 50% of maximal activity, pH 6.5: about 60% of maximal activity
6
assay at
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
40
40 - 50
45
50
55
55 - 60
60
65
70
additional information
-
release of chitosanase across lipid membrane is maximized at 41°C in comparison with that at 37°C and 45°C. Interaction of the 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine liposomes with the cell membrane, induced by heat stress at 41°C changes the surface net hydrophobicity and surface net charge of cell membrane to favorable state for the enhanced release of chitosanase
50
assay at
50
-
wild-type enzyme and fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module AoCBM35 from Amycolatopsis orientalis (CsnA-CBM35)
55
-
fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5), fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module PfCBM32-2 from Paenibacillus fukuinensis (CsnA-CBM32-2)
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 60
-
20%, 30%, and 70% of the maximum activity at 60°C, 10°C, and 30°C, respectively, maximal activity at 45°C
15 - 40
15°C: about 70% of maximal activity, 45°C: about 50% of maximal activity
15 - 50
-
15°C: 49% of maximal activity, 45°C: 96% of maximal activity, 50°C: about 45% of maximal activity
20 - 50
-
15-20% of maximal activity at 20°C, 30% at 50°C, temperature profile, overview
20 - 55
20°C: about 75% of maximal activity, 55°C: about 70% of maximal activity
27 - 50
-
about 55% activity at 27°C, about 62% activity at 32°C, 100% activity at 37°C, about 90% activity at 42°C, and about 80% activity at 50°C
30 - 50
30 - 70
-
30°C: about 45% of maximal activity, 70°C: about 40% of maximal activity, chitosanase B
35 - 60
35°C: about 30% of maximal activity, 60°C: about 50% of maximal activity
40 - 70
45 - 75
about 50% activity at 45°C, about 80% activity at 50°C, 100% activity from 55-65°C, about 80% activity at 70°C, about 50% activity at 75°C
50 - 100
-
50°C: about 50% of maximal activity, 100°C: about 40% of maximal activity
55 - 70
-
55°C: about 85% of maximal activity, 70°C: about 90% of maximal activity
30 - 50
-
about 45% activity at 30°C, about 85% activity at 35°C, 100% activity at 40°C, about 30% activity at 50°C
40 - 70
-
40°C: about 65% of maximal activity, 70°C: about 45% of maximal activity, chitosanase A
40 - 70
-
40°C: about 40% of maximal activity, 70°C: about 15% of maximal activity
40 - 70
40°C: about 50% of maximal activity, 70°C: about 60% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
4.9
8.3
8.8
9.2
3.5
-
estimated by isoelectric focusing electrophoresis on Phast-Gel IEF 3-9
3.5
-
isoelectric focusing, in plants infected either with Glomus mosseae or Glomus intraradices
9.2
-
density gradient column electrofocusing and acrylamide gel electrofocusing
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
K-1
-
-
brenda
isolated from a fresh water lake close to Kangerlussuaq in West Greenland
-
-
brenda
isoform Cel8A exhibiting both chitosanase and beta-1,4-glucanase activities
-
-
brenda
isoform Cel8A exhibiting both chitosanase and beta-1,4-glucanase activities
-
-
brenda
Niallia circulans MH-K1
-
-
-
brenda
K-1
-
-
brenda
isoform BTAL, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
brenda
isoform BTCA, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
brenda
isoform BTDM, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
brenda
isoform BTIS, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
brenda
isoform BTMO, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
brenda
isoform BTSA, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
brenda
isoform BTSO, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
brenda
isoform BTTH, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
brenda
isoform BTTO, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
brenda
three isoforms, chitosanase A, 43 kilodalton, is highly specific for chitosan and represents the major chitosan-hydrolyzing species. Chitosanases B, 39.5 kilodalton, and C, 22 kilodalton, correspond to minor activities and possess comparable specific activities toward chitosan, chitin, and cellulose
-
-
brenda
commercial preparation of cellulase, isolation of a bifunctional chitosanase/cellulase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the highest level of enzyme activity (186 U/ml) is achieved in culture medium using high cell-density cultivation in a 7-l fermenter. Chitosanase is successfully secreted to the culture media through the widely used SecB-dependent type II pathway in Escherichia coli
brenda
-
medium containing shrimp heads as the sole carbon and nitrogen source
brenda
Paenibacillus mucilaginosus TKU032
-
medium containing shrimp heads as the sole carbon and nitrogen source
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the discoidin domain of chitosanase is required for binding to the fungal cell wall
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
chitosanase is responsible for chitosan depolymerisation
metabolism
-
chitosanase is responsible for chitosan depolymerisation
-
physiological function
-
chitosanase is involved in the protection of bacteria against the antimicrobial effect of chitosan
physiological function
-
citosanase inhibits the growth of zygomycetes fungi Rhizopus and Mucor probably via its fungistatic effect
physiological function
-
chitosanase is involved in the protection of bacteria against the antimicrobial effect of chitosan
-
physiological function
Niallia circulans MH-K1
-
citosanase inhibits the growth of zygomycetes fungi Rhizopus and Mucor probably via its fungistatic effect
-
Show AA Sequence and Transmembrane Helices (2397 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10000
16000
-
x * 10000 + x * 16000 + x * 18000 + x * 20000, SDS-PAGE without reducing agent
16400
18000
19000
20000
21000
22000
23000
24000
24500
26000
27000
28000
29000
29020
30000
31000
32000
33000
35000
36000
37000
x * 37000, two discrete bands appear in SDS-PAGE: an intensely stained band showing a molecular mass of about 37 kDa and a fainter band of around 40 kDa
40000
41000
42000
43000
45000
46000
47000
50000
59000
66000
81000
10000
-
x * 10000 + x * 16000 + x * 18000 + x * 20000, SDS-PAGE without reducing agent
16400
-
x * 24500 + x * 16400, purified isoform A is composed of a major and a minor chitosanase isoform, SDS-PAGE
18000
-
x * 10000 + x * 16000 + x * 18000 + x * 20000, SDS-PAGE without reducing agent
20000
-
x * 20000, SDS-PAGE, in roots infected either with Glomus mosseae or Glomus intraradices
20000
-
x * 10000 + x * 16000 + x * 18000 + x * 20000, SDS-PAGE without reducing agent
24500
-
x * 24500 + x * 16400, purified isoform A is composed of a major and a minor chitosanase isoform, SDS-PAGE
31000
-
x * 33000, native enzyme, SDS-PAGE, x * 31000, recombinant enzyme, SDS-PAGE
33000
-
x * 33000, native enzyme, SDS-PAGE, x * 31000, recombinant enzyme, SDS-PAGE
40000
x * 40000, two discrete bands appear in SDS-PAGE: an intensely stained band showing a molecular mass of about 37000 Da and a fainter band of around 40000 Da
47000
molecular mass of recombinant chitosanase with His6-tag at the C-terminus, SDS-PAGE
50000
-
x * 50000, recombinant detagged enzymes, SDS-PAGE, x * 81000, recombinant GST-tagged enzymes, SDS-PAGE
81000
-
x * 50000, recombinant detagged enzymes, SDS-PAGE, x * 81000, recombinant GST-tagged enzymes, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 50000, recombinant detagged enzymes, SDS-PAGE, x * 81000, recombinant GST-tagged enzymes, SDS-PAGE
?
Bacillus sp. (in: Bacteria) No. 7-M
-
-
-
?
-
x * 24500 + x * 16400, purified isoform A is composed of a major and a minor chitosanase isoform, SDS-PAGE
?
-
x * 10000 + x * 16000 + x * 18000 + x * 20000, SDS-PAGE without reducing agent
?
-
x * 33000, native enzyme, SDS-PAGE, x * 31000, recombinant enzyme, SDS-PAGE
?
x * 30000-31000, analysis of the molecular mass by electrospray ionization-mass spectrometry reveals six major peaks from 30000 to 31000 Da that are related to different levels of glycosylation. The mass profile shows a dominant peak of 30772 Da with a series of surrounding peaks differing from each other by 162 Da
?
x * 37000, two discrete bands appear in SDS-PAGE: an intensely stained band showing a molecular mass of about 37 kDa and a fainter band of around 40 kDa
?
x * 40000, two discrete bands appear in SDS-PAGE: an intensely stained band showing a molecular mass of about 37000 Da and a fainter band of around 40000 Da
?
-
x * 30000-31000, analysis of the molecular mass by electrospray ionization-mass spectrometry reveals six major peaks from 30000 to 31000 Da that are related to different levels of glycosylation. The mass profile shows a dominant peak of 30772 Da with a series of surrounding peaks differing from each other by 162 Da
-
?
-
x * 37000, two discrete bands appear in SDS-PAGE: an intensely stained band showing a molecular mass of about 37 kDa and a fainter band of around 40 kDa
-
?
-
x * 40000, two discrete bands appear in SDS-PAGE: an intensely stained band showing a molecular mass of about 37000 Da and a fainter band of around 40000 Da
-
?
-
x * 20000, SDS-PAGE, in roots infected either with Glomus mosseae or Glomus intraradices
monomer
Bacillus sp. (in: Bacteria) No. 7-M
-
1 * 41000, SDS-PAGE
-
monomer
Bacillus sp. (in: Bacteria) No. 7-M
-
1 * 43000, SDS-PAGE
-
additional information
-
structure comparisons of wild-type and mutant enzymes, overview
additional information
-
the extracellular enzyme, composed of 797 amino-acid residues, has discoidin domains, DDs, also called discoidin-like domain, discoidin motif, FA58C or F5/8C, in its C-terminal region, domain structure, overview. The discoidin domain of chitosanase is required for binding to the fungal cell wall, functional analysis, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
additional information
proteolytic modification
-
sequence contains a 33-amino acid, N-terminal signal peptide and a mature enzyme
proteolytic modification
-
sequence contains a 33-amino acid, N-terminal signal peptide and a mature enzyme
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determined at 1.5 A resolution in the active form and at 2.0 A resolution in the inactive form. Hanging-drop vapor-diffusion method
-
two different crystal forms, ChoK-a and ChoK-i are obtained at pH 6.4 and pH 3.7, respectively. ChoK-a crystals belong to space group P2(1)2(1)2(1). From the unit-cell parameters, a = 70.8 A, b = 98.1 A, c = 115.8 A. The number of protein molecules in the asymmetric subunit is estimated to be two. The crystal diffracts well to 1.5 A resolution. The ChoK-i crystal belongs to space group I222, with unit-cell parameters a = 85.1 A, b = 91.1 A, c = 131.5 A. There is one molecule in the asymmetric subunit and the resolution is restricted to 2.0 A
-
in complex with hexaglucosamine, hanging drop vapor diffusion method, using 0.05 M KH2PO4 and 23% (w/v) PEG 8000 using 0.7 M NaCl as the reservoir at 15°C
sitting drop vapor diffusion method at 20°C. The crystal structure of mutant K218P reveals that the main chain and side chain structures of the loop comprising Lys218 are effected by the mutation. It is concluded that the flexible loop comprising Lys128 plays an important role in substrate binding
-
sitting drop vapour diffusion method at 20°C, orthorhombic space group P21212, two globular upper and lower domains which generate the active site cleft for the substrate binding
hanging drop crystallization with 30 mg/ml protein in 20 mM acetate, pH 5.5 mixed with 0.1 volume of a 0.5 M potassium phosphate, 20% w/v PEG 8000 solution, monoclinic space group P21
-
sitting drop vapor diffusion method, using 10% (w/v) MEPEG 5K, 300 mM tetramethylammonium chloride, and 100 mM Bis-Tris, pH 6.5, at 4°C
the substrate binding cleft is composed of six monosaccharide binding subsites
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E22Q
abolished chitosanase activity, does not exhibit antifungal activity
I13T/A87V
-
DNA shuffling of the genes from strains KNUC51 and KNUC55, the shuffled product YM18 shows higher activity than the parents at 40°C. The specific activity of YM18 is enhanced 250% compared to the parents
K66R/N352S
-
DNA shuffling of the genes from strains KNUC51 and KNUC55, the shuffled product YM20 shows higher activity than the parents at 40°C. The specific activity of YM20 is enhanced 350% compared to the parents, YM20 exhibits a shift of the optimal pH level from pH 5.5 to pH 6.5
E309R/N319E
the mutant enzyme can accept N-acetyl-D-glucosamine units at their subsite (-2), which is impossible for the wild-type enzyme
N308V/E309R/N319E
the mutant enzyme can accept N-acetyl-D-glucosamine units at their subsite (-2), which is impossible for the wild-type enzyme
D318N
mutant enzyme shows enhanced specific activity relative to wild-type chitosanase
D175E
-
48.3% of wild-type activity with acetylated chitosan as substrate (acetylation degree: 30%)
D212N
-
37.9% of wild-type activity with acetylated chitosan as substrate (acetylation degree: 30%)
E188D
-
23.6% of wild-type activity with acetylated chitosan as substrate (acetylation degree: 30%)
G151D
-
inactive. Use of strain for isolation of mutant genes with restored activity
G151D/N222S
-
mutant with restored activity based on inactive mutant G151D, 1.2 fold higher in specific activity than wild-type and 17% increase in thermal stability at 50°C
L74Q/V75I/G151D
-
mutant with restored activity based on inactive mutant G151D, 1.5fold higher in specfic activity than wild-type, and protein is efficiently secreted
G151D
-
inactive. Use of strain for isolation of mutant genes with restored activity
-
G151D/N222S
-
mutant with restored activity based on inactive mutant G151D, 1.2 fold higher in specific activity than wild-type and 17% increase in thermal stability at 50°C
-
L74Q/V75I/G151D
-
mutant with restored activity based on inactive mutant G151D, 1.5fold higher in specfic activity than wild-type, and protein is efficiently secreted
-
K218P
Y148S
K218P
Y148S
A207C/L286C
mutant enzyme has a longer half-life at 50°C (from 10.5 to 69.3 min) and a 200% higher catalytic efficiency (Kcat/Km) than that of the wild-type enzyme
G113C/D116C
at 50°C the wild-type shows less than 37% of the initial activity after 30 min, mutant enzyme G113C/D116C retains 62.0% of its initial activity
E302A
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302C
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302D
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302F
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302G
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302H
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302I
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302K
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302K/N312A
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302K/N312D
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302K/N312K
-
site-directed mutagenesis, the mutant enzyme shows no beta-1,4 glucanase activity
E302K/N312R
-
site-directed mutagenesis, the mutant enzyme shows no beta-1,4 glucanase activity
E302L
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302M
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302N
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302P
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302Q
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302R
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302R/N312A
-
site-directed mutagenesis, the mutant enzyme shows no beta-1,4 glucanase activity
E302R/N312D
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302R/N312K
-
site-directed mutagenesis, the mutant enzyme shows no beta-1,4 glucanase activity
E302R/N312R
-
site-directed mutagenesis, the mutant enzyme shows no beta-1,4 glucanase activity
E302S
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302T
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302V
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302Y
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
N312A
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
N312D
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
N312K
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
N312R
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
W228A/Y311A
the mutant shows about 30% of wild type activity
E302A
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
-
E302C
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
-
E302K
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
-
N312A
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
-
D235A
with chitohexaose the mutant enzyme shows about 10% enhanced activity as compared to wild-type enzyme
D25A
with chitohexaose as substrate the mutant enzyme shows about 10% of the activity as compared to wild-type enzyme
D40A
with polymeric substrate the mutant enzyme shows less than 10% of the activity as compared to wild-type enzyme. With chitohexaose as substrate the mutant enzyme shows about 70% of the activity as compared to wild-type enzyme
D41N
hydrolyzing activity against 100% deacetylated chitin is severely affected
D43A
with chitohexaose as substrate the mutant enzyme shows about 10% of the activity as compared to wild-type enzyme
D60E
with chitohexaose as substrate the mutant enzyme shows about 5% of the activity as compared to wild-type enzyme
D91A
with polymeric substrate the mutant enzyme shows about 10% enhanced activity as compared to wild-type enzyme. With chitohexaose as substrate the mutant enzyme shows about 70% of the activity as compared to wild-type enzyme
E120A
with polymeric substrate the mutant enzyme shows about 40% enhanced activity as compared to wild-type enzyme. With chitohexaose the mutant enzyme shows about 40% enhanced activity as compared to wild-type enzyme
E23Q
hydrolyzing activity against 100% deacetylated chitin is severely affected
E39A
with polymeric substrate the mutant enzyme shows about 50% enhanced activity as compared to wild-type enzyme
E63A
with polymeric substrate the mutant enzyme shows about 35% enhanced activity as compared to wild-type enzyme. With chitohexaose the mutant enzyme shows about 20% enhanced activity as compared to wild-type enzyme
H203A
with chitohexaose as substrate the mutant enzyme shows no activity
T58A
with chitohexaose as substrate the mutant enzyme shows about 90% of the activity as compared to wild-type enzyme
Y233A
with polymeric substrate the mutant enzyme shows less than 10% of the activity as compared to wild-type enzyme. With chitohexaose the mutant enzyme shows about 10% enhanced activity as compared to wild-type enzyme
Y37F
with chitohexaose as substrate the mutant enzyme shows about 95 % of the activity as compared to wild-type enzyme
E160A
-
mutant enzyme with decreased thermal stability and reduced specific activity
E160Q
-
mutant enzyme with decreased thermal stability and reduced specific activity
K163A
-
mutant enzyme with decreased thermal stability and reduced specific activity
T114A
-
mutant enzyme with decreased thermal stability and slightly reduced specific activity
D40G
D57A
D57N
W101F
W227F
W28F
D201A
-
time-course is almost identical to that obtained by the wild-type
D40G
D40G/T45D
reaction time is 100 min. It has 0.1% of wild-type specific activity when tested on chitosan substrate
D40G/T45E
has 0.03% of wild-type specific activity when tested on chitosan substrate
E36A/D40G
reaction time is 100 min. Kcat is ca. 18times lower than that of the single mutant D40G. Rate of (GlcN)6 degradation is enhanced by sodium azide
E36Q/D40G
reaction time is 100 min. Kcat is more than 5times lower than that of the single mutant D40G
T45E
has a very low residual activity. Activity of this mutant can not be enhanced by sodium azide
T45S
reaction time is 20 min. It is quite active, keeps ca. 71% of the specific activity of the wild-type enzyme
V148T
has 10% of wild-type activity when tested on chitosan substrate
additional information
K218P
-
mutant enzyme shows 0.16% of wild-type activity with acetylated chitosan
Y148S
-
mutant enzyme shows 12% of wild-type activity with acetylated chitosan
K218P
Niallia circulans MH-K1
-
mutant enzyme shows 0.16% of wild-type activity with acetylated chitosan
-
Y148S
Niallia circulans MH-K1
-
mutant enzyme shows 12% of wild-type activity with acetylated chitosan
-
D57A
-
mutant enzyme shows 0.5% of wild-type activity. Mutant enzyme D57A produces smaller amounts of chitobiose and chitotetraose as compared to chitotriose than does the wild-type enzyme
W101F
-
no effect to the activity in hydrolysing chitohexaose, but just 70-90% activity against 30% acetylated chitosan in contrast to the wild-type enzyme
W227F
-
no effect to the activity in hydrolysing chitohexaose, but just 70-90% activity against 30% acetylated chitosan in contrast to the wild-type enzyme
W28F
-
no effect to the activity in hydrolysing chitohexaose, but just 70-90% activity against 30% acetylated chitosan in contrast to the wild-type enzyme
D40G
reaction time is 20 min. It is distinguished from wild-type by a lower activity, without changing the mechanism of hydrolysis or the mode of interaction with substrate
additional information
-
knock down of chitosanase expression in phytopathogenic fungus Fusarium solani affects its pathogenicity
additional information
-
knock down of chitosanase expression in phytopathogenic fungus Fusarium solani affects its pathogenicity
-
additional information
chimeric chitosanase produced by inserting two peptide loops, each containing a cysteine residue, in opposite walls of the substrate-binding cleft. The two cysteine residues form a disulfide bond crossing the protruding loop, which may alter the binding topology of the substrate and consequently convert the endo-chitosanase into an exo-type enzyme
additional information
Niallia circulans MH-K1
-
chimeric chitosanase produced by inserting two peptide loops, each containing a cysteine residue, in opposite walls of the substrate-binding cleft. The two cysteine residues form a disulfide bond crossing the protruding loop, which may alter the binding topology of the substrate and consequently convert the endo-chitosanase into an exo-type enzyme
-
additional information
-
establishing of a recombinant expression of the enzyme at the cell surface of Saccharomyces cerevisiae strain MT8-1 cells, using a yeast cell surface-displaying system, to facilitate enzyme purification
additional information
-
mutational analysis of discoidin domain function
additional information
-
establishing of a recombinant expression of the enzyme at the cell surface of Saccharomyces cerevisiae strain MT8-1 cells, using a yeast cell surface-displaying system, to facilitate enzyme purification
-
additional information
-
the fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5) exhibits higher chitosan binding capacity and catalytic activity than wild-type enzyme. The fusion of BgCBM5 significantly improves the thermostability of citosanase CsnA
additional information
-
immobilization of chitosanase onto liposome for construction of a biocatalyst, the immobilized enzyme on liposomes shows increased activity and stability to pH and temperature, overview
additional information
-
consensus enzyme mutant designed by multiple amino acid substitutions. Increase in transition temperature
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 9
-
the enzyme is stable and retains more than 80% of its original activity from pH 1.0-9.0 after 15 min
731499
3 - 7
3.5 - 8
the enzyme retains 100% activity after 1 h in the pH range 3.5-8.0
731521
4 - 7
4 - 8
5 - 7
-
the enzyme is relatively stable at pH 5.0-7.0, retaining around 80% of initial activity for 30 min
731582
5 - 8
5 - 9
5.5 - 9
5.8 - 7.9
-
the enzyme retains over 80% of its original activity after incubation at pH ranging from 5.83 to 7.92 at 4°C for 24 h
751631
5.5 - 9
-
the enzyme is stable in the pH range of 5.5-9.0 for up to 12 h
731138
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 90
-
the enzyme is stable over a temperature range of 0-50°C and shows about 20% of the initial activity after heating at 90°C for 10 min
10
-
most stable at 10°C, stability of chitosanase I droppes at higher temperatures and most activity is lost above 60°C
100
20
25 - 40
25 - 50
30
30 - 60
30 - 80
37
40
40 - 50
-
its half-life is only several min at 60°C. At lower temperatures, the enzyme is quite stable, its half-life is extended to several hours at 50 and 40°C. No detectable activity loss at room temperature for several days
40 - 60
-
the purified chitosanase is continuously thermostable at 40°C and the stability is gradually decreased when the temperature is increased to 50°C but rapidly decreases at 60°C
45
45 - 55
-
the enzyme is gradually inactivated during incubation at temperature above 45°C and is completely inactivated at 55°C after 15 min, at 55°C this instability is abolished in the presence of reaction products chitotriose and chitotetraose (2.5 mM each). The residual activities of the enzyme after 1 h of incubation at 60°C with 10 mM chitotriose or chitotetraose are 35.5% and 59.5%, respectively
5 - 30
-
in absence of substrate the chitosanase is stable between 5°C and 30°C
50
50 - 55
half-lives of Csn2 at 50°C and 55°C are 30 min and 11 min, respectively
55
57.8
-
T50-value, fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5)
60
60 - 80
-
the chitosanase maintains its initial activity at less than 60°C, the chitosanase is inactivated completely at 80°C
65
70
70 - 85
the half-life of the enzyme at 70°C in the presence of chitosan substrate is more than 20 h. Maximal activity is observed at 80°C for 10 min and at 85°C for 5 and 3 min incubation times
75
80
80 - 100
the enzyme has half-lives of 2.5 h at 80°C, 1 h at 90°C and 32 min at 100°C. Almost full enzyme activity remains after 1 h at 80°C, 30 min at 90°C and 10 min at 100°C
81.1
-
consensus mutant, transition temperature in presence of chitosan at 6 g/l
83.3
-
mutant A104L, transition temperature in presence of chitosan at 6 g/l
85.1
-
mutant K164R, transition temperature in presence of chitosan at 6 g/l
90
-
half-life 16.7 min, but enzyme retains activity for up to 8 h in presence of 1 mM MnCl2
100
-
the enzyme recovers 95.2%, 89.1% and 88.1% of its initial activity after boiling for 5, 10 and 20 min, respectively
25 - 40
-
maintains its initial activity from 25 to 40°C but is completely inactivated at 80°C
25 - 40
-
maintains its initial activity, has almost half of its activity at 50°C but is completely inactivated at 70°C
25 - 50
-
the enzyme is stable between 25 and 50°C, maintains its initial activity from 25 to 40°C and has 50% of its activity at 50°C, and is inactivated at 80°C
25 - 50
-
maintains more than 90% of its initial activity between 25 and 50°C, but is rapidly inactivated retaining only 60% of its initial activity at 60°C, and is completely inactivated at greater than 70°C
30 - 60
-
more than 90% of the initial activities are retained after incubation at 30, 40, 50, and 60°C for 30 min
30 - 80
-
after 15 min incubation the enzyme shows 100% activity at 30°C, about 90% at 40°C, about 85% at 50°C, about 82% at 60°C, about 80% at 70°C, about 60% at 80°C, about 40° at 90°C, and about 20% activity at 100°C
30 - 80
-
isoform A is stable between 30 and 80°C, whereas isoform B is stable between 30 and 50°C after 60 min incubation
50
-
the recombinant chitosanase is stable at temperatures up to 50°C above which the enzyme activity decreases rapidly
50
-
1 h, 25% residual activity for wild-type, 27% residual activity for mutant L74Q/V75I/G151D, 42% residual activity for mutant G151D/N222S
50
30 min, wild-type shows less than 37% of the initial activity, mutant enzyme G113C/D116C retains 62.0% of its initial activity, mutant enzyme A207C//L286C retains 81.0% of its initial activity
65
-
1 h, wild-type enzyme and fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5) retain 37% activity. Complete loss of activity of fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module PfCBM32-2 from Paenibacillus fukuinensis (CsnA-CBM32-2) and fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module AoCBM35 from Amycolatopsis orientalis (CsnA-CBM35)
70
-
the recombinant chitosanase shows hardly activity after 30 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
acetone, n-butanol and ethylacetate rapidly denature the enzyme
-
heat treatment leads at a concentration of 0.0106 mM protein at 75°C to a irreversible unfolding, but this is reversible when the protein concentation is 20 times lower
-
the enzyme retaines 70% activity after incubation with 10 M urea at room temperature for 30 min
the hydrogen-bond network around Glu160 plays important roles in stabilization of the enzyme
-
unfolding and refolding kinetics with urea are both monophasic half-life for unfolding in 6 M urea is 78.8 s and in 1.75 M urea 73.7 s
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DMSO
Ethanol
Methanol
propanol
DMSO
-
relativly stable at the concentration of 30% at 37°C for 30 min
DMSO
-
relativly stable at the concentration of 30% at 37°C for 30 min
-
DMSO
-
relativly stable at the concentration of 30% at 37°C for 30 min
-
Ethanol
-
relative stable at the concentration of 30% at 37°C for 30 min
Ethanol
-
relative stable at the concentration of 30% at 37°C for 30 min
-
Ethanol
-
relative stable at the concentration of 30% at 37°C for 30 min
-
Methanol
-
relative stable at the concentration of 30% at 37°C for 30 min
Methanol
-
relative stable at the concentration of 30% at 37°C for 30 min
-
Methanol
-
relative stable at the concentration of 30% at 37°C for 30 min
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, stable for 8 weeks, 25% loss of activity after 16 weeks, 55% loss of activity after 20 weeks
-
25°C, the chitosanase is inactivated in the presence of 25% (v/v) ethanol and ethyl ether, 10 days
-
5°C, stable for 6 weeks, 35% loss of activity after 16 weeks, 90% loss of activity after 20 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a one-step purification process using expanded bed adsorption followed by statistical optimization and validation is performed
-
acetone precipitation, Q-Sepharose column chromatography, Hi-Trap Q column chromatography, and hydroxyapatite chromatography
-
ammonium sulfate precipitation, DEAE Sepharose column chromatography, and Sephacryl S-100 gel filtration
-
ammonium sulfate precipitation, DEAE-Sepharose CL-6B column chromatography and Sephacryl S-100 gel filtration
-
ammonium sulfate precipitation, DEAE-Sepharose CL-6B column chromatography, and Sephacryl S-100 gel filtration
-
ammonium sulfate precipitation, HiPrep Q column chromatography, and Superdex 75 gel filtration
-
by a combination of ion-exchange and gel-filtration, 50fold with an overall activity yield of 24%
-
by a two-step procedure involving ion exchange chromatography followed by gel filtration, to purity
-
by gel filtration, about 527fold with overall activity yield of 20%, to homogeneity
-
by two consecutive anion exchange chromatography steps and subsequent reverse-phase column chromatography, to homogeneity, 65fold with a yield of 1.7%
chimeric chitosanase and wild-type Csn purified nearly to homogeneity by cation-exchange chromatography
CM-Toyopearl 650 M column chromatography and Resource S column chromatography
-
glutathione-Sepharose 4B bead chromatography, and Sephacryl S-100 gel filtration
isolation of a bifunctional chitosanase/cellulase from commercial prepapration of cellulase
-
native enzyme 23fold from mycelium by bacitracin affinity chromatography and gel filtration
-
purification is enhanced by expanded bed adsorption chromatography using Doehlert design
-
Q-Sepharose column chromatography and hydroxyapatite column chromatography
recombinant enzyme from Streptomyces lividans strain TK24 by ion exchange and hydroxylapatite chromatography
-
recombinant GST-tagged shuffled mutant enzymes Y18 and Y20 from EScherichia coli strain BL231(DE3) by glutathione affinity chromatography. The tags are cleaved off by thrombin
-
recombinant protein
to homogeneity by immobilized metal-ion affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amplified DNA fragment ligated into a pGEM T-easy vector, subsequently subcloned from the T-vector into a pET vector, expressed as 6 x His tag fused at its N-terminal in the Escherichia coli strain BL21(DE3) as a soluble and active form
-
chimeric chitosanase and wild-type Csn overexpressed from vector pET22b(+) in Escherichia coli strain BL21 (DE3)
csn gene under control of the Aspergillus nidulans gpdA promoter and Aspergillus nidulans trpC terminator, introduced back into the Fusarium solani genome by Agrobacterium tumefaciens-mediated transformation, and usage of the herbicide-resistance gene bar from Streptomyces hygroscopicus as selection marker. Construction of a vector based on pCAMBIA 1300, overexpression in Fusarium solani 0114
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Saccharomyces cerevisiae strain BY4741/sed1DELTA
expressed in Streptomyces lividans strain TK24 and Escherichia coli Gold cells
expression in Escherichia coli
expression in Streptomyces lividans TK24
expression of CsnN174 in Escherichia coli JM109. T45S chitosanase mutant introduced into Streptomyces lividans
expression of GST-tagged shuffled mutant enzymes Y18 and Y20 in Escherichia coli strain BL21(DE3)
-
gene cho, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109
overexpression of Csn1 in Fusarium solani strain T2 using transformation by Agrobacterium tumefaciens strain LBA 4404 and expression vector pCIR
-
overexpression of wild-type enzyme and mutant enzymes E122Q, D183N and E309Q in Escherichia coli
-
subcloning and library construction in Escherichia coli strain DH5alpha, expression of the enzyme in Saccharomyces cerevisiae cells displayed at the cell surface, expression of wild-type and mutant enzymes in Saccharomyces cerevisiae
-
the enzyme is expressed recombinantly as a periplasmic enzyme in Escherichia coli strain BMS172
-
the mature CsnW2 protein is fused to His-tag at C-terminus and expressed in Pichia pastoris X-33
wild-type and mutant overexpressed from vector pET15b/CSO2 in Escherichia coli BL21(DE3)
wild-type and mutants overexpressed in Brevibacillus choshinensis HDP31-M3 carrying the cto1 gene on expression plasmid vector pNCMO2
wild-type and mutants subcloned into vector pFD666 and expressed in Streptomyces lividans TK-24
-
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of chitosan or glucosamine into culture medium induces the chitosanase expression
-
enzyme expression is not induced using chitosan as a carbon source
the chitosanase is suppressed by the simultaneously existing protease which also shows the maximum activity at the third day of incubation with shrimp shell as the sole carbon/nitrogen source
the enzyme's chitosanase and antifungal activities are induced significantly under of growth-limiting conditions of 8 of light and 16 h of darkness
the highest chitosanase activity is observed with fructose, and it shows high activity with other substrates such as lactose, galactose, maltose, and glucose as well
the chitosanase is suppressed by the simultaneously existing protease which also shows the maximum activity at the third day of incubation with shrimp shell as the sole carbon/nitrogen source
-
the chitosanase is suppressed by the simultaneously existing protease which also shows the maximum activity at the third day of incubation with shrimp shell as the sole carbon/nitrogen source
Serratia marcescens TKU019
-
-
the highest chitosanase activity is observed with fructose, and it shows high activity with other substrates such as lactose, galactose, maltose, and glucose as well
-
the highest chitosanase activity is observed with fructose, and it shows high activity with other substrates such as lactose, galactose, maltose, and glucose as well
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
biotechnology
food industry
industry
medicine
the chitosanase has promising benefit as antibiofilm agent against biofilm forming pathogenic bacteria and has promising application as alternative antibiofilm agents to combat the growing number of multidrug resistant pathogen-associated infections, especially in situation where biofilms are involved
pharmacology
synthesis
agriculture
Pedobacter sp. PR-M6
-
oligochitosan produced with Pedobacter sp. PR-M6 chitosanase is a potential agents for an antifungal activity against phytopathogens in field
agriculture
partially acetylated chitosan oligosaccharides have various potential applications in agriculture, biomedicine, and pharmaceutics due to their suitable bioactivities. A more promising approach is enzymatic depolymerization of chitosan using chitinases or chitosanases, as the substrate specificity of the enzyme determines the composition of the oligomeric products
analysis
development of a simple plate assay based on hydrolysis of soluble chitosan, for high-throughput screening for enzyme activity
analysis
-
fluorimetric determination of transition temperature is a reliable method for rapid assessment of the thermal behaviour of chitosanases and applicable to structure-function studies
analysis
-
fluorimetric determination of transition temperature is a reliable method for rapid assessment of the thermal behaviour of chitosanases and applicable to structure-function studies
biotechnology
-
chitosanase is used as a tool for the biotechnological transformation of chitosan
biotechnology
-
chitosanase is used as a tool for the biotechnological transformation of chitosan
-
food industry
-
has potential in the production of functional foods
food industry
-
usage of strain TKU011 on the microbial reclamation of food processing wastes such as shrimp shell wastes for the production of chitosanase
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
-
chitosanase from Paenibacillus mucilaginosus TKU032 may have potential applications in production of bioactive chitosan oligosaccharides for the food and pharmaceutical industries
food industry
partially acetylated chitosan oligosaccharides have various potential applications in agriculture, biomedicine, and pharmaceutics due to their suitable bioactivities. A more promising approach is enzymatic depolymerization of chitosan using chitinases or chitosanases, as the substrate specificity of the enzyme determines the composition of the oligomeric products
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
-
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
-
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
-
food industry
-
usage of strain TKU011 on the microbial reclamation of food processing wastes such as shrimp shell wastes for the production of chitosanase
-
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
-
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
-
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
-
food industry
Bacillus sp. (in: Bacteria) TKU004
-
has potential in the production of functional foods
-
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
-
food industry
Paenibacillus mucilaginosus TKU032
-
chitosanase from Paenibacillus mucilaginosus TKU032 may have potential applications in production of bioactive chitosan oligosaccharides for the food and pharmaceutical industries
-
industry
-
a cheap chitosanase for large-scale chitosan oligosaccharide production in industry
industry
-
the enzyme has a great potential for industrial applications due to its high yield and broad pH stability
industry
-
the fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5) exhibits higher chitosan binding capacity and catalytic activity than wild-type enzyme and improved thermostability. The hybrid enzyme is a useful candidate for industrial application
industry
the high yield of the extracellular overexpression, relevant thermostability, and effective hydrolysis of commercial grade chitosan shows that this recombinant enzyme has a great potential for industrial applications
pharmacology
-
chitosanase from Paenibacillus mucilaginosus TKU032 may have potential applications in production of bioactive chitosan oligosaccharides for the food and pharmaceutical industries
pharmacology
partially acetylated chitosan oligosaccharides have various potential applications in agriculture, biomedicine, and pharmaceutics due to their suitable bioactivities. A more promising approach is enzymatic depolymerization of chitosan using chitinases or chitosanases, as the substrate specificity of the enzyme determines the composition of the oligomeric products
pharmacology
Paenibacillus mucilaginosus TKU032
-
chitosanase from Paenibacillus mucilaginosus TKU032 may have potential applications in production of bioactive chitosan oligosaccharides for the food and pharmaceutical industries
-
synthesis
valuable enzyme for the commercial production of chitosan oligosaccharides and other chitosan hydrolysates
synthesis
-
enhancement of enzyme production from 3.6 U/ml to 118 U/ml by substrate induction, statistical optimization of medium composition and culture conditions with colloidal chitosan being the best inducer and carbon source for chitosanase production
synthesis
-
enzyme is able to catalyze the synthesis of small amounts of chitooctaose from a mixture of chitobiose to chitoheptaose oligomers, possible through transglycosylation. Carrying out this process in reversed micellar microreactors formed by sodium bis-2(ethylhexyl) sulfosuccinate in isooctane significantly increases formation of high degree polymerized chitooligosaccharides. Pentamer and hexamer oligosaccharides are the main glycosyl acceptors
synthesis
-
expression in yeast cells as a whole-cell biocatalyst. Protein is localized to cell surface
synthesis
-
optimization of production conditions. In the optimized medium, strain JG produces 0.8 mmol per min and l of enzymic activity in 72 h
synthesis
chitosanases can be used to produce partially acetylated chitosan oligosaccharides for different applications
synthesis
chitosanases can be used to produce partially acetylated chitosan oligosaccharides for different applications
synthesis
-
chitosanases can be used to produce partially acetylated chitosan oligosaccharides for different applications
synthesis
the enzyme can be a competitive candidate for chitosan oligosaccharide-manufacturing industry
synthesis
the enzyme is a good candidate for production of beta-D-GlcN-(1->4)-beta-D-GlcN
synthesis
-
optimization of production conditions. In the optimized medium, strain JG produces 0.8 mmol per min and l of enzymic activity in 72 h
-
synthesis
-
enzyme is able to catalyze the synthesis of small amounts of chitooctaose from a mixture of chitobiose to chitoheptaose oligomers, possible through transglycosylation. Carrying out this process in reversed micellar microreactors formed by sodium bis-2(ethylhexyl) sulfosuccinate in isooctane significantly increases formation of high degree polymerized chitooligosaccharides. Pentamer and hexamer oligosaccharides are the main glycosyl acceptors
-
synthesis
-
enhancement of enzyme production from 3.6 U/ml to 118 U/ml by substrate induction, statistical optimization of medium composition and culture conditions with colloidal chitosan being the best inducer and carbon source for chitosanase production
-
synthesis
Bacillus sp. (in: Bacteria) KCTC 0377BP
-
valuable enzyme for the commercial production of chitosan oligosaccharides and other chitosan hydrolysates
-
synthesis
Niallia circulans MH-K1
-
chitosanases can be used to produce partially acetylated chitosan oligosaccharides for different applications
-
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Release 2023.1 (January 2023)
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