Information on EC 3.2.1.132 - chitosanase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
3.2.1.132
-
RECOMMENDED NAME
GeneOntology No.
chitosanase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
Biosynthesis of secondary metabolites
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AsChi
-
-
AsChi
Aeromonas sp. HG08
-
-
-
ChA
Penicillium sp. ZD-Z1
-
-
-
ChiN
Microbacterium sp. QU01
-
-
-
chitosanase 1
Q8KZM5
-
ChiX
Microbacterium sp. QU01
-
-
-
Cho-GG
Bacillus thuringiensis JAM-GG01
-
-
-
ChoK
Bacillus sp. K17
-
;
-
Chs1
Q8KZM5
-
Chs1
Pseudomonas sp. TKU015
Q8KZM5
-
-
Csn1
Fusarium solani 114
-
-
-
Csn2
Gongronella sp.
B0LV85
-
Csn2
B0LV85
-
-
CtoA
Amycolatopsis sp.CsO-2
Q9LBG4
-
endo-chitosanase
-
-
endo-chitosanase
-
-
endo-chitosanase
-
-
endochitosanase
-
-
family 46 chitosanase
Amycolatopsis sp.CsO-2
Q9LBG4
-
GH-75 chitosanase
Gongronella sp.
B0LV85
-
GH-75 chitosanase
B0LV85
-
-
MH-K1 chitosanase
-
-
mschito
A7KBW5
-
mschito
A7KBW5
-
-
N174 chitosanase
-
-
PgChP
Penicillium chrysogenum AS51D
D7R809
-
-
MH-K1 chitosanase
Bacillus circulans MH-K1
-
-
-
additional information
C9D7S2
the enzyme belongs to the glycoside hydrolase 3, GH3-like family of Anabaena variabilis ATCC 29413
additional information
-
the enzyme belongs to the glycohydrolase family 8
additional information
-
the chitosanase is related to the glycosyl hydrolase family 46 chitosanases
additional information
-
the enzyme belongs to the glycohydrolase family 8, GH8
CAS REGISTRY NUMBER
COMMENTARY
51570-20-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Acinetobacter sp. C-17
C-17
-
-
Manually annotated by BRENDA team
strain HG08
-
-
Manually annotated by BRENDA team
Aeromonas sp. HG08
strain HG08
-
-
Manually annotated by BRENDA team
alpine bacterium
strain YSK-28
-
-
Manually annotated by BRENDA team
alpine bacterium YSK-28
strain YSK-28
-
-
Manually annotated by BRENDA team
Amycolatopsis sp.CsO-2
-
UniProt
Manually annotated by BRENDA team
RPAN1, gene cho
UniProt
Manually annotated by BRENDA team
Aspergillus fumigatus KB-1
KB-1
-
-
Manually annotated by BRENDA team
Aspergillus fumigatus KH-94
KH-94
-
-
Manually annotated by BRENDA team
Aspergillus oryzae IAM2660
IAM2660
-
-
Manually annotated by BRENDA team
strain D-11
-
-
Manually annotated by BRENDA team
strain NTU-FC-4
-
-
Manually annotated by BRENDA team
strains KNUC51 and KNUC55, genes csn
-
-
Manually annotated by BRENDA team
Bacillus cereus D-11
strain D-11
-
-
Manually annotated by BRENDA team
Bacillus cereus NTU-FC-4
strain NTU-FC-4
-
-
Manually annotated by BRENDA team
Bacillus cereus S1
S1
-
-
Manually annotated by BRENDA team
Bacillus circulans MH-K1
-
Uniprot
Manually annotated by BRENDA team
Bacillus circulans MH-K1
MH-K1
-
-
Manually annotated by BRENDA team
Bacillus circulans MH-K1
MH-K1
Uniprot
Manually annotated by BRENDA team
strain MB-2
-
-
Manually annotated by BRENDA team
Bacillus licheniformis MB-2
strain MB-2
-
-
Manually annotated by BRENDA team
; 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
-
-
Manually annotated by BRENDA team
Bacillus pumilus Bn-262
Bn-262
-
-
Manually annotated by BRENDA team
739; K-1
-
-
Manually annotated by BRENDA team
CK4; K-1
-
-
Manually annotated by BRENDA team
HW-002; K-1
-
-
Manually annotated by BRENDA team
K-1; No. 7-M
-
-
Manually annotated by BRENDA team
K-1; No. 7-M; PI-7S; R-4
-
-
Manually annotated by BRENDA team
K-1; P16
-
-
Manually annotated by BRENDA team
K-1; PI-7S
-
-
Manually annotated by BRENDA team
K-1; R-4
-
-
Manually annotated by BRENDA team
strain K17
-
-
Manually annotated by BRENDA team
strain KCTC 0377BP
SwissProt
Manually annotated by BRENDA team
strain MET 1299
-
-
Manually annotated by BRENDA team
strain S65
-
-
Manually annotated by BRENDA team
Bacillus sp. 739
739
-
-
Manually annotated by BRENDA team
Bacillus sp. HW-002
HW-002
-
-
Manually annotated by BRENDA team
Bacillus sp. K17
strain K17
-
-
Manually annotated by BRENDA team
strain KCTC 0377BP
SwissProt
Manually annotated by BRENDA team
Bacillus sp. MET 1299
strain MET 1299
-
-
Manually annotated by BRENDA team
Bacillus sp. No. 7-M
No. 7-M
-
-
Manually annotated by BRENDA team
Bacillus sp. PI-7S
PI-7S
-
-
Manually annotated by BRENDA team
Bacillus sp. R-4
R-4
-
-
Manually annotated by BRENDA team
Bacillus sp. S65
strain S65
-
-
Manually annotated by BRENDA team
Bacillus sp. TKU004
-
-
-
Manually annotated by BRENDA team
Bacillus subtilis CH2
-
-
-
Manually annotated by BRENDA team
Bacillus subtilis GM9804
GM9804
-
-
Manually annotated by BRENDA team
Bacillus subtilis IMR-NK1
IMR-NK1
-
-
Manually annotated by BRENDA team
isoform BTAL, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
Manually annotated by BRENDA team
isoform BTCA, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
Manually annotated by BRENDA team
isoform BTDM, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
Manually annotated by BRENDA team
isoform BTIS, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
A9P7G0
SwissProt
Manually annotated by BRENDA team
isoform BTMO, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
Manually annotated by BRENDA team
isoform BTSA, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
Manually annotated by BRENDA team
isoform BTSO, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
A9P7G1
SwissProt
Manually annotated by BRENDA team
isoform BTTH, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
SwissProt
Manually annotated by BRENDA team
isoform BTTO, analysis of 29 different serovar strains, identification of nine genes encoding chitosanases with very similar properties
A9P7G3
SwissProt
Manually annotated by BRENDA team
Bacillus thuringiensis JAM-GG01
-
-
-
Manually annotated by BRENDA team
strain CHB101
-
-
Manually annotated by BRENDA team
Burkholderia gladioli CHB101
strain CHB101
-
-
Manually annotated by BRENDA team
Ficus sp.
-
-
-
Manually annotated by BRENDA team
f. sp. phaseoli SUF386
-
-
Manually annotated by BRENDA team
strain 0114, gene csn1
-
-
Manually annotated by BRENDA team
Fusarium solani 114
strain 0114, gene csn1
-
-
Manually annotated by BRENDA team
Gongronella sp.
-
UniProt
Manually annotated by BRENDA team
Gongronella sp.
strain JG
-
-
Manually annotated by BRENDA team
commercial preparation of cellulase, isolation of a bifunctional chitosanase/cellulase
-
-
Manually annotated by BRENDA team
isolated from a fresh water lake close to Kangerlussuaq in West Greenland
-
-
Manually annotated by BRENDA team
strain IB-9374, isoform Cel8A exhibiting both chitosanase and beta-1,4-glucanase activities
-
-
Manually annotated by BRENDA team
strain IB-9374, isoform Cel8A exhibiting both chitosanase and beta-1,4-glucanase activities
-
-
Manually annotated by BRENDA team
Macrotermes estherae
workers, soldiers, males, winged females
-
-
Manually annotated by BRENDA team
strain OU01
-
-
Manually annotated by BRENDA team
strain OU01
SwissProt
Manually annotated by BRENDA team
strain QU01, chitosanase ChiN; strain QU01, chitosanase ChiX
-
-
Manually annotated by BRENDA team
strain OU01
SwissProt
Manually annotated by BRENDA team
Microbacterium sp. QU01
strain QU01, chitosanase ChiN; strain QU01, chitosanase ChiX
-
-
Manually annotated by BRENDA team
Mitsuaria chitosanitabida 3001
strain 3001
-
-
Manually annotated by BRENDA team
Paenibacillus fukuinensis D2
strain D2
-
-
Manually annotated by BRENDA team
chitosanase preprotein
UniProt
Manually annotated by BRENDA team
Penicillium chrysogenum AS51D
chitosanase preprotein
UniProt
Manually annotated by BRENDA team
Penicillium islandicum
-
-
-
Manually annotated by BRENDA team
strain ZD-Z1, isoform ChA
-
-
Manually annotated by BRENDA team
Penicillium sp. ZD-Z1
strain ZD-Z1, isoform ChA
-
-
Manually annotated by BRENDA team
Pseudomonas sp. H-14
H-14
-
-
Manually annotated by BRENDA team
Pseudomonas sp. TKU015
-
UniProt
Manually annotated by BRENDA team
Rhodosporidium toruloides CFR-1
CFR-1
-
-
Manually annotated by BRENDA team
Serratia marcescens subsp. sakuensis TKU019
-
-
-
Manually annotated by BRENDA team
Serratia marcescens TKU011
-
-
-
Manually annotated by BRENDA team
roots colonized by Glomus mosseae or Glomus intraradices
-
-
Manually annotated by BRENDA team
strain strain A3
-
-
Manually annotated by BRENDA team
Streptomyces griseus HUT6037
HUT6037
-
-
Manually annotated by BRENDA team
isolated from soil
-
-
Manually annotated by BRENDA team
N174; No. 6
-
-
Manually annotated by BRENDA team
strain 174
-
-
Manually annotated by BRENDA team
Streptomyces sp. 174
strain 174
-
-
Manually annotated by BRENDA team
Streptomyces sp. No. 6
No. 6
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
chitosanase is responsible for chitosan depolymerisation
physiological function
-
chitosanase is involved in the protection of bacteria against the antimicrobial effect of chitosan
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl beta-chitotrioside + H2O
4-methylumbelliferyl + chitotriose + chitobiose + 4-methylumbelliferyl beta-chitose
show the reaction diagram
-
-
-
-
?
acetylated chitosan + H2O
?
show the reaction diagram
Bacillus circulans, Streptomyces sp., Bacillus circulans MH-K1
-
-
-
-
?
beta-chitin + H2O
?
show the reaction diagram
Serratia marcescens subsp. sakuensis, Serratia marcescens subsp. sakuensis TKU019
-
85% activity with chitin (beta-type) compared to chitosan (95% DD)
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
Bacillus sp., Bacillus sp. S65
-
5.3% of the activity with soluble chitosan
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
not
-
-
-
carboxymethylcellulose + H2O
?
show the reaction diagram
-
not
-
-
-
carboxymethylcellulose + H2O
?
show the reaction diagram
-
not
-
-
-
carboxymethylcellulose + H2O
?
show the reaction diagram
Penicillium islandicum
-
not
-
-
-
carboxymethylcellulose + H2O
?
show the reaction diagram
-
not
-
-
-
carboxymethylcellulose + H2O
?
show the reaction diagram
-
slow cleavage
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
substrate for isoforms B, C
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
Streptomyces sp. No. 6
-
not
-
-
-
carboxymethylcellulose + H2O
?
show the reaction diagram
-
not
-
-
-
carboxymethylcellulose + H2O
?
show the reaction diagram
Bacillus circulans MH-K1
-
not
-
-
-
carboxymethylcellulose + H2O
?
show the reaction diagram
Bacillus sp. No. 7-M
-
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
Bacillus cereus S1
-
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
Bacillus sp. PI-7S
-
not
-
-
-
carboxymethylcellulose + H2O
?
show the reaction diagram
Bacillus sp. PI-7S, Bacillus sp. R-4
-
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
Bacillus sp. K-1
-
not
-
-
-
carboxymethylcellulose + H2O
?
show the reaction diagram
Bacillus sp. K-1
-
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethylchitosan + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethylchitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitin (beta-type) + H2O
?
show the reaction diagram
Bacillus sp., Bacillus sp. TKU004
-
2% relative activity
-
-
?
chitin + H2O
?
show the reaction diagram
-
-
-
-
?
chitin + H2O
?
show the reaction diagram
-
substrate for isoform B, C
-
-
?
chitobiose + H2O
glucosamine
show the reaction diagram
-
chitosanase II
-
-
?
chitohexaose + H2O
?
show the reaction diagram
-
-
-
-
?
chitohexaose + H2O
?
show the reaction diagram
Q9ALZ1
20.0% of the activity with chitosan
-
-
?
chitohexaose + H2O
?
show the reaction diagram
-
ChiN hydrolyzes oligomers larger than chitopentaose
-
-
?
chitohexaose + H2O
?
show the reaction diagram
Q9ALZ1
20.0% of the activity with chitosan
-
-
?
chitohexaose + H2O
?
show the reaction diagram
Microbacterium sp. QU01
-
ChiN hydrolyzes oligomers larger than chitopentaose
-
-
?
chitohexaose + H2O
chitobiose + chitotriose + chitotetraose
show the reaction diagram
-
-
mutant enzyme D57A produces smaller amounts of chitobiose and chitotetraose as compared to chitotriose than does the wild-type enzyme
-
?
chitopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Penicillium islandicum
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
alpine bacterium
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Macrotermes estherae
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
activity increases with the degree of deacetylation of chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
-
degree of acetylation is 30%
-
-
?
chitosan + H2O
?
show the reaction diagram
-
chitosan of approximately 100 kDa and degree of deacetylation 96%
-
-
?
chitosan + H2O
?
show the reaction diagram
-
specific substrate, isoform A
-
-
?
chitosan + H2O
?
show the reaction diagram
-
activity decreases with the degree of deacetylation of chitosan. The enzyme hydrolyzes chitosan with 60-95% degree of deacetylation
-
-
?
chitosan + H2O
?
show the reaction diagram
Q8KZM5
activity toward 94% deacetylated soluble chitosan, 85% deacetylated soluble chitosan, and 73% deacetylated soluble chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
Amycolatopsis sp.CsO-2
Q9LBG4
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
?
show the reaction diagram
-
Chitosan, or beta-1,4-linked glucosamine, is a deacetylated derivative of chitin. The chitosanase is specific for chitosan as substrate
-
-
?
chitosan + H2O
?
show the reaction diagram
-
chitosanase is a glycosyl hydrolase that endolytically hydrolyzes beta-1,4-linkages between D -glucosamine residues in a partially acetylated chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
partially acetylated chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
-
soluble chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
the chitosanase is specific for chitosan as substrate
-
-
?
chitosan + H2O
?
show the reaction diagram
-
100% activity with chitosan (95% degree of deacetylation), 26% activity with chitosan (85% degree of deacetylation)
-
-
?
chitosan + H2O
?
show the reaction diagram
D7R809, -
the enzyme liberates a mean of 0.6 mM D-glucosamine per microgram of protein in 4 h reaction
-
-
?
chitosan + H2O
?
show the reaction diagram
alpine bacterium YSK-28
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus subtilis CH2
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Streptomyces sp. No. 6
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus pumilus Bn-262
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. S65
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Serratia marcescens TKU011
-
activity decreases with the degree of deacetylation of chitosan. The enzyme hydrolyzes chitosan with 60-95% degree of deacetylation
-
-
?
chitosan + H2O
?
show the reaction diagram
Aspergillus fumigatus KB-1
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus circulans MH-K1
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Pseudomonas sp. TKU015
Q8KZM5
activity toward 94% deacetylated soluble chitosan, 85% deacetylated soluble chitosan, and 73% deacetylated soluble chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
Pseudomonas sp. H-14
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. No. 7-M
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. K17
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. HW-002
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Aspergillus fumigatus KH-94
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Penicillium chrysogenum AS51D
D7R809
the enzyme liberates a mean of 0.6 mM D-glucosamine per microgram of protein in 4 h reaction
-
-
?
chitosan + H2O
?
show the reaction diagram
Fusarium solani 114
-
Chitosan, or beta-1,4-linked glucosamine, is a deacetylated derivative of chitin. The chitosanase is specific for chitosan as substrate, the chitosanase is specific for chitosan as substrate
-
-
?
chitosan + H2O
?
show the reaction diagram
Streptomyces sp. 174
-
chitosan of approximately 100 kDa and degree of deacetylation 96%
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus cereus S1
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Acinetobacter sp. C-17
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Burkholderia gladioli CHB101
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. PI-7S
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. R-4
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. 739
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Aeromonas sp. HG08
-
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
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus subtilis GM9804
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Rhodosporidium toruloides CFR-1
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Streptomyces griseus HUT6037
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Microbacterium sp. QU01
-
activity increases with the degree of deacetylation of chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. K-1
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Aspergillus oryzae IAM2660
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Serratia marcescens subsp. sakuensis TKU019
-
100% activity with chitosan (95% degree of deacetylation), 26% activity with chitosan (85% degree of deacetylation)
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
chitobiose + chitotriose + chitotetraose
show the reaction diagram
-
-
-
-
?
chitosan + H2O
chitobiose + chitotriose + chitotetraose
show the reaction diagram
Microbacterium sp., Microbacterium sp. QU01
-
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
chitohexaose + chitopentaose + chitotetraose + chitotriose + chitobiose
show the reaction diagram
Bacillus sp., Bacillus sp. 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
chitosan oligosaccharides
show the reaction diagram
-
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
-
products are a variety of oligomers
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Q9ALZ1
activity of the enzyme increases with an increase of the degrees of deacetylation of the chitosan substrate
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
substrate chitosan, 99% deacetylated, 67% of the activity with colloidal chitosan, substrate colloidal chitosan, 85% deacetylated
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Gongronella sp.
-
substrate with 85% deacetylation
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
substrate with average molecular weight of 220 kDA, 85% deacetylated
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
1 g of enzyme can hydrolyze about 100 kg of chitosan
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
substrate with 85% deacetylation
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
substrate chitosan, 99% deacetylated, 67% of the activity with colloidal chitosan, substrate colloidal chitosan, 85% deacetylated
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Penicillium sp. ZD-Z1
-
-
-
-
?
chitosan + H2O
chitotriose + chitotetraose + chitopentaose
show the reaction diagram
-
-
major hydrolytic products
-
?
chitosan + H2O
low molecular weight chitosan polymers + chitosan oligomers
show the reaction diagram
Ficus sp.
-
most effectively hydrolyzes chitosan polymers that are 52-70% deacetylated
-
-
?
chitosan + H2O
chitopentaose + chitohexaose
show the reaction diagram
Bacillus licheniformis, Bacillus licheniformis MB-2
-
85% deacetylated soluble chitosan is the most susceptible substrate
products after 24 h incunation at 70C
-
?
chitosan + H2O
chitopentaose + chitotetraose + chitotriose
show the reaction diagram
A7KBW5
about 99% deacetylated substrate
-
-
?
chitosan + H2O
chitotriose + chitotetraose
show the reaction diagram
-
-
-
-
?
chitosan + H2O
chitotriose + chitotetraose
show the reaction diagram
A9P7F5, A9P7F6, A9P7F7, A9P7F8, A9P7F9, A9P7G0, A9P7G1, A9P7G2, A9P7G3, -
-
-
-
?
chitosan + H2O
chitotriose + chitotetraose
show the reaction diagram
Bacillus thuringiensis JAM-GG01
-
-
-
-
?
chitosan + H2O
glucosamine oligomer + N-acetyl-glucosamine oligomer
show the reaction diagram
-
-
hydrolysates are oligomers with one to four glucosamine residues and some oligomers with longer chain length
-
?
chitosan + H2O
chitosan-oligosaccharides
show the reaction diagram
A9QUB2
85% deacetylated chitin, transformants show a significant increase in chitosanase production by 2.1fold than control
-
-
?
chitosan + H2O
chitosan-oligosaccharides
show the reaction diagram
P33665
catalyzes the hydrolysis of beta-1,4-glycosidic links
-
-
?
chitosan + H2O
GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcN
show the reaction diagram
P33673
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
glucosamine
show the reaction diagram
-
hydrolysis of chitosan hexamer, chitosan substrates are 55-80% deacetylated
dimers and trimers
-
?
chitosan heptasaccharide + H2O
chitosan pentasaccharide + chitosan disaccharide
show the reaction diagram
Bacillus cereus, Bacillus cereus D-11
-
-
-
-
?
chitosan heptasaccharide + H2O
chitosan tetrasaccharide + chitosan trisaccharide
show the reaction diagram
Bacillus cereus, Bacillus cereus D-11
-
-
-
-
?
chitosan hexasaccharide + H2O
chitosan disaccharide + chitosan trisaccharide + chitosan tetrasaccharide
show the reaction diagram
Bacillus cereus, Bacillus cereus NTU-FC-4
-
-
-
-
?
chitosan hexasaccharide + H2O
chitosan tetrasaccharide + chitosan disaccharide
show the reaction diagram
Bacillus cereus, Bacillus cereus D-11
-
-
-
-
?
chitosan hexasaccharide + H2O
chitosan trisaccharide
show the reaction diagram
Bacillus cereus, Bacillus cereus D-11
-
-
-
-
?
chitosan pentasaccharide + H2O
?
show the reaction diagram
-
-, 92% deacetylated chitosan, development of a Remazol Brilliant Blue R dye-coupled, quantitative enzyme assay method, overview
-
-
?
chitosan pentasaccharide + H2O
chitosan disaccharide + chitosan trisaccharide
show the reaction diagram
-
-
-
-
?
chitosan pentasaccharide + H2O
chitosan disaccharide + chitosan trisaccharide
show the reaction diagram
-
hydrolysis of the chitosan oligosaccharide (GlcN)5 to (GlcN)2 and (GlcN)3
-
-
?
chitosan pentasaccharide + H2O
chitosan disaccharide + chitosan trisaccharide
show the reaction diagram
-, C9D7S2
hydrolysis of the chitosan oligosaccharide (GlcN)5 to (GlcN)2 and (GlcN)3
-
-
?
chitosan pentasaccharide + H2O
chitosan disaccharide + chitosan trisaccharide
show the reaction diagram
Bacillus cereus NTU-FC-4
-
hydrolysis of the chitosan oligosaccharide (GlcN)5 to (GlcN)2 and (GlcN)3
-
-
?
chitotetraose + H2O
chitobiose
show the reaction diagram
-
-
-
?
chitotetraose + H2O
chitobiose
show the reaction diagram
-
-
-
-
?
chitotetraose + H2O
chitobiose
show the reaction diagram
Bacillus cereus S1
-
-
-
?
chitotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
chitotetraose + H2O
?
show the reaction diagram
Q9ALZ1
15.0% of the activity with chitosan
-
-
?
chitotriose + H2O
?
show the reaction diagram
-
-
-
-
?
colloidal chitin + H2O
?
show the reaction diagram
-
-
-
-
?
colloidal chitin + H2O
?
show the reaction diagram
-
-
-
-
?
colloidal chitin + H2O
?
show the reaction diagram
-
-
-
-
?
colloidal chitin + H2O
?
show the reaction diagram
-
-
-
-
?
colloidal chitin + H2O
?
show the reaction diagram
-
5.1% of the activity with colloidal chitosan
-
-
?
colloidal chitin + H2O
?
show the reaction diagram
Bacillus sp., Bacillus sp. TKU004
-
6% relative activity
-
-
?
colloidal chitin + H2O
?
show the reaction diagram
-
5.1% of the activity with colloidal chitosan
-
-
?
colloidal chitin + H2O
?
show the reaction diagram
Bacillus subtilis IMR-NK1
-
-
-
-
?
colloidal chitosan + H2O
?
show the reaction diagram
Q8KZM5
100% deacetylated chitin
-
-
?
colloidal chitosan + H2O
chitobiose + chitotriose + chitotetraose
show the reaction diagram
Gongronella sp., Gongronella sp. JG-2005
B0LV85
85% deacetylated, Csn2 displays stronger hydrolysis capability against colloidal chitosan than soluble chitosan
-
-
?
GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcN + H2O
GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcNbeta(1-4)GlcN + D-glucosamine
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
glycol chitin + H2O
?
show the reaction diagram
-
-
-
-
?
glycol chitin + H2O
?
show the reaction diagram
-
-
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
Q8KZM5
activity is ca. 4fold higher than toward chitosan
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
Gongronella sp.
B0LV85
weak activity against glycol chitosan, Csn2 displays 4% of the activity for colloidal chitosan
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
-
hydrolysis of glycol chitosan with release of glucosamine
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
Paenibacillus fukuinensis D2
-
-
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
Aspergillus fumigatus KH-94
-
-
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
B0LV85
weak activity against glycol chitosan, Csn2 displays 4% of the activity for colloidal chitosan
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
Bacillus sp. CK4, Bacillus sp. K-1
-
-
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
Bacillus subtilis IMR-NK1
-
-
-
-
?
glycol chitosan + H2O
glycol chitosan oligosaccharides
show the reaction diagram
-
-
-
-
?
glycol chitosan + H2O
glycol chitosan oligosaccharides
show the reaction diagram
-
-
-
-
?
glycol chitosan + H2O
glycol chitosan oligosaccharides
show the reaction diagram
-
substrate approximately 40% deacetylated, 38% of the activity with colloidal chitosan
-
-
?
glycol chitosan + H2O
glycol chitosan oligosaccharides
show the reaction diagram
Bacillus licheniformis MB-2
-
-
-
-
?
glycol chitosan + H2O
glycol chitosan oligosaccharides
show the reaction diagram
-
substrate approximately 40% deacetylated, 38% of the activity with colloidal chitosan
-
-
?
N,N'',N'''-triacetylchitotriose + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-chitooligosaccharides + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetylated chitosan + H2O
?
show the reaction diagram
Q8KZM5
activity is ca. 3fold less than toward chitosan
-
-
?
shrimp-shell powder + H2O
?
show the reaction diagram
Serratia marcescens, Serratia marcescens TKU011
-
sole carbon/nitrogen source
-
-
?
soluble chitosan + H2O
?
show the reaction diagram
Gongronella sp.
B0LV85
85% deacetylated, Csn2 displays 14% of the activity for colloidal chitosan
-
-
?
soluble chitosan + H2O
?
show the reaction diagram
Bacillus sp., Bacillus sp. TKU004
-
activity decreases with the degree of deacetylation of chitosan. The enzyme hydrolyzes chitosan with 82-100% degree of deacetylation.
-
-
?
soluble chitosan + H2O
?
show the reaction diagram
B0LV85
85% deacetylated, Csn2 displays 14% of the activity for colloidal chitosan
-
-
?
water-soluble chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
substrate 40-50% deacetylated, 7.6% of the activity with colloidal chitosan
-
-
?
chitoheptaose + H2O
?
show the reaction diagram
Q9ALZ1
23.8% of the activity with chitosan
-
-
?
chitohexaose + H2O
additional information
-
-
-
-
?
chitohexaose + H2O
additional information
-
-
-
-
-
chitohexaose + H2O
additional information
-
-
-
-
-
chitohexaose + H2O
additional information
-
Aspergillus fumigatus, Aspergillus fumigatus KH-94
-
chitosanase I
-
-
chitopentaose + H2O
?
show the reaction diagram
Q9ALZ1
16.8% of the activity with chitosan
-
-
?
chitopentaose + H2O
additional information
-
-
-
-
?
chitopentaose + H2O
additional information
-
-
-
-
-
?
chitopentaose + H2O
additional information
-
-
-
-
-
?
chitopentaose + H2O
additional information
-
Aspergillus fumigatus, Aspergillus fumigatus KH-94
-
chitosanase I
-
?
chitopentaose + H2O
additional information
-
Bacillus cereus S1
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus subtilis IMR-NK1
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
Macrotermes estherae
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
-
-
products from 100% deacetylated chitosan are chitobiose: 27.2%, chitotriose: 40.6% and chitotetraose: 32.2%
?
chitosan + H2O
additional information
-
-
-
chitosanase I produced glucosamine, chitosanase II produced chitooligosaccharides
?
chitosan + H2O
additional information
-
-
-
diglucosamine and triglucosamine
?
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
-
-
specificity
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
enzyme degrades soluble and colloidal chitosan
-
-
?
chitosan + H2O
additional information
-
-
most effective with 68-88% deacetylated chitosan as substrate
-
-
?
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
-
-
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
-
-
the smallest of the substrates is a tetramer of 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
-
alpine bacterium
-
most effective with 70% deacetylated chitosan as substrate
-
-
?
chitosan + H2O
additional information
-
-
most effective with 70-100% deacetylated chitosan as substrate
-
-
?
chitosan + H2O
additional information
-
-
most susceptible substrates are: chitohexaose and chitoheptaose
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
hydrolysis of: soluble 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 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
-
-
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
-
Penicillium islandicum
-
polymers with 30% to 60% acetylation
with 60% acetylated chitosan as substrate a dimer is also found, major oligomeric product from 30% acetylated chitosan is a trimer, the products depend on the degree of acetylation of the polymer
?
chitosan + H2O
additional information
-
-
enzyme I prefers chitosan with 30% acetylation, but enzyme II mostly effects chitosan without acetylation
-
-
?
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
-
-
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: 100% deacetylated chitosan
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: colloidal chitosan 80% deacetylated, not 100% deacetylated
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: colloidal chitosan 80% deacetylated, not 100% deacetylated
GlcNAc4-6 and colloidal chitin are hydrolyzed to GlcNAc2, the main cleavage site with GlcNAc3-6 is the second linkage from the non-reducing end, based on the pattern of pNp-GlcNAc2-5, colloidal chitosan is hydrolyzed to GlcNAc2 and to similar partially N-acetylated chitooligosaccharides
?
chitosan + H2O
additional information
-
-
most susceptible substrate is: 80% deacetylated chitosan
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
Penicillium islandicum
-
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, major oligomeric product from 30% acetylated chitosan is a trimer, the products depend on the degree of acetylation of the polymer
?
chitosan + H2O
additional information
-
-
deacetylation degree from 70% to 100%
-
-
?
chitosan + H2O
additional information
-
-
deacetylation degree from 70% to 100%
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: glycol chitosan
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: glycol 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
-
-
hydrolysis of: glycol chitosan
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
alpine bacterium YSK-28
-
most effective with 70% deacetylated chitosan as substrate
-
-
?
chitosan + H2O
additional information
-
Streptomyces sp. No. 6
-
-
diglucosamine and triglucosamine
?
chitosan + H2O
additional information
-
Streptomyces sp. No. 6
-
-
-
-
?
chitosan + H2O
additional information
-
Bacillus pumilus Bn-262
-
specificity
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
Aspergillus fumigatus KB-1
-
-
chitosanase I produced glucosamine, chitosanase II produced chitooligosaccharides
?
chitosan + H2O
additional information
-
Bacillus circulans MH-K1
-
the smallest of the substrates is a tetramer of glucosamine, substrates with less than 40% deacetylation are not affected by the enzyme
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
Bacillus circulans MH-K1
-
-
-
-
?
chitosan + H2O
additional information
-
Pseudomonas sp. H-14
-
high substrate specificity for highly deacetylated chitosan
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
Pseudomonas sp. H-14
-
-
-
-
?
chitosan + H2O
additional information
-
Bacillus sp. 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
-
Bacillus sp. No. 7-M
-
-
-
-
?
chitosan + H2O
additional information
-
Bacillus sp. HW-002
-
-
-
-
?
chitosan + H2O
additional information
-
Aspergillus fumigatus KH-94
-
-
-
-
?
chitosan + H2O
additional information
-
Bacillus cereus S1
-
-
products from 100% deacetylated chitosan are chitobiose: 27.2%, chitotriose: 40.6% and chitotetraose: 32.2%
?
chitosan + H2O
additional information
-
Acinetobacter sp. C-17
-
-
-
-
?
chitosan + H2O
additional information
-
Burkholderia gladioli CHB101
-
most effective with 70-100% deacetylated chitosan as substrate
-
-
?
chitosan + H2O
additional information
-
Bacillus sp. PI-7S
-
-
-
-
?
chitosan + H2O
additional information
-
Bacillus sp. R-4
-
hydrolysis of: glycol chitosan
-
-
?
chitosan + H2O
additional information
-
Bacillus sp. R-4
-
-
-
-
?
chitosan + H2O
additional information
-
Bacillus sp. 739
-
-
-
-
?
chitosan + H2O
additional information
-
-
enzyme degrades soluble and colloidal chitosan
-
-
?
chitosan + H2O
additional information
-
Rhodosporidium toruloides CFR-1
-
-
chitosan of an average MW 36000 is reduced by the enzymatic catalysis to nearly one-fourth this size
?
chitosan + H2O
additional information
-
Streptomyces griseus HUT6037
-
-
-
-
?
chitosan + H2O
additional information
-
Bacillus sp. K-1
-
hydrolysis of: glycol chitosan
-
-
?
chitosan + H2O
additional information
-
Bacillus sp. K-1
-
-
-
-
?
chitosan + H2O
additional information
-
Bacillus sp. K-1
-
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
-
Bacillus sp. K-1
-
enzyme degrades soluble and colloidal chitosan
-
-
?
chitosan + H2O
additional information
-
Bacillus sp. K-1
-
-
-
-
?
chitosan + H2O
additional information
-
Aspergillus oryzae IAM2660
-
enzyme I prefers chitosan with 30% acetylation, but enzyme II mostly effects chitosan without acetylation
-
-
?
chitosan + H2O
additional information
-
-
-
-
-
?
chitosan + H2O
additional information
-
Bacillus subtilis IMR-NK1
-
degrades 60-94% deacetylated chitosan most effectively
end products of chitosan hydrolysis are chitobiose, chitotetraose and some chitooligosaccharides with a longer chain length
?
hexa-N-acetylchitohexaose + H2O
?
show the reaction diagram
-
-
-
-
?
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 chitin (i.e. 100% acetylated chitosan)
-
-
-
additional information
?
-
Penicillium islandicum
-
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 glycol chitin
-
-
-
additional information
?
-
-
no activity with powdered chitosan
-
-
-
additional information
?
-
-
no activity with glucosamine dimer and trimer
-
-
-
additional information
?
-
-
no activity with cellulose
-
-
-
additional information
?
-
Penicillium islandicum
-
slow cleavage of: pentamer of N-acetylglucosamine, glucosamine oligomers
-
-
-
additional information
?
-
-
no activity with methylcellulose
-
-
-
additional information
?
-
Penicillium islandicum
-
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
?
-
-
degrades glucosamine tetramer to dimer and pentamer and to dimer and trimer
-
-
-
additional information
?
-
-
no activity with colloidal chitin
-
-
-
additional information
?
-
-
no activity with colloidal chitin
-
-
-
additional information
?
-
Penicillium islandicum
-
no activity with colloidal chitin
-
-
-
additional information
?
-
-
the enzyme is constitutively produced, no activity on colloidal chitin
-
-
-
additional information
?
-
Q9ALZ1
no hydrolysis of chitobiose and chitotriose
-
-
-
additional information
?
-
-
the enzyme cannot hydrolyze colloidal chitin and crystalline cellulose
-
-
-
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
?
-
-
at 37C and pH 5.0, beta-1,4-glucanase activitiy is about 2.5fold higher than activity on colloidal 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
?
-
-
enzyme cleaves both glucosamine-glucosamine and N-acetylglucosamine-glucosamine linkages of chitosan. Enzyme additionally has cellulase activity for carboxymethylcellulose
-
-
-
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
?
-
-
no substrate: carboxymethyl chitosan
-
-
-
additional information
?
-
-
no substrates: colloidal and glycol chitin
-
-
-
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
?
-
Gongronella sp.
B0LV85
does not hydrolyze colloidal chitin and carboxylmethyl cellulose
-
-
-
additional information
?
-
-
does not hydrolyze GlcNbeta(1-4)GlcN or GlcNbeta(1-4)GlcNbeta(1-4)GlcN
-
-
-
additional information
?
-
-
no activity against colloidal chitin, chitin (a-type) and chitin (b-type). The enzyme has antioxidant activity
-
-
-
additional information
?
-
Q8KZM5
no activity toward 82% deacetylated soluble chitosan, 73% deacetylated soluble chitosan, colloidal chitin, carboxymethyl cellulose, and xylan
-
-
-
additional information
?
-
-
chitosanases hydrolyze the polysaccharide chitosan, which is composed of partially acetylated beta-(1,4)-linked glucosamine residues
-
-
-
additional information
?
-
-
bacterial chitosanase of the GH-8 group possessing additional glucanase activity
-
-
-
additional information
?
-
-, C9D7S2
catalytic residues Glu121 and Glu141 are important for the antifungal effect of the cho product
-
-
-
additional information
?
-
-
hydrolysis profiles, overview
-
-
-
additional information
?
-
-
no activity with 50% deacetylated chitosan, 19% deacetylated colloidal chitin, carboxymethylcellulose sodium, and carboxymethyl chitosan
-
-
-
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 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 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
?
-
-
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
?
-
-
the enzyme does not hydrolyze glycolchitosan, chitin, carboxymethyl cellulose, barley beta-glucan or phosphoric acid swollen cellulose (0.2% each)
-
-
-
additional information
?
-
-
the enzyme shows no activity with chitosan (73% and 60% degrees of deacetylation), glycols chitosan, and alpha-chitin
-
-
-
additional information
?
-
Streptomyces sp. No. 6
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
-
additional information
?
-
Bacillus cereus NTU-FC-4
-
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
?
-
Bacillus cereus NTU-FC-4
-
hydrolysis profiles, overview
-
-
-
additional information
?
-
Bacillus thuringiensis JAM-GG01
-
the enzyme does not hydrolyze glycolchitosan, chitin, carboxymethyl cellulose, barley beta-glucan or phosphoric acid swollen cellulose (0.2% each)
-
-
-
additional information
?
-
Bacillus cereus D-11
-
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
?
-
Paenibacillus fukuinensis D2
-
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 chitin (i.e. 100% acetylated chitosan), no activity with glucosamine dimer and trimer, degrades glucosamine tetramer to dimer and pentamer and to dimer and trimer
-
-
-
additional information
?
-
Bacillus sp. S65
-
the enzyme cannot hydrolyze colloidal chitin and crystalline cellulose
-
-
-
additional information
?
-
Serratia marcescens TKU011
-
no activity against colloidal chitin, chitin (a-type) and chitin (b-type). The enzyme has antioxidant activity
-
-
-
additional information
?
-
Bacillus circulans MH-K1
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
-
additional information
?
-
Q9ALZ1
no hydrolysis of chitobiose and chitotriose
-
-
-
additional information
?
-
Pseudomonas sp. TKU015
Q8KZM5
no activity toward 82% deacetylated soluble chitosan, 73% deacetylated soluble chitosan, colloidal chitin, carboxymethyl cellulose, and xylan
-
-
-
additional information
?
-
Bacillus sp. No. 7-M
-
no activity with chitin (i.e. 100% acetylated chitosan), no activity with glycol chitin, no activity with powdered chitosan, no activity with cellulose, no activity with methylcellulose
-
-
-
additional information
?
-
Bacillus licheniformis MB-2
-
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, no substrates: colloidal and glycol chitin
-
-
-
additional information
?
-
Bacillus sp. 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
?
-
B0LV85
does not hydrolyze colloidal chitin and carboxylmethyl cellulose
-
-
-
additional information
?
-
Bacillus sp. PI-7S
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
-
additional information
?
-
-
at 37C and pH 5.0, beta-1,4-glucanase activitiy is about 2.5fold higher than activity on colloidal chitosan
-
-
-
additional information
?
-
Bacillus sp. MET 1299
-
the enzyme is constitutively produced, no activity on colloidal chitin
-
-
-
additional information
?
-
Aeromonas sp. HG08
-
no activity with 50% deacetylated chitosan, 19% deacetylated colloidal chitin, carboxymethylcellulose sodium, and carboxymethyl chitosan
-
-
-
additional information
?
-
Bacillus sp. K-1
-
no activity with chitin (i.e. 100% acetylated chitosan), no activity with glycol chitin, no activity with powdered chitosan, no activity with cellulose, no activity with methylcellulose
-
-
-
additional information
?
-
Bacillus sp. K-1
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
-
additional information
?
-
Penicillium sp. ZD-Z1
-
no substrate: carboxymethyl chitosan
-
-
-
additional information
?
-
Serratia marcescens subsp. sakuensis TKU019
-
the enzyme shows no activity with chitosan (73% and 60% degrees of deacetylation), glycols chitosan, and alpha-chitin
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Penicillium islandicum
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
alpine bacterium
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Macrotermes estherae
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
Chitosan, or beta-1,4-linked glucosamine, is a deacetylated derivative of chitin. The chitosanase is specific for chitosan as substrate
-
-
?
chitosan + H2O
?
show the reaction diagram
-
chitosanase is a glycosyl hydrolase that endolytically hydrolyzes beta-1,4-linkages between D -glucosamine residues in a partially acetylated chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
alpine bacterium YSK-28
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Streptomyces sp. No. 6
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus pumilus Bn-262
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Aspergillus fumigatus KB-1
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus circulans MH-K1
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Pseudomonas sp. H-14
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. No. 7-M
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. HW-002
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Aspergillus fumigatus KH-94
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Fusarium solani 114
-
Chitosan, or beta-1,4-linked glucosamine, is a deacetylated derivative of chitin. The chitosanase is specific for chitosan as substrate
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus cereus S1
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Acinetobacter sp. C-17
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Burkholderia gladioli CHB101
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. PI-7S
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. R-4
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. 739
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus subtilis GM9804
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Rhodosporidium toruloides CFR-1
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Streptomyces griseus HUT6037
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. K-1
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Aspergillus oryzae IAM2660
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus subtilis IMR-NK1
-
-
-
-
?
chitosan pentasaccharide + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme is constitutively produced
-
-
-
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
?
-
-
chitosanases hydrolyze the polysaccharide chitosan, which is composed of partially acetylated beta-(1,4)-linked glucosamine residues
-
-
-
additional information
?
-
Bacillus licheniformis MB-2
-
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
?
-
Bacillus sp. MET 1299
-
the enzyme is constitutively produced
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ag+
-
activation
Ca2+
-
activates enzyme B
Ca2+
-
influences folding an stability of newly translocated protein, one weak Ca2+-binding site with a KA of 300 M-1
Ca2+
Amylomyces rouxii, Penicillium islandicum
-
-
Ca2+
-
5-10 mM, activity is increased by about 1.6fold
Ca2+
-
1 mM, 20% activation
Ca2+
-
35% increase in activity
Ca2+
Q8KZM5
5 mM activates by 11% at 25C for 30 min
Ca2+
Gongronella sp.
B0LV85
activates
Ca2+
-
activates
Co2+
-
activity increases about 2.5fold by the addition of 10 mM Co2+
CoCl2
-
5 mM, 15% enhancement of activity
Cu2+
-
activation
Cu2+
Gongronella sp.
B0LV85
stimulates Csn2 at 1 mM
CuCl2
-
1 mM, 19% enhancement of activity
K+
-
slight activation
K+
-
activates enzyme A
Mg2+
-
activates
Mn2+
-
slight stimulation with MnCl2
Mn2+
-
activity increases about 1.4fold by the addition of 10 mM Mn2+
Mn2+
-
increases the activities of both isoforms
Mn2+
-
1 mM, 37% activation
Mn2+
Gongronella sp.
-
100% stimulation at 1 and 10 mM
Mn2+
-
45% increase in activity
Mn2+
Gongronella sp.
B0LV85
activates
Mn2+
-
activates 46% at 1 mM
Sr2+
Gongronella sp.
B0LV85
activates
ZnCl2
-
1 mM, 24.3% enhancement of activity
MnCl2
-
1 mM, 41.2% enhancement of activity
additional information
-
Mn2+ is neither activating nor inhibitory
additional information
Q8KZM5
5 mM of Mg2+, Ba2+ have no effect on activity
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
-
not influenced by 5 mM Ca2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,4-dinitro-1-fluorbenzene
Ficus sp.
-
5 mM, 24% inhibition
2-Hydroxy-5-nitrobenzyl bromide
-
69% inhibition at 5 mM, 33% inhibition at 1 mM
2-Hydroxy-5-nitrobenzylbromide
-
-
acetate
-
enzyme A, enzyme B is not affected
Ag+
-
1 mM, 20% loss of activity
Ag+
Gongronella sp.
-
1 mM, 3% residaul activity
Ag+
-
inhibits 60% at 1 mM
Ag+
-
89% inhibition at 1 mM, 79% at 0.5 mM
Ba2+
-
5 mM inhibits by 15%, in 50 mM phosphate buffer, pH 7, for 30 min at 37C
Ba2+
-
11% inhibition at 1 mM
benzalkonium chloride
-
-
Bi2+
-
48% inhibition of chitosanase I
Ca2+
-
5 mM inhibits by 10%, in 50 mM phosphate buffer, pH 7, for 30 min at 37C
Ca2+
-
95% residual activity at 5 mM
CaCl2
-
10 mM, 48% inhibition
Cd2+
-
complete deactivation
Cd2+
Q8KZM5
1 mM inhibits by 36%, with colloidal chitosan as substrate
Cd2+
-
13% inhibition at 1 mM
chitosan
-
soluble chitosan, above 0.5 g/l
chitosan
-
substrate inhibition, enzyme B
chitosan
-
substrate inhibition, isoform A
Chloramine T
-
-
Co2+
Q8KZM5
1 mM inhibits by 86%, with colloidal chitosan as substrate
Co2+
-
13% inhibition at 1 mM
Co2+
-
60% inhibition at 1 mM
CoCl2
-
10 mM, 33% inhibition
Cs+
Q8KZM5
1 mM inhibits by 22%, with colloidal chitosan as substrate
Cu2+
-
59% inhibition of chitosanase I and 48% inhibition of chitosanase II
Cu2+
-
inhibition of chitosanase A and B
Cu2+
Penicillium islandicum
-
-
Cu2+
Q8KZM5
5 mM completely inhibits at 25C for 30 min
Cu2+
Q8KZM5
1 mM completely inhibits, with colloidal chitosan as substrate
Cu2+
-
5 mM inhibits by 92% at 37C for 30 min
Cu2+
Gongronella sp.
B0LV85
inhibits Csn2 activity at 10 mM
Cu2+
-
5 mM inhibits by 41%, in 50 mM phosphate buffer, pH 7, for 30 min at 37C
Cu2+
-
inhibits 25% at 1 mM
Cu2+
-
92% inhibition at 1 mM, 82% at 0.5 mM
Cu2+
-
70% inhibition at 1 mM
Cu2+
-
68% residual activity at 5 mM
CuCl2
-
10 mM, 69% inhibition
EDTA
Gongronella sp.
-
1 mM, 78% residual activity
EDTA
Q8KZM5
10 mM inhibits by 86% at 25C for 30 min
EDTA
-
5 mM completely inhibits at 37C for 30 min
EDTA
Gongronella sp.
B0LV85
-
EDTA
-
5 mM inhibits by 10%, in 50 mM phosphate buffer, pH 7, for 30 min at 37C
EDTA
-
inhibits 18% at 1 mM
EDTA
-
17% inhibtion at 1% w/v, 82% at 5% w/v
Fe2+
-
50% inhibition of chitosanase I
-
Fe2+
-
1 mM, 60% inhibition
-
Fe2+
Q8KZM5
5 mM inhibits by 67% at 25C for 30 min
-
Fe2+
-
5 mM completely inhibits at 37C for 30 min
-
Fe2+
-
5 mM inhibits by 77%, in 50 mM phosphate buffer, pH 7, for 30 min at 37C
-
Fe2+
-
26% inhibition at 1 mM, 9% at 0.5 mM
-
Fe2+
-
92% residual activity at 5 mM
-
Fe3+
-
49% inhibition of chitosanase I
-
Fe3+
-
inhibits 60% at 1 mM
-
Fe3+
-
35% inhibition at 1 mM
-
FeCl2
-
1 mM, 80.7% inhibition
FeCl3
-
1 mM, 84.8% inhibition
glucosamine
-
-
guanidinium hydrochloride
-
2 M, 32% residual activity
Hg2+
-
81% inhibition of chitosanase I and 80% inhibition of chitosanase II
Hg2+
-
inhibition of chitosanase A and B
Hg2+
Penicillium islandicum
-
-
Hg2+
Q9ALZ1
1 mM, 68% inhibition
Hg2+
-
1 mM, 44% inhibition
Hg2+
-
1 mM, 80% loss of activity
Hg2+
-
complete deactivation
Hg2+
Q8KZM5
1 mM completely inhibits, with colloidal chitosan as substrate
Hg2+
-
inhibits 37% at 1 mM
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
98% inhibition at 1 mM
KCl
Q9ALZ1
0.4 M, 50% inhibition
KCl
-
complete inhibition at 100 mM
L-cysteine
-
-
Mg2+
-
5 mM inhibits by 14%, in 50 mM phosphate buffer, pH 7, for 30 min at 37C
Mn2+
-
42% inhibition of chitosanase I
Mn2+
-
inhibition of chitosanase A and B
Mn2+
Q9ALZ1
1 mM, 69% inhibition
Mn2+
Q8KZM5
5 mM completely inhibits at 25C for 30 min
Mn2+
Q8KZM5
1 mM inhibits by 30%, with colloidal chitosan as substrate
Mn2+
-
5 mM completely inhibits at 37C for 30 min
Mn2+
-
5 mM inhibits by 17%, in 50 mM phosphate buffer, pH 7, for 30 min at 37C
Mn2+
-
2% residual activity at 5 mM
Mo2+
-
94% inhibition of chitosanase I and 88% inhibition of chitosanase II
N-bromosuccinimide
-
-
N-bromosuccinimide
-
-
N-bromosuccinimide
-
-
N-bromosuccinimide
-
-
N-bromosuccinimide
Ficus sp.
-
0.25 mM, 96% loss of activity
Na2SO4
-
complete inhibition at 100 mM
NaCl
Q9ALZ1
0.4 M, 50% inhibition
NaCl
-
complete inhibition at 100 mM
Ni2+
-
38% residual activity
Ni2+
Q8KZM5
1 mM inhibits by 84%, with colloidal chitosan as substrate
Ni2+
-
25% inhibition at 1 mM
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoic acid
-
-
p-hydroxymercuribenzoic acid
-
-
Pb2+
-
69% inhibition of chitosanase I
Pb2+
-
inhibition of chitosanase A and B
Pb2+
-
complete deactivation
Pb2+
-
14% inhibition at 1 mM, 8% at 0.5 mM
Pd2+
-
96% inhibition at 1 mM
PMSF
Q8KZM5
5 mM completely inhibits at 25C for 30 min
PMSF
-
5 mM inhibits by 73% at 37C for 30 min
reduced glutathione
-
-
SDS
Q8KZM5
2 mM of the anionic surfactant SDS completely inhibits at 25C for 30 min
SDS
-
inhibits 21% at 1 mM
SDS
-
82% inhibtion at 1% w/v
SDS
-
57% residual activity at 2 mM
Sn2+
-
inhibition of chitosanase A and B
Sn2+
-
20% inhibition at 1 mM, 9% at 0.5 mM
sulfhydryl reagents
-
glutathione or L-cysteine restores activity
Tetramers of N-acetylglucosamine
Penicillium islandicum
-
-
-
Trimers of N-acetylglucosamine
Penicillium islandicum
-
-
-
Triton X-100
Q8KZM5
0.5% nonionic surfactant of Triton X-100 inhibits by 56% at 25C for 30 min
Triton X-100
-
80% inhibtion at 1% w/v
Tween 20
Q8KZM5
0.5% nonionic surfactant of Tween 20 inhibits by 16% at 25C for 30 min
Tween 20
-
72% inhibtion at 1% w/v
Tween 40
Q8KZM5
0.5% nonionic surfactant of Tween 40 inhibits by 29% at 25C for 30 min
Tween 80
-
79% inhibtion at 1% w/v
Zn2+
-
about 43% loss of activity
Zn2+
Q8KZM5
5 mM inhibits by 21% at 25C for 30 min
Zn2+
-
5 mM inhibits by 49% at 37C for 30 min
Zn2+
-
5 mM inhibits by 18%, in 50 mM phosphate buffer, pH 7, for 30 min at 37C
Zn2+
-
24% inhibition at 1 mM, 9% at 0.5 mM
Zn2+
-
72% residual activity at 5 mM
ZnCl2
-
10 mM, 42.8% inhibition
monoiodoacetate
-
-
additional information
-
Mn2+ is neither activating nor inhibitory
-
additional information
-
enzyme is not affected by presence of 1 M NaCl or 6 M urea
-
additional information
Q8KZM5
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 37C for 30 min. After keeping at 25C for 10 days, the chitosanase is inactivated in the presence of 25% (v/v) ethanol and ethyl ether
-
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
P33665
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
-
additional information
Amycolatopsis sp.CsO-2
Q9LBG4
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
-
PMSF has no effect on enzyme 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 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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activates 28% at 1 mM
Chelating agents
-
especially EDTA, activate
Co2+
-
2.5 mM, 16% increase in activity
Triton X-100
Q8KZM5
2% nonionic surfactant of Triton X-100 activates by 51% at 25C for 30 min
Tween 20
Q8KZM5
2% nonionic surfactant of Tween 20 activates by 38% at 25C for 30 min
Tween 40
Q8KZM5
2% nonionic surfactant of Tween 40 activates by 6% at 25C for 30 min
Tween 80
-
0.25-1%, increases activity 7-40%
Mn2+
-
3 mM, 18% increase in activity
additional information
-
chitosanase is activated after keeping at 4C 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 41C increases chitosanase production and release to 2.2times higher than that at 37C without the 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine liposomes. Lipid mimicking cell membrane liposome under heat at 41C 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 41C
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.21
-
4-methylumbelliferyl beta-chitotrioside
-
40C, pH 5.5
2.9
-
chitohexaose
-
40C, pH 5.5
additional information
-
chitosan
-
Km value is 10 mg/ml
additional information
-
additional information
Penicillium islandicum
-
1.4 mg/ml: 5% or 30% acetylated chitosan
-
additional information
-
additional information
-
2.0% glycol chitosan; Km: 3.3% soluble chitosan
-
additional information
-
additional information
-
0.18% carboxymethylcellulose; 0.21% glycol chitosan
-
additional information
-
additional information
-
0.688 mg/ml chitosan, at pH 5.5
-
additional information
-
additional information
-
0.83 mg/ml chitosan
-
additional information
-
additional information
-
0.63 mg chitosan/ml
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
0.088 mg/ml chitosan
-
additional information
-
additional information
-
0.8 mg/ml chitosan; at pH 5.6, 22C, Km value 0.8 mg per ml, isoform A
-
additional information
-
additional information
-
0.52 mg/ml with 20.2% acetylated chitosan as substrate
-
additional information
-
additional information
-
25 mg/ml with colloidal chitosane as substrate
-
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 1.25 mg/ml
-
additional information
-
additional information
-
-
-
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
-
0.63 mg chitosan/ml
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
KM is 0.82 mg/ml
-
additional information
-
additional information
-
KM is 33 mg/ml
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
KM is 0.3 mg/ml
-
additional information
-
additional information
Penicillium islandicum
-
1.4 mg/ml: 5% or 30% acetylated chitosan
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
0.83 mg/ml chitosan
-
additional information
-
additional information
-
KM is 2.1 mg/ml
-
additional information
-
additional information
-
0.088 mg/ml chitosan; 0.688 mg/ml chitosan, at pH 5.5
-
additional information
-
additional information
-
0.088 mg/ml chitosan
-
additional information
-
additional information
-
KM-value for colloidal chitosan is 37.5 g/L
-
additional information
-
additional information
-
Michaelis-Menten kinetics, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
38.4
-
30% N-acetylated chitosan
P33665
40C, pH 5.5, W227F
-
42.1
-
30% N-acetylated chitosan
P33665
40C, pH 5.5, W28F/W101F
-
45.1
-
30% N-acetylated chitosan
P33665
40C, pH 5.5, W101F
-
50.1
-
30% N-acetylated chitosan
P33665
40C, pH 5.5, W28F
-
71.4
-
30% N-acetylated chitosan
P33665
40C, pH 5.5, wild-type
-
0.000081
-
4-methylumbelliferyl beta-chitotrioside
-
40C, pH 5.5
107
-
chitohexaose
-
40C, pH 5.5
0.0167
-
chitosan
P33665
mutant D40G/T45D, assayed as the amount of D-glucosamine released from chitosan
0.024
-
chitosan
P33665
mutant E36A/D40G, assayed as the amount of D-glucosamine released from chitosan
0.0368
-
chitosan
P33665
mutant T45E, assayed as the amount of D-glucosamine released from chitosan
0.0683
-
chitosan
P33665
mutant E36Q/D40G, assayed as the amount of D-glucosamine released from chitosan
0.44
-
chitosan
P33665
mutant D40G, assayed as the amount of D-glucosamine released from chitosan
2.3
-
chitosan
-
40C, pH 4, isoform PSC-II
5.9
-
chitosan
-
40C, pH 4, isoform PSC-I
6.2
-
chitosan
-
40C, pH 4, isoform PSC-III
6.827
-
chitosan
P33665
mutant E36N, assayed as the amount of D-glucosamine released from chitosan
8.34
-
chitosan
P33665
mutant E36D, assayed as the amount of D-glucosamine released from chitosan
10.48
-
chitosan
P33665
mutant T45S, assayed as the amount of D-glucosamine released from chitosan
11.47
-
chitosan
P33665
mutant E36A, assayed as the amount of D-glucosamine released from chitosan
11.66
-
chitosan
P33665
mutant E36Q, assayed as the amount of D-glucosamine released from chitosan
12.4
-
chitosan
P33665
wild-type, assayed as the amount of D-glucosamine released from chitosan
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.002
-
-
culture supernatant
0.005316
-
-
culture supernatant
0.006
-
-
culture supernatant, at pH 7.0 and 60C
0.01
-
P33665
mutant T45H
0.011
-
P33665
mutant T45E
0.02
-
P33665
mutant D40G/T45E
0.032
-
-
enzyme HEWL
0.055
-
-
enzyme BCVC-4
0.06
-
Q8KZM5
culture supernatant
0.06
-
P33665
mutant D40G/T45D
0.07
-
P33665
mutant E36A/D40G
0.075
-
-
enzyme BCVC-3
0.087
-
-
enzyme BCVC-5
0.114
-
-
enzyme BCVC-6
0.18
-
-
after 30fold purification, at pH 7.0 and 60C
0.3
-
P33665
mutant E36Q/D40G
0.402
-
-
pH 5.2, 60C
0.567
-
-
enzyme Yam
1.291
-
-
enzyme BCLVC
1.38
1.53
-
activity of enzyme immobilized on liposomes
1.6
-
P33665
mutant D40G
2.62
-
-
after Toyopearl HW-50 chromatography
2.76
-
-
after second Sephadex G-75 chromatography
2.8
-
-
527fold purified enzyme
3.411
-
-
enzyme BCVC-1
3.9
-
Q8KZM5
65fold purified enzyme
5.84
-
-
after Sephadex G-100 chromatography
7
-
-
50fold purified enzyme
9.3
-
Q8KZM5
culture supernatant
10
-
Penicillium islandicum
-
after treatment with hydroxylapatite
10
-
Penicillium islandicum
-
-
17.1
-
-
culture broth, pH 6.0, 50C
17.2
-
-
enzyme I after after Sephadex G-100 chromatography
21.9
-
P33665
mutant E36N
29.1
-
P33665
mutant E36D
29.2
-
P33665
mutant E36A
35.61
-
-
after Sephadex G-75 chromatography
35.61
-
-
-
37.6
-
P33665
mutant T45S
38.8
-
-
enzyme II after after Sephadex G-100 chromatography
42.7
-
-
after second Mono Q HR 5/5 chromatography, enzyme A
44.7
-
P33665
mutant E36Q
51.8
-
-
after TSKgel G2000SWXL chromatography
51.8
-
-
-
52.9
-
P33665
wild-type
58.9
-
-
Bio-Gel A eluate of the recombinant protein
59.1
-
Q8KZM5
6.4fold purified enzyme
59.8
-
-
after Bio-Gel A 0.5 M chromatography
61.4
-
-
after Sephadex G-75 chromatography
82
-
Gongronella sp.
-
pH 4.8, 50C
89.6
-
-
desalted extraction
93.6
-
-
-
102.3
-
-
after Superose 6 HR 10/30 chromatography, enzyme B
105
-
-
diethylaminoethyl-cellulose eluate
126
-
-
after TSK-gel HW-55F gel filtration
154.8
-
-
isoform A, pH 5.6, 22C
160
-
-
after gel filtration
163.8
-
-
after Mono-S cation exchange chromatography with 0.06 to 0.08 M KCl
196
-
-
after purification on Super Q Toyopearl
200
-
-
after DE-52 chromatography
319
-
-
after CM-Sephadex C-50 (II) chromatography
319
-
-
-
412
-
-
after 24.1fold purification, pH 6.0, 50C
444
-
-
after Superdex 75 HR gel filtration
476
-
-
-
489.8
-
-
isoenzyme PSC-II
733.5
-
-
isoenzyme PSC-III
742.6
-
-
isoenzyme PSC-I
850
-
-
purified enzyme
1700
-
Q9ALZ1
-
2819
-
-
after DEAE-Sephacel ion exchange chromatography
additional information
-
Ficus sp.
-
-
additional information
-
-
between 270-290 U/mg, recombinant chitosanase
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
isoenzyme PSC-III
4
-
Q8KZM5
-
4.5
5.5
-
chitosanase II
4.5
6
Penicillium islandicum
-
with 30% or 5% acetylated chitosan
4.5
6
-
at 25C
4.5
6
Penicillium islandicum, Streptomyces sp.
-
-
4.5
-
Ficus sp.
-
-
4.6
4.8
Gongronella sp.
-
-
4.9
-
Macrotermes estherae
-
enzyme from males
5
5.2
-
optimal at an ionic strength of 0.2
5
-
-
isoenzymes PSC-I and PSC-II
5
-
-
and 7.0, at pH 7.0 higher chitosanase activity than at pH 5.0
5
-
-
assay at
5.2
-
-
chitosan hydrolysis
5.3
-
Macrotermes estherae
-
enzyme from winged females
5.5
6
-
-
5.5
6.9
-
-
5.5
-
-
chitosanase II
5.5
-
-
-
5.5
-
-
chitosanase I
5.5
-
-
-
5.5
-
-
wild-type enzyme
5.6
-
-
-
5.6
-
Gongronella sp.
B0LV85
-
5.6
-
-
assay at
5.8
-
Macrotermes estherae
-
enzyme from soldiers
5.8
-
Macrotermes estherae
-
enzyme from soldiers
6
6.5
-
-
6.2
-
Macrotermes estherae
-
enzyme from workers
6.2
-
-
chitosanase ChiN
6.2
-
-
-
6.5
-
-
carboxymethylcellulose hydrolysis
6.5
-
-
chitosanase I
6.5
-
-
-
6.5
-
-
mutant YM20
6.6
-
-
chitosanase ChiX
7
-
-
and 5.0, at pH 7.0 higher chitosanase activity than at pH 5.0
7
-
-, C9D7S2
assay at
8
-
-
chitosanase activity
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
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
8.5
-
chitosanase II
4
6
-
pH 4.0: about 45% of maximal activity, pH 6.0: about 25% of maximal activity
4
6.5
Penicillium islandicum
-
rapid drop in activity below pH 4.0 and above pH 6.5
4
7
-
20% of maximal activity at pH 4.0, 10% at pH 7.0, pH profile, overview
4
8
-
about 20% of maximal activity at pH 4 and 8
4
8
-
the recombinant enzyme is inactive above pH 8.0 and shows 90% of maximal activity at pH 4.0
4.2
5.8
Gongronella sp.
B0LV85
-
4.3
-
A7KBW5
calculated
4.5
10
-
-
4.5
6.5
-
isoform A
4.5
6.5
-
more than 80% of activity maximum at pH 4.5 and 6.5
5
8
-
more than 80% of maximum activity
6
9
-
isoenzyme PSC-III is stable in this range
6
-
A9P7F5, A9P7F6, A9P7F7, A9P7F8, A9P7F9, A9P7G0, A9P7G1, A9P7G2, A9P7G3, -
assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at
6
-
-
loss of 50% of 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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
25
Macrotermes estherae
-
enzyme from soldiers
24
26
Macrotermes estherae
-
enzyme from workers
24
-
Macrotermes estherae
-
enzyme from males
25
-
Macrotermes estherae
-
enzyme from winged females
30
-
-
PSC-III
30
-
-, C9D7S2
assay at
40
-
-
-
40
-
-
PSC-I and PSC-II
40
-
-
wild-type enzyme
40
-
-
assay at
45
55
-
-
45
-
Penicillium islandicum
-
-
45
-
Penicillium islandicum, Rhodosporidium toruloides
-
-
45
-
-
assay at
50
60
-
chitosanase II
50
-
-
-
50
-
-
at pH 6.5
50
-
-
enzyme B
50
-
-
; enzyme A
50
-
-
chitosanase ChiN
50
-
A9P7F5, A9P7F6, A9P7F7, A9P7F8, A9P7F9, A9P7G0, A9P7G1, A9P7G2, A9P7G3, -
assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at
50
-
Gongronella sp.
-
-
50
-
Q8KZM5
-
50
-
-
mutant YM18
55
60
Gongronella sp.
B0LV85
optimal reaction temperature is between 55C and 60C
55
-
-
enzyme A
55
-
-
pH 5.3
60
-
-
chitosanase I
60
-
Q9ALZ1
-
60
-
-
chitosanase ChiX
60
-
-
-
60
-
-
in acetate buffer (pH 5.6)
65
-
Ficus sp.
-
-
65
-
-
-
70
80
-
chitosanase I
70
-
-
chitosanase II
70
-
-
mutant YM20
additional information
-
-
release of chitosanase across lipid membrane is maximized at 41C in comparison with that at 37C and 45C. Interaction of the 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine liposomes with the cell membrane, induced by heat stress at 41C changes the surface net hydrophobicity and surface net charge of cell membrane to favorable state for the enhanced release of chitosanase
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
60
-
chitosanase II
10
60
-
20%, 30%, and 70% of the maximum activity at 60C, 10C, and 30C, respectively, maximal activity at 45C
20
50
-
15-20% of maximal activity at 20C, 30% at 50C, temperature profile, overview
30
50
-
-
40
70
-
40C: about 40% of maximal activity, 70C: about 15% of maximal activity
55
70
-
55C: about 85% of maximal activity, 70C: about 90% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
-
-
isoelectric focusing, in plants infected either with Glomus mosseae or Glomus intraradices
4.2
-
Penicillium islandicum
-
-
4.4
-
-
isoelectrofocusing, PSC-III
4.6
4.7
-
isoelectrofocusing, PSC-II
4.7
4.8
-
chitosanase A
4.8
-
-
chitosanase II
4.9
-
-
isoelectrofocusing, PSC-I
4.9
-
-
chitosanase A
5
-
D7R809, -
isoelectric focusing
5.1
-
-
isoelectric focusing
5.8
-
Gongronella sp.
-
isoelectric focusing
5.9
-
-
isoelectric focusing
7.11
-
-
sequence analysis
7.3
7.4
-
chitosanase I
8.3
-
-
isoelectric focusing
8.3
-
-
-
8.3
-
-
isoelectric focusing
8.8
-
-
isoelectric focalization
9.2
-
-
density gradient column electrofocusing and acrylamide gel electrofocusing
10.1
-
-
-
10.3
-
-
Spectra Phoresis 1000 CE, enzyme BCLVC
10.5
-
-
Spectra Phoresis 1000 CE, enzymes BCVC-1, BCVC-4, BCVC-5 and BCVC-6
10.6
-
-
Spectra Phoresis 1000 CE, enzymes BCVC-2 and BCVC-3
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
enzyme is constitutively produced
Manually annotated by BRENDA team
Bacillus circulans MH-K1, Bacillus sp. K-1, Bacillus sp. PI-7S
-
-
-
Manually annotated by BRENDA team
Bacillus sp. S65
-
enzyme is constitutively produced
-
Manually annotated by BRENDA team
-
best source of enzyme
Manually annotated by BRENDA team
-
air-dried and defatted
Manually annotated by BRENDA team
Fusarium solani 114
-
-
-
Manually annotated by BRENDA team
-
colonized by Glomus mosseae or Glomus intraradices
Manually annotated by BRENDA team
Macrotermes estherae
-
-
Manually annotated by BRENDA team
additional information
-
in crude pepsin preparation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the discoidin domain of chitosanase is required for binding to the fungal cell wall
Manually annotated by BRENDA team
Penicillium islandicum
-
-
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
Acinetobacter sp. C-17
-
-
-
-
Manually annotated by BRENDA team
Aeromonas sp. HG08
-
the enzyme is secreted
-
-
Manually annotated by BRENDA team
Amycolatopsis sp. CsO-2, Aspergillus oryzae IAM2660, Bacillus circulans MH-K1, Bacillus licheniformis MB-2, Bacillus sp. K-1, Bacillus sp. MET 1299, Bacillus sp. P16, Bacillus subtilis GM9804, Lysobacter sp. IB-9374, Rhodosporidium toruloides CFR-1, Streptomyces sp. No. 6
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10000
-
-
gel filtration
16600
-
Ficus sp.
-
gel filtration
18000
-
-
gel filtration
18780
-
-
sequence analysis
22500
-
-
chitosanase I
23000
-
-
gel filtration
23000
-
-
gel filtration
23380
-
-
mass spectrometry, chitosanase II
24000
-
-
gel filtration
24000
-
-
gel filtration
25000
-
-
gel filtration
25590
-
Q8KZM5
sequence analysis
26000
-
-
gel filtration
26490
-
Amycolatopsis sp.CsO-2
Q9LBG4
sequence analysis
27000
-
-
gel filtration
27000
-
-
gel filtration
27000
-
-
gel filtration
28000
-
Q8KZM5
purified protein
28000
-
Gongronella sp.
B0LV85
gel filtration
28900
-
-
deduced from amino acid sequence
29000
-
-
gel filtration
29000
-
-
-
29000
-
-
gel filtration
29020
-
-
deduced from nucleotide sequence
30000
-
Penicillium islandicum
-
gel filtration
30000
-
-
gel filtration
30000
-
Penicillium islandicum
-
gel filtration
30000
-
-
chitosanase ChiN
31000
-
-
gel filtration
31000
-
Macrotermes estherae
-
enzyme from males and winged females
31000
-
-
gel filtration
31400
-
-
gel filtration
31480
-
-
sequence analysis
35000
-
Macrotermes estherae
-
enzyme from soldiers
35000
-
-
gel filtration
36000
-
-
gel filtration
37500
-
-
gel filtration, isoform PSC-I
40000
-
Macrotermes estherae
-
enzyme from workers
40600
-
-
gel filtration, isoform PSC-II
42000
-
-
gel filtration
43000
-
-
gel filtration
43700
-
-
gel filtration, isoform PSC-III
63000
-
-
enzyme B, gel filtration
64000
-
-
gel filtration
70000
-
-
gel filtration
79000
-
-
enzyme A, gel filtration
81000
-
-
chitosanase ChiX
100000
-
-
gel filtration
108000
-
-
chitosanase II
111200
-
-
mass spectrometry, chitosanase I
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 19000, SDS-PAGE without reducing agent
?
-
x * 10000 + x * 16000 + x * 18000 + x * 20000, SDS-PAGE without reducing agent
?
-
x * 18000 + x * 21000, SDS-PAGE without reducing agent
?
-
x * 23000 + x * 19000, SDS-PAGE without reducing agent
?
-
x * 18000 + x * 22000, SDS-PAGE without reducing agent
?
-
x * 23000 + x * 22000 + x * 19000, SDS-PAGE without reducing agent
?
-
x * 19000 + x * 22000, SDS-PAGE without reducing agent
?
-
x * 18000 + x * 19000, SDS-PAGE without reducing agent
?
-
x * 22000, enzyme C, SDS-PAGE; x * 43000, enzyme B, SDS-PAGE
?
-
x * 30500, SDS-PAGE
?
-
x * 35400, SDS-PAGE
?
-
x * 135000, SDS-PAGE, enzyme II; x * 40000, SDS-PAGE, enzyme I
?
-
x * 47000, SDS-PAGE
?
-
x * 45000, SDS-PAGE
?
-
x * 46000
?
-
x * 20000, SDS-PAGE, in roots infected either with Glomus mosseae or Glomus intraradices
?
-
x * 26000, SDS-PAGE
?
-
x * 76000, SDS-PAGE
?
-
x * 31000, SDS-PAGE
?
-
x * 43000, enzyme B, SDS-PAGE
?
-
x * 50000, SDS-PAGE
?
-
x * 36000, SDS-PAGE
?
-
x * 35000, SDS-PAGE
?
-
x * 35000, SDS-PAGE
?
-
x * 26000, SDS-PAGE; x * 29500, SDS-Page
?
-
x * 15800, SDS-PAGE
?
-
x * 27000, SDS-PAGE; x * 31420, calculated from sequence
?
-
x * 52000, SDS-PAGE
?
-
x * 59000, SDS-PAGE
?
-
x * 45000, SDS-PAGE
?
-
x * 41000, SDS-PAGE, x * 41241, calculated
?
A7KBW5
x * 28200, calculated
?
Gongronella sp.
-
x * 90000, SDS-PAGE
?
-
x * 75000, SDS-PAGE
?
-
x * 43000, SDS-PAGE
?
Q8KZM5
x * 30000, SDSPAGE
?
-
x * 50000, recombinant detagged enzymes, SDS-PAGE, x * 81000, recombinant GST-tagged enzymes, SDS-PAGE
?
-
x * 42000, SDS-PAGE
?
-
x * 39000, enzyme with signal peptide, SDS-PAGE
?
-
x * 85610, sequence calculation
?
-
x * 33000, native enzyme, SDS-PAGE, x * 31000, recombinant enzyme, SDS-PAGE
?
D7R809, -
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 * 32000, deduced from amino acid sequence; 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 * 43000, SDS-PAGE
?
-
x * 29000, SDS-PAGE
?
Acinetobacter sp. C-17
-
x * 35400, SDS-PAGE
-
?
Aspergillus oryzae IAM2660
-
x * 135000, SDS-PAGE, enzyme II; x * 40000, SDS-PAGE, enzyme I
-
?
Bacillus cereus S1
-
x * 45000, SDS-PAGE
-
?
Bacillus licheniformis MB-2
-
x * 75000, SDS-PAGE
-
?
Bacillus sp. 739
-
x * 46000
-
?
Bacillus sp. K-1
-
; x * 46000
-
?
-
x * 45000, SDS-PAGE
-
?
Bacillus sp. MET 1299
-
x * 52000, SDS-PAGE
-
?
Bacillus sp. No. 7-M, Bacillus sp. PI-7S, Bacillus sp. R-4
-
-
-
?
Bacillus sp. S65
-
x * 45000, SDS-PAGE
-
?
Bacillus subtilis CH2
-
x * 29000, SDS-PAGE
-
?
Bacillus thuringiensis JAM-GG01
-
x * 43000, SDS-PAGE
-
?
-
x * 90000, SDS-PAGE
-
?
-
x * 41000, SDS-PAGE, x * 41241, calculated
-
?
-
x * 28200, calculated
-
?
Penicillium chrysogenum AS51D
-
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 * 32000, deduced from amino acid sequence; 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
-
?
Penicillium sp. ZD-Z1
-
x * 43000, SDS-PAGE
-
?
Pseudomonas sp. H-14
-
x * 35000, SDS-PAGE; x * 35000, SDS-PAGE
-
?
Pseudomonas sp. TKU015
-
x * 30000, SDSPAGE
-
?
Streptomyces sp. No. 6
-
x * 26000, SDS-PAGE; x * 29500, SDS-Page
-
monomer
Penicillium islandicum
-
-
monomer
-
1 * 41000, SDS-PAGE
monomer
-
1 * 26000, gel filtration
monomer
-
1 * 31000, SDS-PAGE
monomer
-
1 * 43000, SDS-PAGE
monomer
-
1 * 29000, SDS-PAGE
monomer
-
1 * 45000, SDS-PAGE
monomer
-
1 * 41000, SDS-PAGE
monomer
-
1 * 40000, SDS-PAGE
monomer
-
1 * 46000, SDS-PAGE
monomer
-
1 * 27000, SDS-PAGE
monomer
-
1 * 32000, SDS-PAGE
monomer
-
1 * 41000, SDS-PAGE; 1 * 43000, SDS-PAGE
monomer
-
1 * 25500, SDS-PAGE
monomer
Ficus sp.
-
-
monomer
-
1 * 66000, SDS-PAGE
monomer
-
1 * 21000, SDS-PAGE
monomer
Gongronella sp.
B0LV85
1 * 28000, SDS-PAGE
monomer
-
1 * 29000, SDSPAGE
monomer
Amycolatopsis sp.CsO-2
Q9LBG4
1 * 30000, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 36000, SDS-PAGE
monomer
Aeromonas sp. HG08
-
1 * 70000, SDS-PAGE
-
monomer
-
1 * 27000, SDS-PAGE
-
monomer
Bacillus circulans MH-K1
-
1 * 31000, SDS-PAGE; 1 * 32000, SDS-PAGE; 1 * 32000, SDS-PAGE
-
monomer
-
1 * 29000, SDS-PAGE
-
monomer
Bacillus sp. HW-002
-
1 * 46000, SDS-PAGE
-
monomer
Bacillus sp. K-1
-
1 * 29000, SDS-PAGE; 1 * 41000, SDS-PAGE; 1 * 41000, SDS-PAGE; 1 * 43000, SDS-PAGE; 1 * 43000, SDS-PAGE; 1 * 45000, SDS-PAGE; 1 * 46000, SDS-PAGE
-
monomer
Bacillus sp. No. 7-M
-
1 * 41000, SDS-PAGE; 1 * 41000, SDS-PAGE; 1 * 43000, SDS-PAGE
-
monomer
-
1 * 45000, SDS-PAGE
-
monomer
Bacillus sp. PI-7S
-
1 * 41000, SDS-PAGE; 1 * 43000, SDS-PAGE; 1 * 43000, SDS-PAGE
-
monomer
Bacillus sp. R-4
-
1 * 41000, SDS-PAGE; 1 * 43000, SDS-PAGE
-
monomer
Bacillus sp. TKU004
-
1 * 29000, SDSPAGE
-
monomer
Bacillus subtilis IMR-NK1
-
1 * 41000, SDS-PAGE
-
monomer
-
1 * 28000, SDS-PAGE
-
monomer
Serratia marcescens subsp. sakuensis TKU019
-
1 * 36000, SDS-PAGE
-
monomer
Serratia marcescens TKU011
-
1 * 21000, SDS-PAGE
-
monomer
Streptomyces sp. No. 6
-
1 * 26000, gel filtration
-
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
Bacillus circulans MH-K1
-
-
-
proteolytic modification
-
deletion of a signal peptide with SDS-PAGE
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
-
glycoprotein
D7R809, -
-
glycoprotein
Penicillium chrysogenum AS51D
-
-
-
additional information
Penicillium islandicum
-
carbohydrate content is less than 0.5%
additional information
-
no glucosamine or other carbohydrate
additional information
Streptomyces sp. No. 6
-
no glucosamine or other carbohydrate
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of mutant enzyme K218P
-
sitting drop vapor diffusion method at 20C. 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 20C, orthorhombic space group P21212, two globular upper and lower domains which generate the active site cleft for the substrate binding
-
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
-
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
-
the substrate binding cleft is composed of six monosaccharide binding subsites
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
-
Q9ALZ1
1 h, complete inactivation
2
-
-
loss of 90% of activity after 1 h incubation
3
7
-
isoenzyme PSC-II is stable in this range
3
7
-
30C, stable for at least 24 h
3
8
-
stable for at least 7 h
3
9
Q8KZM5
-
3.8
9.9
-
37C, 30 min, stable
4
8
Q9ALZ1
1 h, stable
5
8
-
stable at this range
5
8
-
isoenzyme PSC-I is stable in this range
5
8
Q8KZM5
purified enzyme
5
9
-
stable at 25C for 1 h
5
-
-
most stable at this pH
5.5
6.5
-
28C, 60 min, stable
5.5
9
-
stable at temperatures below 60C
6
11
-
stable for 60 min at 40C
7
-
-
drastical decrease in activity at pH 7
9
-
-
and above, loss of 50% of activity after 1 h incubation
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
-
stable in this range
0
-
-
stable
5
30
-
in absence of substrate the chitosanase is stable between 5C and 30C
10
-
-
most stable at 10C, stability of chitosanase I droppes at higher temperatures and most activity is lost above 60C
20
70
-
all three isoforms are stable in this range for 30 min
20
-
-
stable
20
-
-
purified enzyme, pH 5.8, 2 h, 98% activity remaining
25
40
Q8KZM5
maintains its initial activity, has almost half of its activity at 50C but is completely inactivated at 70C
25
40
-
maintains its initial activity from 25 to 40C but is completely inactivated at 80C
25
50
-
maintains more than 90% of its initial activity between 25 and 50C, but is rapidly inactivated retaining only 60% of its initial activity at 60C, and is completely inactivated at greater than 70C
30
40
-
stable at this range
30
70
-
stable for 2 h
30
-
-
pH 5.0, 30 min, stable
30
-
-
rather stable for 20 min
30
-
-
purified enzyme, pH 5.8, 2 h, 92% activity remaining
37
-
Penicillium islandicum
-
denaturation in 1-2 h, stabilized by 1.0 mM Ca2+
37
-
-
pH 6.0-8.0, stable, unstable at elevated temperatures
37
-
-
stable
40
50
-
its half-life is only several min at 60C. At lower temperatures, the enzyme is quite stable, its half-life is extended to several hours at 50 and 40C. No detectable activity loss at room temperature for several days
40
60
-
the purified chitosanase is continuously thermostable at 40C and the stability is gradually decreased when the temperature is increased to 50C but rapidly decreases at 60C
40
-
-
pH 5.0, 30 min, stable
40
-
-
rapid decrease of activity above
40
-
-
15 min, stable up to
40
-
-
rather stable for 20 min
40
-
-
pH 6, 1 h, stable below
40
-
-
30 min, 20 mM acetate pH 5.0, stable up to 40C
40
-
-
purified enzyme, pH 5.8, 2 h, 85% activity remaining
43.4
-
-
transition temperature in absence of chitosan
45
55
-
the enzyme is gradually inactivated during incubation at temperature above 45C and is completely inactivated at 55C after 15 min, at 55C 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 60C with 10 mM chitotriose or chitotetraose are 35.5% and 59.5%, respectively
45
-
-
pH 6.8, 15 min, stable below
45
-
-
isoform A, stable up to
45
-
-
gradual inactivation of the enzyme
45
-
-
stable for 1 h
45
-
Q9ALZ1
24 h, enzyme retains full activity
50
55
Gongronella sp.
B0LV85
half-lives of Csn2 at 50C and 55C are 30 min and 11 min, respectively
50
-
-
stable below, pH 6.0, 15 min
50
-
-
stable
50
-
-
60 min, stable
50
-
-
half-maximum inactivation after 1 h
50
-
-
gradual inactivation of the enzyme
50
-
-
stable below
50
-
alpine bacterium
-
active below 50C
50
-
Q9ALZ1
half-life: 5 h
50
-
-
pH 6, 1 h, stable below
50
-
-
pH 6, 1 h, about 50% loss of activity
50
-
-
30 min, 20 mM acetate pH 5.0, 95% loss of activity
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
-
Gongronella sp.
-
half-life 65 min
50
-
-
purified enzyme, pH 5.8, half-live is 30 min
50
-
-
the recombinant chitosanase is stable at temperatures up to 50C above which the enzyme activity decreases rapidly
54
-
-
wild-type, transition temperature in absence of chitosan
55
-
-
significant loss in activity
55
-
Q9ALZ1
half-life: 10 min
60
80
-
the chitosanase maintains its initial activity at less than 60C, the chitosanase is inactivated completely at 80C
60
-
-
pH 6.0, 15 min, 40% loss of activity
60
-
-
30 min, pH 5.0, complete inactivation
60
-
-
60 min, 40% loss of activity
60
-
-
stable up to
60
-
-
loss of 75% activity after 15 min
60
-
Q9ALZ1
half-life: 5 min
60
-
-
pH 5.5-9.0, stable below
60
-
-
purified enzyme, pH 5.8, half-live is 13 min
61
-
-
both wild-type and mutants A104L, K164R are active over 90 min
65
-
-
pH 6, 10 min, about 90% loss of activity
68.6
-
-
transition temperature in presence of chitosan at 6 g/l
69.5
-
-
wild-type, transition temperature in presence of chitosan at 6 g/l
70
-
-
pH 6.0, 15 min, complete loss of activity
70
-
-
15 min, 30% loss of activity
70
-
-
60 min, 70% loss of activity
70
-
-
stable for 60 min
70
-
-
loss of 95% activity after 15 min
70
-
-
in presence of substrate remarkable stability at
70
-
Ficus sp.
-
30 min, enzyme retains almost all of its activity
70
-
-
optimum for chitosanase acivity
70
-
-
half-life 26.6 min
70
-
-
the recombinant chitosanase shows hardly activity after 30 min
75
-
Ficus sp.
-
30 min, about 35% loss of activity
80
-
-
60 min, 80% loss of activity
80
-
-
15 min, 55% loss of activity
80
-
-
stable for 30 min
80
-
Ficus sp.
-
5 min, about 70% loss of activity
80
-
-
15 min, almost complete loss of activity
80
-
-
half-life 18.4 min
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
-
-
10 min, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
acetone, n-butanol and ethylacetate rapidly denature the enzyme
-
quite stable in 5% SDS
-
resistant to 6 M urea or 2 M guanidine HCl at 37C for 30 min
-
heat treatment leads at a concentration of 0.0106 mM protein at 75C to a irreversible unfolding, but this is reversible when the protein concentation is 20 times lower
-
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
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
DMSO
-
relativly stable at the concentration of 30% at 37C for 30 min
DMSO
Bacillus sp. K-1, Bacillus sp. P16
-
relativly stable at the concentration of 30% at 37C for 30 min
-
Ethanol
-
-
Ethanol
-
relative stable at the concentration of 30% at 37C for 30 min
Ethanol
-
10%, 57% residual activity
Ethanol
Bacillus licheniformis MB-2
-
10%, 57% residual activity
-
Ethanol
-
-
-
Ethanol
Bacillus sp. K-1
-
; relative stable at the concentration of 30% at 37C for 30 min
-
Ethanol
-
relative stable at the concentration of 30% at 37C for 30 min
-
Methanol
-
relative stable at the concentration of 30% at 37C for 30 min
Methanol
Bacillus sp. K-1, Bacillus sp. P16
-
relative stable at the concentration of 30% at 37C for 30 min
-
propanol
-
10%, 57% residual activity
propanol
Bacillus licheniformis MB-2
-
10%, 57% residual activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 50% glycerol, stable for at least 6 months
-
-15C, stable for 8 weeks, 25% loss of activity after 16 weeks, 55% loss of activity after 20 weeks
-
5C, stable for 6 weeks, 35% loss of activity after 16 weeks, 90% loss of activity after 20 weeks
-
4C, pH 6.5, stable for at least 24 h
-
25C, the chitosanase is inactivated in the presence of 25% (v/v) ethanol and ethyl ether, 10 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme 21.25fold
-
-
alpine bacterium
-
to homogeneity
Amycolatopsis sp.CsO-2
Q9LBG4
2 forms: A and B
-
native enzyme 281fold by three steps of anion exchange 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
-
chimeric chitosanase and wild-type Csn purified nearly to homogeneity by cation-exchange chromatography
P33673
3 enzymes: A, B and C
-
by gel filtration, about 527fold with overall activity yield of 20%, to homogeneity
-
HW-002
-
No. 7-M
-
to homogeneity by immobilized metal-ion affinity chromatography
-
ammonium sulfate precipitation and Sephadex-G100 gel filtration
-
SuperQ column chromatography and CM Toyopearl column chromatography
-
2 isoforms: A1-CF1 and A1-CF2
-
-
Ficus sp.
-
f. sp. phaseoli
-
-
Gongronella sp.
-
by gel filtration
Gongronella sp.
B0LV85
isolation of a bifunctional chitosanase/cellulase from commercial prepapration of cellulase
-
native enzyme 23fold from mycelium by bacitracin affinity chromatography and gel filtration
-
-
Penicillium islandicum
-
by gel filtration, to homogeneity, 6.4fold
Q8KZM5
by two consecutive anion exchange chromatography steps and subsequent reverse-phase column chromatography, to homogeneity, 65fold with a yield of 1.7%
Q8KZM5
by a combination of ion-exchange and gel-filtration, 50fold with an overall activity yield of 24%
-
ammonium sulfate precipitation, DEAE-Sepharose CL-6B column chromatography and Sephacryl S-100 gel filtration
-
recombinant enzyme from Streptomyces lividans strain TK24 by ion exchange and hydroxylapatite chromatography
-
recombinant protein
-
by a two-step procedure involving ion exchange chromatography followed by gel filtration, to purity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
wild-type and mutant overexpressed from vector pET15b/CSO2 in Escherichia coli BL21(DE3)
Amycolatopsis sp.CsO-2
Q9LBG4
gene cho, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109
-, C9D7S2
expressed in Escherichia coli
-
expression of GST-tagged shuffled mutant enzymes Y18 and Y20 in Escherichia coli strain BL21(DE3)
-
chimeric chitosanase and wild-type Csn overexpressed from vector pET22b(+) in Escherichia coli strain BL21 (DE3)
P33673
expression in Escherichia coli
-
-
Q9ALZ1
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
-
expression in Escherichia coli
-
overexpression of wild-type enzyme and mutant enzymes E122Q, D183N and E309Q in Escherichia coli
-
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
A9P7F5, A9P7F6, A9P7F7, A9P7F8, A9P7F9, A9P7G0, A9P7G1, A9P7G2, A9P7G3, -
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
A9QUB2
expression in Saccharomyces cerevisiae
-
overexpression of Csn1 in Fusarium solani strain T2 using transformation by Agrobacterium tumefaciens strain LBA 4404 and expression vector pCIR
-
genomic sequence of Csn2 cloned from the DNA library by PCR
Gongronella sp.
B0LV85
the enzyme is expressed recombinantly as a periplasmic enzyme in Escherichia coli strain BMS172
-
expression as a fusion protein in Escherichia coli
A7KBW5
expression in Escherichia coli
-
expression in yeast cells as a whole-cell biocatalyst
-
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
-
wild-type and mutants overexpressed in Brevibacillus choshinensis HDP31-M3 carrying the cto1 gene on expression plasmid vector pNCMO2
Q8KZM5
expression in Streptomyces lividans strain TK24
-
expression in Streptomyces lividans TK24
-
expression of CsnN174 in Escherichia coli JM109. T45S chitosanase mutant introduced into Streptomyces lividans
P33665
wild-type and mutants subcloned into vector pFD666 and expressed in Streptomyces lividans TK-24
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme's chitosanase and antifungal activities are induced significantly under of growth-limiting conditions of 8 of light and 16 h of darkness
-, C9D7S2
enzyme expression is not induced using chitosan as a carbon source
-
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
-
enzyme expression is not induced using chitosan as a carbon source
Bacillus subtilis CH2
-
-
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
Bacillus subtilis CH2
-
-
addition of chitosan or glucosamine into culture medium induces the chitosanase expression
-
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 subsp. sakuensis TKU019
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E22Q
Amycolatopsis sp.CsO-2
Q9LBG4
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 40C. 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 40C. 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
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
Y148S
-
mutant enzyme shows 12.5% of wild-type activity
K218P
Bacillus circulans MH-K1
-
mutant enzyme shows 0.16% of wild-type activity with acetylated chitosan
-
Y148S
Bacillus circulans MH-K1
-
mutant enzyme shows 12% of wild-type activity with acetylated chitosan
-
D183N
-
0.0403% of wild-type activity
E122Q
-
0.00965% of wild-type activity
E309Q
-
0.0105% of wild-type activity
D183N
Bacillus sp. K17
-
0.0403% of wild-type activity
-
E122Q
Bacillus sp. K17
-
0.00965% of wild-type activity
-
E309Q
Bacillus sp. K17
-
0.0105% of wild-type activity
-
D175E
-
48.3% of wild-type activity with acetylated chitosan as substrate (acetylation degree: 30%)
D175N
-
inactive mutant enzyme
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 50C
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
Mitsuaria chitosanitabida 3001
-
inactive. Use of strain for isolation of mutant genes with restored activity
-
G151D/N222S
Mitsuaria chitosanitabida 3001
-
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 50C
-
L74Q/V75I/G151D
Mitsuaria chitosanitabida 3001
-
mutant with restored activity based on inactive mutant G151D, 1.5fold higher in specfic activity than wild-type, and protein is efficiently secreted
-
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
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
E302A
Paenibacillus fukuinensis D2
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
-
E302C
Paenibacillus fukuinensis D2
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
-
N312A
Paenibacillus fukuinensis D2
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
-
D41N
Q8KZM5
hydrolyzing activity against 100% deacetylated chitin is severely affected
D201A
-
mutant enzyme shows 38.5% of wild-type activity
D37E
-
relative activity to wild-type enzyme is 20-90%
D37N
-
relative activity to wild-type enzyme is 20-90%
D40G
-
relative activity to wild-type enzyme is 0.02-0.8%
D40N
-
relative activity to wild-type enzyme is 0.02-0.8%
D57A
-
0.5% activity of wild-type enzyme, less stable to temperature
D57A
-
reduced activity towards chitohexaose to 0.48% of that of wild-type
D57A
-
mutant enzyme shows 0.5% of wild-type activity
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
D57N
-
72% activity of wild-type enzyme
D57N
-
mutant enzyme shows 72% of wild-type activity
D6N
-
relative activity to wild-type enzyme is 20-90%
E197A
-
mutant enzyme shows 20% of wild-type activity
E22A
-
relative activity to wild-type enzyme is 0.02-0.8%
E22D
-
relative activity to wild-type enzyme is 0.02-0.8%
E22Q
-
relative activity to wild-type enzyme is 0.02-0.8%
R205A
-
relative activity to wild-type enzyme is 0.1-0.2%
R205H
-
relative activity to wild-type enzyme is 0.1-0.2%
R205Y
-
relative activity to wild-type enzyme is 0.1-0.2%
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
W101F
P33665
decreased midpoint temperature by about 7C
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
W227F
P33665
decreased midpoint temperature by about 7C
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
W28F
P33665
decreased midpoint temperature by about 7C
W28F/W101F
P33665
decreased midpoint temperature by about 11C
D201A
-
time-course is almost identical to that obtained by the wild-type
D40E
P33665
lower activity than mutant D40G
D40G
P33665
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
D40G
-
reduces activity to 2%
D40G/T45D
P33665
reaction time is 100 min. It has 0.1% of wild-type specific activity when tested on chitosan substrate
D40G/T45E
P33665
has 0.03% of wild-type specific activity when tested on chitosan substrate
D40N
P33665
lower activity than mutant D40G
E36A
P33665
reaction time is 10 min
E36A/D40G
P33665
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
E36D
P33665
reaction time is 10 min
E36N
P33665
reaction time is 10 min
E36Q
P33665
reaction time is 10 min
E36Q/D40G
P33665
reaction time is 100 min. Kcat is more than 5times lower than that of the single mutant D40G
T45E
P33665
has a very low residual activity. Activity of this mutant can not be enhanced by sodium azide
T45H
P33665
results in a complete loss of activity
T45S
P33665
reaction time is 20 min. It is quite active, keeps ca. 71% of the specific activity of the wild-type enzyme
V148T
P33665
has 10% of wild-type activity when tested on chitosan substrate
K218P
-
mutant enzyme shows 0.16% of wild-type activity
additional information
P33673
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
E188Q
-
inactive mutant enzyme
additional information
-
knock down of chitosanase expression in phytopathogenic fungus Fusarium solani affects its pathogenicity
additional information
Fusarium solani 114
-
knock down of chitosanase expression in phytopathogenic fungus Fusarium solani affects its pathogenicity
-
E302Y
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-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
E302K
Paenibacillus fukuinensis D2
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
-
additional information
Paenibacillus fukuinensis D2
-
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
-
E23Q
Q8KZM5
hydrolyzing activity against 100% deacetylated chitin is severely affected
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
E36Q
-
relative activity to wild-type enzyme is 20-90%
additional information
-
consensus enzyme mutant designed by multiple amino acid substitutions. Increase in transition temperature
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Bacillus cereus NTU-FC-4
-
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
-
food industry
-
has potential in the production of functional foods
industry
-
a cheap chitosanase for large-scale chitosan oligosaccharide production in industry
synthesis
Q9ALZ1
valuable enzyme for the commercial production of chitosan oligosaccharides and other chitosan hydrolysates
synthesis
-
valuable enzyme for the commercial production of chitosan oligosaccharides and other chitosan hydrolysates
-
food industry
Bacillus sp. TKU004
-
has potential in the production of functional foods
-
analysis
A9P7F5, A9P7F6, A9P7F7, A9P7F8, A9P7F9, A9P7G0, A9P7G1, A9P7G2, A9P7G3, -
development of a simple plate assay based on hydrolysis of soluble chitosan, for high-throughput screening for enzyme activity; development of a simple plate assay based on hydrolysis of soluble chitosan, for high-throughput screening for enzyme activity; development of a simple plate assay based on hydrolysis of soluble chitosan, for high-throughput screening for enzyme activity; development of a simple plate assay based on hydrolysis of soluble chitosan, for high-throughput screening for enzyme activity; development of a simple plate assay based on hydrolysis of soluble chitosan, for high-throughput screening for enzyme activity; development of a simple plate assay based on hydrolysis of soluble chitosan, for high-throughput screening for enzyme activity; development of a simple plate assay based on hydrolysis of soluble chitosan, for high-throughput screening for enzyme activity; development of a simple plate assay based on hydrolysis of soluble chitosan, for high-throughput screening for enzyme activity; development of a simple plate assay based on hydrolysis of soluble chitosan, for high-throughput screening for enzyme activity
industry
A9QUB2
application of chitosanase-overexpression strains
synthesis
Gongronella sp.
-
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
-
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
-
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
-
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
-
expression in yeast cells as a whole-cell biocatalyst. Protein is localized to cell surface
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
Serratia marcescens TKU011
-
usage of strain TKU011 on the microbial reclamation of food processing wastes such as shrimp shell wastes for the production of chitosanase
-
analysis
-
fluorimetric determination of transition temperature is a reliable method for rapid assessment of the thermal behaviour of chitosanases and applicable to strucuture-function studies
biotechnology
-
chitosanase is used as a tool for the biotechnological transformation of chitosan
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