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
LITERATURE
Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
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
COMMENTARY
LITERATURE
actase
-
-
actase
Bacillus cereus GU-02
-
-
-
AsChi
-
-
AsChi
Aeromonas sp. HG08
-
-
-
ChA
Penicillium sp. ZD-Z1
-
-
-
CHI
Paenibacillus fukuinensis D2
-
-
ChiN
Microbacterium sp. QU01
-
-
-
chitosan N-acetylglucosaminohydrolase
-
-
chitosan N-acetylglucosaminohydrolase
Acinetobacter calcoaceticus TKU024
-
-
-
chitosan N-acetylglucosaminohydrolase
-
-
chitosan N-acetylglucosaminohydrolase
Aspergillus sp. QD-2
-
-
-
chitosan N-acetylglucosaminohydrolase
-
-
chitosan N-acetylglucosaminohydrolase
Bacillus cereus D-11
-
-
-
chitosan N-acetylglucosaminohydrolase
-
-
chitosan N-acetylglucosaminohydrolase
Bacillus subtilis TKU002
-
-
-
chitosan N-acetylglucosaminohydrolase
Bambusa oldhamii, Gongronella sp.
-
-
chitosan N-acetylglucosaminohydrolase
Gongronella sp. JG
-
-
-
chitosan N-acetylglucosaminohydrolase
Janthinobacterium sp., Paenibacillus sp.
-
-
chitosan N-acetylglucosaminohydrolase
-
-
-
chitosan N-acetylglucosaminohydrolase
-
-
chitosan N-acetylglucosaminohydrolase
Serratia marcescens TKU011
-
-
-
chitosan N-acetylglucosaminohydrolase
-
-
chitosanase II
-
-
chitosanase II
Aspergillus fumigatus ATCC13073
-
-
-
ChiX
Microbacterium sp. QU01
-
-
-
CHO
-
gene name
CHO
-
gene name
-
Cho-GG
Bacillus thuringiensis JAM-GG01
-
-
-
ChoK
Bacillus sp. K17
-
;
-
Chs1
Pseudomonas sp. TKU015
-
-
Csn
Aspergillus fumigatus Y2K
-
-
Csn1
Fusarium solani 114
-
-
-
Csn2
Gongronella sp.
-
CsnB
Aspergillus fumigatus AfS35
-
-
-
CtoA
Amycolatopsis sp.CsO-2
-
Culf-Z
-
free enzyme
endo-chitosanase
-
-
endo-chitosanase
-
-
endo-chitosanase
-
-
endochitosanase
-
-
family 46 chitosanase
Amycolatopsis sp.CsO-2
-
GH-75 chitosanase
Gongronella sp.
-
GH-75 chitosanase
-
-
ImmB-Z
-
in situ immobilized enzyme
MH-K1 chitosanase
-
-
N174 chitosanase
-
-
PgChP
Penicillium chrysogenum AS51D
-
-
MH-K1 chitosanase
Bacillus circulans MH-K1
-
-
-
additional information
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
UNIPROT
SEQUENCE DB
SOURCE
Acinetobacter calcoaceticus TKU024
-
-
-
Manually annotated by BRENDA team
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
synonym Aspergillus fumigatus
UniProt
Manually annotated by BRENDA team
Aspergillus fumigatus AfS35
-
-
-
Manually annotated by BRENDA team
Aspergillus fumigatus ATCC13073
-
-
-
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 fumigatus Y2K
synonym Aspergillus fumigatus
UniProt
Manually annotated by BRENDA team
Aspergillus oryzae IAM2660
IAM2660
-
-
Manually annotated by BRENDA team
Aspergillus sp. QD-2
-
-
-
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
-
-
-
Manually annotated by BRENDA team
Bacillus cereus D-11
strain D-11
-
-
Manually annotated by BRENDA team
Bacillus cereus GU-02
-
-
-
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 cereus TKU030
-
-
-
Manually annotated by BRENDA team
Bacillus cereus TKU031
-
-
-
Manually annotated by BRENDA team
Bacillus circulans MH-K1
-
Uniprot
Manually annotated by BRENDA team
Bacillus circulans MH-K1
-
-
-
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
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
Bacillus subtilis TKU002
-
-
-
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
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
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
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.
-
-
-
Manually annotated by BRENDA team
Gongronella sp.
strain JG
-
-
Manually annotated by BRENDA team
Gongronella sp. JG
-
-
-
Manually annotated by BRENDA team
Hypocrea pachybasioides
-
-
-
Manually annotated by BRENDA team
Janthinobacterium sp.
-
-
-
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
-
UniProt
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
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
Streptomyces roseolus DH
-
-
-
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
Streptomyces zaomyceticus C6
-
-
-
Manually annotated by BRENDA team
commercial preparation of cellulase, isolation of a bifunctional chitosanase/cellulase
-
-
Manually annotated by BRENDA team
isolate GB2 from Indralaya Swamp South Sumatera
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
chitosanase is responsible for chitosan depolymerisation
metabolism
-
chitosanase is responsible for chitosan depolymerisation
-
physiological function
-
chitosanase is involved in the protection of bacteria against the antimicrobial effect of chitosan
physiological function
-
citosanase inhibits the growth of zygomycetes fungi Rhizopus and Mucor probably via its fungistatic effect
physiological function
Bacillus circulans MH-K1
-
citosanase inhibits the growth of zygomycetes fungi Rhizopus and Mucor probably via its fungistatic effect
-
physiological function
-
chitosanase is involved in the protection of bacteria against the antimicrobial effect of chitosan
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl beta-chitotrioside + H2O
4-methylumbelliferone + chitotriose + chitobiose + 4-methylumbelliferyl N-acetyl-beta-D-glucosaminide
show the reaction diagram
-
-
-
?
acetylated chitosan + H2O
?
show the reaction diagram
Bacillus circulans, Streptomyces sp., Bacillus circulans MH-K1
-
-
-
-
?
alginate + H2O
?
show the reaction diagram
Bacillus cereus, Bacillus cereus GU-02
-
12.7% activity compared to chitosan
-
-
?
alpha-chitin + H2O
?
show the reaction diagram
Bacillus cereus, Bacillus cereus TKU030
-
11.8% activity compared to chitosan
-
-
?
avicel + H2O
?
show the reaction diagram
-
63% activity compared to 50% deacetylated chitosan
-
-
?
beta-chitin + H2O
?
show the reaction diagram
-
85% activity with chitin (beta-type) compared to chitosan (95% DD)
-
-
?
beta-chitin + H2O
?
show the reaction diagram
Bacillus cereus, Bacillus cereus TKU030
-
68.7% activity compared to chitosan
-
-
?
beta-chitin + H2O
?
show the reaction diagram
Serratia marcescens subsp. sakuensis TKU019
-
85% activity with chitin (beta-type) compared to chitosan (95% DD)
-
-
?
beta-glucan + H2O
?
show the reaction diagram
Bacillus cereus, Bacillus cereus GU-02
-
32.7% activity compared to chitosan
-
-
?
carboxylmethyl cellulose + H2O
?
show the reaction diagram
Bacillus cereus, Bacillus cereus TKU030
-
61.9% activity compared to chitosan
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
-
5.3% of the activity with soluble chitosan
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
-
55% activity compared to 50% deacetylated chitosan
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
-
5.3% of the activity with soluble chitosan
-
-
?
carboxymethyl chitin + H2O
?
show the reaction diagram
-
isoform A shows 41.8% activity and isoform B 17.2% activity compared to 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
-
slow cleavage
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
substrate for isoforms B, C
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
58% activity compared to chitosan
-
-
?
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, Bacillus sp. R-4
-
-
-
-
?
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
-
-
?
chitin + H2O
?
show the reaction diagram
-
isoform A shows 7.8% activity and isoform B 10.8% activity compared to chitosan
-
-
?
chitobiose + H2O
glucosamine
show the reaction diagram
-
chitosanase II
-
?
chitohexaose + H2O
?
show the reaction diagram
-
-
-
-
?
chitohexaose + H2O
?
show the reaction diagram
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
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
-
-
-
-
?
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
Trichoderma koningii, Hypocrea pachybasioides
-
-
-
-
?
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 + H2O
?
show the reaction diagram
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
best substrate
-
-
?
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
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
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
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
-
100% activity with 50% deacetylated chitosan, 89% activity with 70% deacetylated chitosan, 91% activity with 98% deacetylated chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
-
100% activity with chitosan of 60% degrees of deacetylation
-
-
?
chitosan + H2O
?
show the reaction diagram
-
the enzyme hydrolyzes 70% deacetylated chitosan faster than fully deacetylated chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
the wild type chitosanase shows a clear preference for chitosan with high degrees of N-deacetylation (84-97%)
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
?
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
Aspergillus fumigatus AfS35
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Paenibacillus fukuinensis D2
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
?
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
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
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
Bacillus cereus TKU030
-
100% activity with chitosan of 60% degrees of deacetylation
-
-
?
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
Aspergillus fumigatus ATCC13073
-
the enzyme hydrolyzes 70% deacetylated chitosan faster than fully deacetylated chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. PI-7S
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
best substrate
-
-
?
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
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
-
-
?
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
-
-
chitosan oligosaccharides comprise oligomers with degree of polymerization mainly from dimers to pentamers
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
-
the enzyme produces various chitooligomers with different degrees of polymerisation from 3 to 8
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
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
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Streptomyces zaomyceticus C6
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Gongronella sp. JG, Bacillus cereus D-11
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Aspergillus fumigatus Y2K
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Serratia marcescens TKU011
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Bacillus cereus GU-02
-
-
chitosan oligosaccharides comprise oligomers with degree of polymerization mainly from dimers to pentamers
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
substrate with 85% deacetylation
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Bacillus cereus TKU031
-
-
the enzyme produces various chitooligomers with different degrees of polymerisation from 3 to 8
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Acinetobacter calcoaceticus TKU024
-
-
-
?
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
Aspergillus sp. QD-2
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Penicillium sp. ZD-Z1
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Bacillus subtilis TKU002
-
-
-
?
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
about 99% deacetylated substrate
-
?
chitosan + H2O
chitotriose + chitotetraose
show the reaction diagram
-
-
-
?
chitosan + H2O
chitotriose + chitotetraose
show the reaction diagram
-
-
?
chitosan + H2O
chitotriose + chitotetraose
show the reaction diagram
Bacillus thuringiensis JAM-GG01
-
-
-
?
chitosan + H2O
D-glucosamine + ?
show the reaction diagram
-
chitosan polymers with various degrees of deacetylation (10-94%) are susceptible to hydrolysis by both isoforms. Polymers with 50-70% deacetylation are most susceptible to hydrolysis by isoform A and polymers with 40-80% deacetylation are most susceptible to isoform B
-
?
chitosan + H2O
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
85% deacetylated chitin, transformants show a significant increase in chitosanase production by 2.1fold than control
-
?
chitosan + H2O
chitosan-oligosaccharides
show the reaction diagram
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
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 + H2O
chitosan oligomers
show the reaction diagram
-
chitodimer and chitotrimer as main products, a monoacetyl chitodimer and a monoacetyl chitotrimer but no significant amount of monomer glucosamine or chitotetramer is identified
?
chitosan 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
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
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
-
6% relative activity
-
-
?
colloidal chitin + H2O
?
show the reaction diagram
-
52% activity compared to 50% deacetylated chitosan
-
-
?
colloidal chitin + H2O
?
show the reaction diagram
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
-
best substrate
-
-
?
colloidal chitosan + H2O
?
show the reaction diagram
100% deacetylated chitin
-
-
?
colloidal chitosan + H2O
?
show the reaction diagram
Streptomyces roseolus DH
-
best substrate
-
-
?
colloidal chitosan + H2O
chitobiose + chitotriose + chitotetraose
show the reaction diagram
Gongronella sp., Gongronella sp. JG-2005
85% deacetylated, Csn2 displays stronger hydrolysis capability against colloidal chitosan than soluble chitosan
-
?
fucoidan + H2O
?
show the reaction diagram
Bacillus cereus, Bacillus cereus GU-02
-
16.9% activity compared to chitosan
-
-
?
Glc-beta-(1->4)-Glc-beta-(1->4)-beta-(1->4)-GlcNAc-GlcN-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4) + H2O
?
show the reaction diagram
Aspergillus fumigatus, Aspergillus fumigatus ATCC13073
-
-
-
-
?
Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-beta-(1->4)-GlcNAc + H2O
?
show the reaction diagram
Aspergillus fumigatus, Aspergillus fumigatus ATCC13073
-
-
-
-
?
Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-GlcN-beta-(1->4) + H2O
?
show the reaction diagram
-
-
-
-
?
Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-GlcN-beta-(1->4) + H2O
?
show the reaction diagram
-
-
-
-
?
GlcN-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4) + H2O
?
show the reaction diagram
Streptomyces roseolus, Streptomyces roseolus DH
-
-
-
-
?
GlcN-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-beta-(1->4)-GlcNAc + H2O
?
show the reaction diagram
-
-
-
-
?
GlcN-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4) + H2O
triglucosamine + diglucosamine + tetraglucosamine
show the reaction diagram
-
-
triglucosamine is the main product
?
GlcN-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-GlcN-beta-(1->4) + H2O
?
show the reaction diagram
-
-
-
?
GlcN-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-GlcN-beta-(1->4) + H2O
GlcN-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4) + Glc-beta-(1->4)-Glc-beta-(1->4) + GlcN-beta-(1->4)-GlcN-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)
show the reaction diagram
-
best substrate
GlcN-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4) is the main product
?
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 chitin + H2O
?
show the reaction diagram
-
11% activity compared to colloidal chitosan
-
-
?
glycol chitin + H2O
?
show the reaction diagram
-
isoform A shows 29.7% activity and isoform B 14.1% activity compared to chitosan
-
-
?
glycol chitin + H2O
?
show the reaction diagram
Streptomyces roseolus DH
-
11% activity compared to colloidal chitosan
-
-
?
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
activity is ca. 4fold higher than toward chitosan
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
Gongronella sp.
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
-
12% activity compared to colloidal chitosan
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
Paenibacillus fukuinensis D2
-
-
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
Streptomyces roseolus DH
-
12% activity compared to colloidal chitosan
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
Aspergillus fumigatus KH-94
-
-
-
-
?
glycol chitosan + H2O
?
show the reaction diagram
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
-
?
hexa-N-acetylchitohexaose + H2O
?
show the reaction diagram
-
-
-
-
?
hyaluronic acid + H2O
?
show the reaction diagram
Bacillus cereus, Bacillus cereus GU-02
-
26.7% activity compared to 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
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.
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
85% deacetylated, Csn2 displays 14% of the activity for colloidal chitosan
-
-
?
sulfate chitin + H2O
?
show the reaction diagram
-
9.6% activity compared to 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
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
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
-
-
-
-
?
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
-
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
-
-
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
-
-
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
-
-
most susceptible substrate is: 100% deacetylated chitosan
-
?
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, most susceptible substrate is: 80% deacetylated chitosan
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
Bacillus circulans MH-K1
-
-
-
?
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. PI-7S
-
-
-
?
chitosan + H2O
additional information
-
-
hydrolysis of: glycol chitosan
-
?
chitosan + H2O
additional information
-
-
-
-
?
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
-
Bacillus sp. K-1
-
-
-
?
chitosan + H2O
additional information
-
Bacillus sp. K-1
-
-
-
?
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
?
methylcellulose + H2O
?
show the reaction diagram
14% activity compared to 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
?
-
-
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
?
-
-
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
?
-
-
slow cleavage of: pentamer of N-acetylglucosamine, glucosamine oligomers
-
-
-
additional information
?
-
-
no activity with methylcellulose
-
-
-
additional information
?
-
-
no activity with trimers or tetramers of N-acetylglucosamine, carboxymethylcellulose, dextran, galactan, polygalacturonic acid, laminaran, mucoran, pectin, pullulan, salicin, xylan, 4-nitrophenyl-beta-D-acetylglucosamine, 4-nitrophenyl-beta-D-glucosamine
-
-
-
additional information
?
-
-
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
?
-
-
no activity with colloidal chitin
-
-
-
additional information
?
-
-
no activity with colloidal chitin
-
-
-
additional information
?
-
-
the enzyme is constitutively produced, no activity on colloidal chitin
-
-
-
additional information
?
-
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.
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
?
-
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
?
-
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
?
-
does not hydrolyze microcrystalline cellulose, chitin, xylan, laminarin, pustulan, pachyman, mannan, or beta-1,3-1,4-glucan
-
-
-
additional information
?
-
-
the enzyme cannot hydrolyze colloidal chitin, carboxylmethyl cellulose, diglucosamine, triglucosamine, or tetraglucosamine
-
-
-
additional information
?
-
-
the enzyme does not hydrolyze colloidal chitin or carboxymethylcellulose
-
-
-
additional information
?
-
the enzyme does not react with chitin. Oligosaccharides with degree of polymerization above 4 are not hydrolyzed
-
-
-
additional information
?
-
-
the enzyme is not able to degrade chitin
-
-
-
additional information
?
-
-
the enzyme splits GlcN-GlcN and GlcNAc-GlcN bonds but not GlcNAc-GlcNAc or GlcN-GlcNAc bonds
-
-
-
additional information
?
-
does not hydrolyze microcrystalline cellulose, chitin, xylan, laminarin, pustulan, pachyman, mannan, or beta-1,3-1,4-glucan
-
-
-
additional information
?
-
Streptomyces sp. No. 6
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
-
additional information
?
-
Streptomyces zaomyceticus C6
-
the enzyme is not able to degrade chitin
-
-
-
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
?
-
-
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
?
-
the enzyme does not react with chitin. Oligosaccharides with degree of polymerization above 4 are not hydrolyzed
-
-
-
additional information
?
-
Bacillus circulans MH-K1
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
-
additional information
?
-
no hydrolysis of chitobiose and chitotriose
-
-
-
additional information
?
-
Pseudomonas sp. TKU015
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
?
-
Streptomyces roseolus DH
-
the enzyme cannot hydrolyze colloidal chitin, carboxylmethyl cellulose, diglucosamine, triglucosamine, or tetraglucosamine
-
-
-
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
?
-
does not hydrolyze colloidal chitin and carboxylmethyl cellulose
-
-
-
additional information
?
-
Bacillus cereus TKU030
-
no activity with colloidal chitin
-
-
-
additional information
?
-
Aspergillus fumigatus ATCC13073
-
the enzyme does not hydrolyze colloidal chitin or carboxymethylcellulose, the enzyme splits GlcN-GlcN and GlcNAc-GlcN bonds but not GlcNAc-GlcNAc or GlcN-GlcNAc bonds
-
-
-
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
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
-
-
-
-
?
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
Trichoderma koningii, Hypocrea pachybasioides
-
-
-
-
?
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
G2NRC4
-
-
-
?
chitosan + H2O
?
show the reaction diagram
J7G4R4
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Q93IE7
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
best substrate
-
-
?
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
-
100% activity with 50% deacetylated chitosan, 89% activity with 70% deacetylated chitosan, 91% activity with 98% deacetylated chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
-
100% activity with chitosan of 60% degrees of deacetylation
-
-
?
chitosan + H2O
?
show the reaction diagram
-
the enzyme hydrolyzes 70% deacetylated chitosan faster than fully deacetylated chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
P33665
the wild type chitosanase shows a clear preference for chitosan with high degrees of N-deacetylation (84-97%)
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Q875I9
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
-
chitosan oligosaccharides comprise oligomers with degree of polymerization mainly from dimers to pentamers
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
-
the enzyme produces various chitooligomers with different degrees of polymerisation from 3 to 8
?
chitosan + H2O
D-glucosamine + ?
show the reaction diagram
-
chitosan polymers with various degrees of deacetylation (10-94%) are susceptible to hydrolysis by both isoforms. Polymers with 50-70% deacetylation are most susceptible to hydrolysis by isoform A and polymers with 40-80% deacetylation are most susceptible to isoform B
-
?
chitosan + H2O
chitosan oligomers
show the reaction diagram
A7KBW5
-
chitodimer and chitotrimer as main products, a monoacetyl chitodimer and a monoacetyl chitotrimer but no significant amount of monomer glucosamine or chitotetramer is identified
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
-
-
-
?
chitosan + H2O
?
show the reaction diagram
J7G4R4
-
-
-
?
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
Aspergillus fumigatus AfS35
-
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Streptomyces zaomyceticus C6
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Gongronella sp. JG, Bacillus cereus D-11
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Paenibacillus fukuinensis D2
Q93IE7
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Aspergillus fumigatus Y2K
Q875I9
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Serratia marcescens TKU011
-
-
-
?
chitosan + H2O
?
show the reaction diagram
G2NRC4
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Aspergillus fumigatus KB-1
-
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus circulans MH-K1
-
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Bacillus cereus GU-02
-
-
chitosan oligosaccharides comprise oligomers with degree of polymerization mainly from dimers to pentamers
?
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
chitosan oligomers
show the reaction diagram
A7KBW5
-
chitodimer and chitotrimer as main products, a monoacetyl chitodimer and a monoacetyl chitotrimer but no significant amount of monomer glucosamine or chitotetramer is identified
?
chitosan + H2O
?
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
chitosan oligosaccharides
show the reaction diagram
Bacillus cereus TKU031
-
-
the enzyme produces various chitooligomers with different degrees of polymerisation from 3 to 8
?
chitosan + H2O
?
show the reaction diagram
Bacillus cereus TKU030
-
100% activity with chitosan of 60% degrees of deacetylation
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Acinetobacter calcoaceticus TKU024
-
-
-
?
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
Aspergillus fumigatus ATCC13073
-
the enzyme hydrolyzes 70% deacetylated chitosan faster than fully deacetylated chitosan
-
-
?
chitosan + H2O
?
show the reaction diagram
Bacillus sp. PI-7S
-
-
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Aspergillus sp. QD-2
-
-
-
?
chitosan + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
best substrate
-
-
?
chitosan + H2O
chitosan oligosaccharides
show the reaction diagram
Bacillus subtilis TKU002
-
-
-
?
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
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+
-
5-10 mM, activity is increased by about 1.6fold
Ca2+
-
1 mM, 20% activation
Ca2+
-
35% increase in activity
Ca2+
5 mM activates by 11% at 25C for 30 min
Ca2+
-
activates
Ca2+
-
stimulates activity
Ca2+
Gongronella sp.
-
activates
Ca2+
-
isoform B shows 117% residual activity at 1 mM
Ca2+
-
chitosan degrading activity is enhanced by 15% in the presence of calcium ions (8 mM)
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.
stimulates Csn2 at 1 mM
Cu2+
-
stimulates activity
CuCl2
-
1 mM, 19% enhancement of activity
Fe2+
-
stimulates activity
K+
-
slight activation
K+
-
activates enzyme A
K+
-
activates
Mg2+
-
activates
Mg2+
-
slightly activated by Mg2+
Mg2+
-
slightly activated by Mn2+
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+
-
activates 46% at 1 mM
Mn2+
Gongronella sp.
-
activates
Na+
-
activates
Na+
-
isoform A shows 111% activity at 5 mM
Sr2+
Gongronella sp.
-
activates
Zn2+
-
stimulates activity
Zn2+
-
activates
Zn2+
-
isoform B shows 111% residual activity at 1 mM
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
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+
additional information
-
Ba2+ and Ca2+ show nearly no effect on relative enzymatic activity
additional information
-
not influenced by Cu2+, Mg2+, K+, and EDTA
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-dinitro-1-fluorbenzene
Ficus sp.
-
5 mM, 24% inhibition
2,4-Dinitro-1-fluorobenzene
-
isoform A shows 95% residual activity at 0.625 mM, isoform B shows 84% residual activity at 0.625 mM
2-Hydroxy-5-nitrobenzyl bromide
-
69% inhibition at 5 mM, 33% inhibition at 1 mM
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
Ag+
-
strong inhibition
Ag+
10 mM inhibits more than 50% of the enzyme activity
Ag+
-
isoform A shows 91% residual activity at 1 mM, isoform B shows 86% residual activity at 1 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+
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
chitosan
substrate inhibition with Ki of 01.66 mg/ml
chitosan
the wild type enzyme shows a Ki value of 1.547 mg/ml
Chloramine T
-
-
Co2+
1 mM inhibits by 86%, with colloidal chitosan as substrate
Co2+
-
13% inhibition at 1 mM
Co2+
-
60% inhibition at 1 mM
Co2+
-
38% residual activity at 10 mM
CoCl2
-
10 mM, 33% inhibition
Cs+
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+
5 mM completely inhibits at 25C for 30 min
Cu2+
1 mM completely inhibits, with colloidal chitosan as substrate
Cu2+
-
5 mM inhibits by 92% at 37C for 30 min
Cu2+
Gongronella sp.
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
Cu2+
10 mM inhibits more than 50% of the enzyme activity
Cu2+
-
27% residual activity at 10 mM
Cu2+
-
8.1% residual activity at 5 mM
CuCl2
-
10 mM, 69% inhibition
EDTA
Gongronella sp.
-
1 mM, 78% residual activity
EDTA
10 mM inhibits by 86% at 25C for 30 min
EDTA
-
5 mM completely inhibits at 37C for 30 min
EDTA
Gongronella sp.
-
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
EDTA
-
68% residual activity at 10 mM
EDTA
-
73.4% residual activity at 5 mM
EDTA
-
slightly inactivated at 0.5 mM
ethyl acetimidate
-
isoform B shows 56% residual activity at 250 mM
Fe2+
-
50% inhibition of chitosanase I
Fe2+
-
1 mM, 60% inhibition
Fe2+
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
Fe2+
-
18.7% residual activity at 5 mM
Fe3+
-
49% inhibition of chitosanase I
Fe3+
-
inhibits 60% at 1 mM
Fe3+
-
35% inhibition at 1 mM
Fe3+
-
strong inhibition
Fe3+
strongly inhibited by 10 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+
1 mM, 68% inhibition
Hg2+
-
1 mM, 44% inhibition
Hg2+
-
1 mM, 80% loss of activity
Hg2+
-
complete deactivation
Hg2+
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
Hg2+
-
strong inhibition
Hg2+
-
isoform B shows 77% residual activity at 0.25 mM
KCl
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
Mg2+
-
slightly inactivated at 0.5 mM
Mn2+
-
42% inhibition of chitosanase I
Mn2+
-
inhibition of chitosanase A and B
Mn2+
1 mM, 69% inhibition
Mn2+
5 mM completely inhibits at 25C for 30 min
Mn2+
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
Mn2+
-
45% residual activity at 10 mM
Mn2+
-
2.3% residual activity at 5 mM
Mo2+
-
94% inhibition of chitosanase I and 88% inhibition of chitosanase II
N-Acetylimidazole
-
isoform A shows 96% residual activity at 5 mM, isoform B shows 84% residual activity at 5 mM
N-bromosuccinimide
-
-
N-bromosuccinimide
-
-
N-bromosuccinimide
-
-
N-bromosuccinimide
-
-
N-bromosuccinimide
-
-
N-bromosuccinimide
Ficus sp.
-
0.25 mM, 96% loss of activity
N-bromosuccinimide
-
isoform A shows 12% residual activity at 2.5 mM, isoform B is completely inhibited at 2.5 mM
Na2SO4
-
complete inhibition at 100 mM
NaCl
0.4 M, 50% inhibition
NaCl
-
complete inhibition at 100 mM
NaCl
-
slightly inactivated at 0.5 mM
Ni2+
-
38% residual activity
Ni2+
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
phenylmethylsulfonyl fluoride
-
isoform B shows 86% residual activity at 2.5 mM
PMSF
5 mM completely inhibits at 25C for 30 min
PMSF
-
5 mM inhibits by 73% at 37C for 30 min
reduced glutathione
-
-
SDS
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
SDS
strongly inhibited by 0.1% (w/v) SDS
SDS
-
51.3% 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
-
-
-
TKUPSP017
-
chitosanase is inhibited completely by 0.05% (w/v) TKUPSP017
-
TKUPSP074
-
chitosanase is inhibited completely by 0.05% (w/v) TKUPSP074
-
Trimers of N-acetylglucosamine
-
-
-
Triton X-100
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
TritonX-100
-
48.4% residual activity at 1% (v/v)
-
Tween 20
0.5% nonionic surfactant of Tween 20 inhibits by 16% at 25C for 30 min
Tween 20
-
72% inhibtion at 1% w/v
Tween 20
-
57.2% residual activity at 0.5% (v/v)
Tween 40
0.5% nonionic surfactant of Tween 40 inhibits by 29% at 25C for 30 min
Tween 40
-
51.2% residual activity at 1% (v/v)
Tween 80
-
79% inhibtion at 1% w/v
Woodward's reagent
-
N-ethyl-5-phenylisoazoline-3'-sulfonate, isoform A shows 95% residual activity at 50 mM, isoform B shows 1% residual activity at 50 mM
-
Zn2+
-
about 43% loss of activity
Zn2+
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
Zn2+
-
50% residual activity at 10 mM
Zn2+
-
41.5% residual activity at 5 mM
Zn2+
-
slightly inactivated at 0.5 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
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
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
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
-
additional information
-
not inhibited by phenylmethylsulfonyl fluoride, TKUPSP018, TKUPSP073, TKUPSP011, TKUPSP035, TKUPSP080, and TKUPSP062
-
additional information
-
not inhibited by diethyl dicarbonate, 1,2-cyclohexanedione, and p-hydroxymercuribenzoate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activates 28% at 1 mM
Chelating agents
-
especially EDTA, activate
Co2+
-
2.5 mM, 16% increase in activity
diethyl dicarbonate
-
isoform A shows 111% activity at 2.5 mM
p-hydroxymercuribenzoate
-
isoform A shows 112% activity at 0.5 mM
Triton X-100
2% nonionic surfactant of Triton X-100 activates by 51% at 25C for 30 min
Tween 20
2% nonionic surfactant of Tween 20 activates by 38% at 25C for 30 min
Tween 40
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.21
4-methylumbelliferyl beta-chitotrioside
-
40C, pH 5.5
0.000327
chitosan
-
at pH 8.5 and 37C
7.99
Glc-beta-(1->4)-Glc-beta-(1->4)-beta-(1->4)-GlcNAc-GlcN-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)
-
at pH 5.7 and 37C
-
0.65
GlcN-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-beta-(1->4)-GlcNAc
-
at pH 5.7 and 37C
-
2.9
chitohexaose
-
40C, pH 5.5
additional information
chitosan
-
Km value is 10 mg/ml
1.2
GlcN-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-GlcN-beta-(1->4)
-
at pH 5.7 and 37C
-
additional information
additional information
-
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
-
-
-
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
-
1.4 mg/ml: 5% or 30% acetylated chitosan
-
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
38.4
30% N-acetylated chitosan
Streptomyces sp.
P33665
40C, pH 5.5, W227F
-
42.1
30% N-acetylated chitosan
Streptomyces sp.
P33665
40C, pH 5.5, W28F/W101F
-
45.1
30% N-acetylated chitosan
Streptomyces sp.
P33665
40C, pH 5.5, W101F
-
50.1
30% N-acetylated chitosan
Streptomyces sp.
P33665
40C, pH 5.5, W28F
-
71.4
30% N-acetylated chitosan
Streptomyces sp.
P33665
40C, pH 5.5, wild-type
-
0.000081
4-methylumbelliferyl beta-chitotrioside
Streptomyces sp.
-
40C, pH 5.5
107
chitohexaose
Streptomyces sp.
-
40C, pH 5.5
0.0167
chitosan
Streptomyces sp. N174
P33665
mutant D40G/T45D, assayed as the amount of D-glucosamine released from chitosan
0.024
chitosan
Streptomyces sp. N174
P33665
mutant E36A/D40G, assayed as the amount of D-glucosamine released from chitosan
0.0368
chitosan
Streptomyces sp. N174
P33665
mutant T45E, assayed as the amount of D-glucosamine released from chitosan
0.0683
chitosan
Streptomyces sp. N174
P33665
mutant E36Q/D40G, assayed as the amount of D-glucosamine released from chitosan
0.44
chitosan
Streptomyces sp. N174
P33665
mutant D40G, assayed as the amount of D-glucosamine released from chitosan
0.9
chitosan
Streptomyces sp.
P33665
mutant enzyme R42K, at 37C in 50 mM sodium acetate buffer (pH 5.5)
1.6
chitosan
Streptomyces sp.
P33665
mutant enzyme R42E at 37C in 50 mM sodium acetate buffer (pH 5.5)
2.3
chitosan
Sus scrofa
-
40C, pH 4, isoform PSC-II
5.9
chitosan
Sus scrofa
-
40C, pH 4, isoform PSC-I
6.2
chitosan
Sus scrofa
-
40C, pH 4, isoform PSC-III
6.5
chitosan
Streptomyces sp.
G2NRC4
chitosan with 75-85% deacetylation, at pH 6.0 and 45C
6.827
chitosan
Streptomyces sp. N174
P33665
mutant E36N, assayed as the amount of D-glucosamine released from chitosan
8.34
chitosan
Streptomyces sp. N174
P33665
mutant E36D, assayed as the amount of D-glucosamine released from chitosan
10
chitosan
Streptomyces sp.
G2NRC4
chitosan with less than 75% deacetylation, at pH 6.0 and 45C
10.48
chitosan
Streptomyces sp. N174
P33665
mutant T45S, assayed as the amount of D-glucosamine released from chitosan
10.7
chitosan
Streptomyces sp.
P33665
wild type enzyme, at 37C in 50 mM sodium acetate buffer (pH 5.5)
11.2
chitosan
Streptomyces sp.
G2NRC4
chitosan with more than 90% deacetylation, at pH 6.0 and 45C
11.47
chitosan
Streptomyces sp. N174
P33665
mutant E36A, assayed as the amount of D-glucosamine released from chitosan
11.66
chitosan
Streptomyces sp. N174
P33665
mutant E36Q, assayed as the amount of D-glucosamine released from chitosan
12.4
chitosan
Streptomyces sp. N174
P33665
wild-type, assayed as the amount of D-glucosamine released from chitosan
126.5
chitosan
Paenibacillus sp.
J7G4R4
at pH 4.8 and 37C
205
chitosan
Microbacterium sp.
A7KBW5
at pH 5.6 and 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
Zn2+
Streptomyces roseolus
-
at pH 6.0 and 50C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0012
mutant enzyme D40G/R42E, at 37C in 50 mM sodium acetate buffer (pH 5.5)
0.002
-
culture supernatant
0.002
-
culture supernatant, at pH 4.0 and 40C
0.005316
-
culture supernatant
0.006
-
culture supernatant, at pH 7.0 and 60C
0.0065
-
crude extract, at pH and C
0.011
mutant T45E
0.018
mutant enzyme D40G/R42K, at 37C in 50 mM sodium acetate buffer (pH 5.5)
0.02
mutant D40G/T45E
0.032
-
enzyme HEWL
0.055
-
enzyme BCVC-4
0.06
culture supernatant
0.06
mutant D40G/T45D
0.07
mutant E36A/D40G
0.075
-
enzyme BCVC-3
0.087
-
enzyme BCVC-5
0.114
-
enzyme BCVC-6
0.177
-
after 88.5fold purification, at pH 4.0 and 40C
0.18
-
after 30fold purification, at pH 7.0 and 60C
0.243
-
isoform B, after 115.1fold purification, at pH 4.5 and 50C
0.3
mutant E36Q/D40G
0.402
-
pH 5.2, 60C
0.567
-
enzyme Yam
0.753
-
isoform A, after 115.1fold purification, at pH 4.5 and 50C
0.9
mutant enzyme R42E at 37C in 50 mM sodium acetate buffer (pH 5.5)
1.291
-
enzyme BCLVC
1.38 - 1.53
-
activity of enzyme immobilized on liposomes
1.4
mutant enzyme R42K, at 37C in 50 mM sodium acetate buffer (pH 5.5)
1.6
mutant enzyme D40G, at 37C in 50 mM sodium acetate buffer (pH 5.5)
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
65fold purified enzyme
5.84
-
after Sephadex G-100 chromatography
7
-
50fold purified enzyme
7.59
-
culture filtrate, at pH 5.7 and 37C
8.8
-
after 1.16fold purification, at pH 5.7 and 37C
9.3
culture supernatant
10
-
after treatment with hydroxylapatite
17.1
-
culture broth, pH 6.0, 50C
17.2
-
enzyme I after after Sephadex G-100 chromatography
35.61
-
after Sephadex G-75 chromatography
35.61
-
-
38.8
-
enzyme II after after Sephadex G-100 chromatography
42.7
-
after second Mono Q HR 5/5 chromatography, enzyme A
51.8
-
after TSKgel G2000SWXL chromatography
52.9
wild type enzyme, at 37C in 50 mM sodium acetate buffer (pH 5.5)
58.9
-
Bio-Gel A eluate of the recombinant protein
59.1
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
412
-
after 24.1fold purification, pH 6.0, 50C
444
-
after Superdex 75 HR gel filtration
489.8
-
isoenzyme PSC-II
733.5
-
isoenzyme PSC-III
742.6
-
isoenzyme PSC-I
850
-
purified enzyme
2819
-
after DEAE-Sephacel ion exchange chromatography
additional information
Ficus sp.
-
-
additional information
-
between 270-290 U/mg, recombinant chitosanase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
isoenzyme PSC-III
4.5
Ficus sp.
-
-
4.5 - 5.5
-
chitosanase II
4.5 - 6
-
with 30% or 5% acetylated chitosan
4.5 - 6
-
at 25C
4.6 - 4.8
Gongronella sp.
-
-
4.9
Macrotermes estherae
-
enzyme from males
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 - 5.2
-
optimal at an ionic strength of 0.2
5 - 7
Janthinobacterium sp.
-
-
5.2
-
chitosan hydrolysis
5.3
Macrotermes estherae
-
enzyme from winged females
5.5
-
chitosanase II
5.5
-
chitosanase I
5.5
-
wild-type enzyme
5.5
Hypocrea pachybasioides, Trichoderma koningii
-
-
5.5 - 6
-
-
5.5 - 6.9
-
-
5.6
-
assay at
5.6
Gongronella sp.
-
-
5.8
Macrotermes estherae
-
enzyme from soldiers
6
-
optimum pH for free and in situ immobilized enzymes
6 - 6.5
-
-
6.2
Macrotermes estherae
-
enzyme from workers
6.2
-
chitosanase ChiN
6.5
-
carboxymethylcellulose hydrolysis
6.5
-
chitosanase I
6.5
-
mutant YM20
6.6
-
chitosanase ChiX
7
-
and 5.0, at pH 7.0 higher chitosanase activity than at pH 5.0
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
-
both purified isoforms A and B retain approximately 70-100% relative activity between pH 3.0 and 6.0 but rapidly lose activity above pH 6.0
3.5 - 8.5
-
chitosanase II
3.8 - 6.5
the enzyme keeps at least 80% of activity between pH 3.8 and 6.5
4 - 6
-
pH 4.0: about 45% of maximal activity, pH 6.0: about 25% of maximal activity
4 - 6.5
-
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 - 7.5
more than 50% activity between pH 4.0 and 7.5, more than 90% activity between pH 4.5 and 7.0
4 - 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.
-
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 - 11
-
about 55% activity at pH 3.0, about 57% activity at pH 5.0, about 80% activity at pH 6.0, 100% activity at pH 9.0, about 75% activity at pH 10.0-11.0
5 - 8
-
more than 80% of maximum activity
6
assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at
6
-
loss of 50% of activity
6 - 9
-
isoenzyme PSC-III is stable in this range
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23 - 25
Macrotermes estherae
-
enzyme from soldiers
24
Macrotermes estherae
-
enzyme from males
24 - 26
Macrotermes estherae
-
enzyme from workers
25
Macrotermes estherae
-
enzyme from winged females
30
-
PSC-III
30 - 50
-
optimum temperature for free enzyme
40
-
PSC-I and PSC-II
40
-
wild-type enzyme
40 - 65
-
optimum temperature for in situ immobilized enzyme
45
-
assay at
45
Janthinobacterium sp.
-
-
45 - 55
-
-
50
-
at pH 6.5
50
-
enzyme B
50
-
; enzyme A
50
-
chitosanase ChiN
50
assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at
50
Gongronella sp.
-
-
50
-
mutant YM18
50
-
isoform CHSA1
50 - 60
-
chitosanase II
55
-
enzyme A
55 - 60
Gongronella sp.
optimal reaction temperature is between 55C and 60C
55 - 60
Gongronella sp.
-
-
60
-
chitosanase I
60
-
chitosanase ChiX
60
-
in acetate buffer (pH 5.6)
60
-
isoform CHSA2
60
-
isoform B
60 - 70
-
-
65
Ficus sp.
-
-
70
-
chitosanase II
70
-
mutant YM20
70
-
isoform A
70 - 80
-
chitosanase I
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
ORGANISM
UNIPROT
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
27 - 50
-
about 55% activity at 27C, about 62% activity at 32C, 100% activity at 37C, about 90% activity at 42C, and about 80% activity at 50C
30 - 50
-
-
30 - 50
-
about 45% activity at 30C, about 85% activity at 35C, 100% activity at 40C, about 30% activity at 50C
40 - 70
-
40C: about 40% of maximal activity, 70C: about 15% of maximal activity
45 - 75
about 50% activity at 45C, about 80% activity at 50C, 100% activity from 55-65C, about 80% activity at 70C, about 50% activity at 75C
55 - 70
-
55C: about 85% of maximal activity, 70C: about 90% of maximal activity
60
-
the enzyme retains more than 80% of activity at 60C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
-
isoelectric focusing, in plants infected either with Glomus mosseae or Glomus intraradices
4.3
-
isoform A, isoelectric focusing
4.4
-
isoelectrofocusing, PSC-III
4.5
-
isoelectric focusing
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
isoelectric focusing
5.1
-
isoelectric focusing
5.8
Gongronella sp.
-
isoelectric focusing
5.9
-
isoelectric focusing
6.5
-
isoelectric focusing
7.11
-
sequence analysis
7.3 - 7.4
-
chitosanase I
8.3
-
isoelectric focusing
8.3
-
isoelectric focusing
8.8
-
isoelectric focalization
9.2
-
density gradient column electrofocusing and acrylamide gel electrofocusing
9.2
-
isoform B, isoelectric focusing
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
COMMENTARY
LITERATURE
SOURCE
Aspergillus fumigatus AfS35
-
-
-
Manually annotated by BRENDA team
-
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
-
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
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the discoidin domain of chitosanase is required for binding to the fungal cell wall
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 cereus GU-02, 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, Streptomyces zaomyceticus C6
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10000
-
gel filtration
646742
16600
Ficus sp.
-
gel filtration
665277
18000
-
gel filtration
697120
18780
-
sequence analysis
697120
22500
-
chitosanase I
646788
23000
-
gel filtration
646790
23000
-
gel filtration
646792
23380
-
mass spectrometry, chitosanase II
646766
24000
-
gel filtration
646792
24000
-
gel filtration
664395
25000
-
gel filtration
646749, 646792, 697133
25590
sequence analysis
696815
26000
-
gel filtration
646792
26490
Amycolatopsis sp.CsO-2
sequence analysis
697996
27000
-
gel filtration
646746
27000
-
gel filtration
646752
27000
-
-
646792
27000
-
gel filtration
646792
28000
-
-
646791
28000
purified protein
696815
28000
Gongronella sp.
gel filtration
697126
28900
-
deduced from amino acid sequence
646792
29000
-
gel filtration
646744
29000
-
-
646771, 646792
29000
-
gel filtration
646792
29020
-
deduced from nucleotide sequence
646747
29020
-
-
646770
30000
-
gel filtration
646740
30000
-
gel filtration
646741, 646792
30000
-
gel filtration
646792
30000
-
chitosanase ChiN
664430
31000
-
gel filtration
646743
31000
Macrotermes estherae
-
enzyme from males and winged females
646764, 646783
31000
-
gel filtration
646792
31400
-
gel filtration
646793
31480
-
sequence analysis
697133
34000
-
-
646786
35000
Macrotermes estherae
-
enzyme from soldiers
646764, 646783
35000
-
gel filtration
715729
36000
-
gel filtration
646774
37500
-
gel filtration, isoform PSC-I
646783
40000
Macrotermes estherae
-
enzyme from workers
646764, 646783
40600
-
gel filtration, isoform PSC-II
646783
42000
-
gel filtration
646772
43000
-
gel filtration
714540
43700
-
gel filtration, isoform PSC-III
646783
63000
-
enzyme B, gel filtration
646748
64000
-
gel filtration
678006
70000
-
gel filtration
707019
79000
-
enzyme A, gel filtration
646748
81000
-
chitosanase ChiX
664430
95000
-
gel filtration
731243
100000
-
gel filtration
646792
108000
-
chitosanase II
646788
111200
-
mass spectrometry, chitosanase I
646766
SUBUNITS
ORGANISM
UNIPROT
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
?
x * 28200, calculated
?
Gongronella sp.
-
x * 90000, SDS-PAGE
?
-
x * 75000, SDS-PAGE
?
-
x * 43000, SDS-PAGE
?
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
?
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
?
x * 40000, SDS-PAGE; x * 41800, calculated from amino acid sequence
?
-
x * 36000-110000, SDS-PAGE and zymogram technique
?
-
x * 23525, MALDI-TOF mass spectrometry; x * 30000, SDS-PAGE
?
x * 28000, SDS-PAGE
?
-
x * 27000, isoform CHSA1, SDS-PAGE; x * 66000, isoform CHSA2, SDS-PAGE
?
-
x * 41000, SDS-PAGE
?
-
x * 16400, isoform B, SDS-PAGE; x * 24500, isoform A, SDS-PAGE
?
Gongronella sp.
-
x * 28000, SDS-PAGE
?
Janthinobacterium sp.
-
x * 33000, SDS-PAGE
?
-
x * 40000, SDS-PAGE
?
-
x * 21000, SDS-PAGE
?
-
x * 41000, SDS-PAGE
?
-
x * 43000, SDS-PAGE
?
-
x * 16400, isoform B, SDS-PAGE; x * 24500 + x * 16400, purified isoform A is composed of a major and a minor chitosanase isoform, SDS-PAGE
?
-
x * 47000, SDS-PAGE
?
Acinetobacter calcoaceticus TKU024
-
x * 27000, isoform CHSA1, SDS-PAGE; x * 66000, isoform CHSA2, SDS-PAGE
-
?
Acinetobacter sp. C-17
-
x * 35400, SDS-PAGE
-
?
Aspergillus fumigatus ATCC13073
-
x * 23525, MALDI-TOF mass spectrometry; x * 30000, SDS-PAGE
-
?
Aspergillus fumigatus Y2K
-
x * 28000, SDS-PAGE
-
?
Aspergillus oryzae IAM2660
-
x * 135000, SDS-PAGE, enzyme II; x * 40000, SDS-PAGE, enzyme I
-
?
Bacillus cereus D-11
-
x * 41000, SDS-PAGE
-
?
Bacillus cereus S1
-
x * 45000, SDS-PAGE
-
?
Bacillus cereus TKU030
-
x * 43000, 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
-
-
-
?
-
x * 45000, SDS-PAGE
-
?
Bacillus subtilis CH2
-
x * 29000, SDS-PAGE
-
?
Bacillus thuringiensis JAM-GG01
-
x * 43000, SDS-PAGE
-
?
-
x * 90000, SDS-PAGE
-
?
Gongronella sp. JG
-
x * 28000, SDS-PAGE
-
?
-
x * 41000, SDS-PAGE, x * 41241, calculated
-
?
-
x * 28200, calculated
-
?
-
x * 40000, SDS-PAGE; x * 40000, SDS-PAGE; x * 41800, calculated from amino acid sequence
-
?
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
-
?
Serratia marcescens TKU011
-
x * 21000, SDS-PAGE
-
?
Streptomyces roseolus DH
-
x * 41000, SDS-PAGE
-
?
Streptomyces sp. No. 6
-
x * 26000, SDS-PAGE; x * 29500, SDS-Page
-
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.
1 * 28000, SDS-PAGE
monomer
-
1 * 29000, SDSPAGE
monomer
Amycolatopsis sp.CsO-2
1 * 30000, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 36000, SDS-PAGE
monomer
-
1 * 95000, 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
-
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
-
monomer
Streptomyces zaomyceticus C6
-
1 * 95000, SDS-PAGE
-
additional information
-
structure comparisons of wild-type and mutant enzymes, overview
additional information
-
the extracellular enzyme, composed of 797 amino-acid residues, has discoidin domains, DDs, also called discoidin-like domain, discoidin motif, FA58C or F5/8C, in its C-terminal region, domain structure, overview. The discoidin domain of chitosanase is required for binding to the fungal cell wall, functional analysis, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
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
Penicillium chrysogenum AS51D
-
-
-
additional information
-
no glucosamine or other carbohydrate
additional information
Streptomyces sp. No. 6
-
no glucosamine or other carbohydrate
-
additional information
-
carbohydrate content is less than 0.5%
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
-
in complex with hexaglucosamine, hanging drop vapor diffusion method, using 0.05 M KH2PO4 and 23% (w/v) PEG 8000 using 0.7 M NaCl as the reservoir at 15C
hanging drop crystallization with 30 mg/ml protein in 20 mM acetate, pH 5.5 mixed with 0.1 volume of a 0.5 M potassium phosphate, 20% w/v PEG 8000 solution, monoclinic space group P21
-
sitting drop vapor diffusion method, using 10% (w/v) MEPEG 5K, 300 mM tetramethylammonium chloride, and 100 mM Bis-Tris, pH 6.5, at 4C
the substrate binding cleft is composed of six monosaccharide binding subsites
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 9
-
the enzyme is stable and retains more than 80% of its original activity from pH 1.0-9.0 after 15 min
731499
2
1 h, complete inactivation
663697
2
-
loss of 90% of activity after 1 h incubation
680991
3 - 7
-
isoenzyme PSC-II is stable in this range
646783
3 - 7
-
-
646784
3 - 7
-
30C, stable for at least 24 h
678006
3 - 7
-
the enzyme is stable between pH 3.0 and 7.0
731935
3 - 8
-
stable for at least 7 h
680991
3 - 9
-
691643
3.5 - 8
the enzyme retains 100% activity after 1 h in the pH range 3.5-8.0
731521
3.8 - 9.9
-
37C, 30 min, stable
664395
4 - 7
-
-
697133
4 - 8
1 h, stable
663697
4 - 8
-
-
697120
4.5 - 6.5
-
the enzyme is stable over a a pH range of 4.5-6.5
731243
5
-
most stable at this pH
646790
5 - 7
-
the enzyme is relatively stable at pH 5.0-7.0, retaining around 80% of initial activity for 30 min
731582
5 - 8
-
stable at this range
646765
5 - 8
-
isoenzyme PSC-I is stable in this range
646783
5 - 8
purified enzyme
696815
5 - 9
-
stable at 25C for 1 h
646774
5 - 9
-
the enzyme remains stable between pH 5.0 and 9.0
732902
5.5 - 6.5
-
28C, 60 min, stable
665286
5.5 - 9
-
stable at temperatures below 60C
664986
5.5 - 9
-
the enzyme is stable in the pH range of 5.5-9.0 for up to 12 h
731138
6 - 11
-
stable for 60 min at 40C
646769
7
-
drastical decrease in activity at pH 7
646768
9
-
and above, loss of 50% of activity after 1 h incubation
680991
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0
-
stable in this range
646746
0
-
stable
646752
0 - 90
-
the enzyme is stable over a temperature range of 0-50C and shows about 20% of the initial activity after heating at 90C for 10 min
731243
5 - 30
-
in absence of substrate the chitosanase is stable between 5C and 30C
665017
10
-
most stable at 10C, stability of chitosanase I droppes at higher temperatures and most activity is lost above 60C
646766
20
-
stable
646757
20
-
purified enzyme, pH 5.8, 2 h, 98% activity remaining
707019
20 - 70
-
all three isoforms are stable in this range for 30 min
646783
25 - 40
maintains its initial activity, has almost half of its activity at 50C but is completely inactivated at 70C
691643
25 - 40
-
maintains its initial activity from 25 to 40C but is completely inactivated at 80C
697133
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
697120
25 - 50
-
the enzyme is stable between 25 and 50C, maintains its initial activity from 25 to 40C and has 50% of its activity at 50C, and is inactivated at 80C
731935
27 - 50
-
the enzyme is stable between 27 and 50C for up to 3 h
731138
30
-
pH 5.0, 30 min, stable
646748
30
-
rather stable for 20 min
646774
30
-
purified enzyme, pH 5.8, 2 h, 92% activity remaining
707019
30 - 40
-
stable at this range
646765
30 - 60
-
more than 90% of the initial activities are retained after incubation at 30, 40, 50, and 60C for 30 min
731582
30 - 70
-
stable for 2 h
678006
30 - 80
-
after 15 min incubation the enzyme shows 100% activity at 30C, about 90% at 40C, about 85% at 50C, about 82% at 60C, about 80% at 70C, about 60% at 80C, about 40 at 90C, and about 20% activity at 100C
731499
30 - 80
-
isoform A is stable between 30 and 80C, whereas isoform B is stable between 30 and 50C after 60 min incubation
731964
37
-
denaturation in 1-2 h, stabilized by 1.0 mM Ca2+
646740
37
-
pH 6.0-8.0, stable, unstable at elevated temperatures
646742
37
-
stable
646751
40
-
pH 5.0, 30 min, stable
646748
40
-
rapid decrease of activity above
646751
40
-
15 min, stable up to
646754
40
-
rather stable for 20 min
646774
40
-
pH 6, 1 h, stable below
665286
40
-
30 min, 20 mM acetate pH 5.0, stable up to 40C
678783
40
-
purified enzyme, pH 5.8, 2 h, 85% activity remaining
707019
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
697132
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
715885
42.5
melting temperature of the wild type enzyme
731275
43.4
-
transition temperature in absence of chitosan
678466
45
-
pH 6.8, 15 min, stable below
646749
45
-
isoform A, stable up to
646753
45
-
gradual inactivation of the enzyme
646774
45
-
stable for 1 h
646790
45
24 h, enzyme retains full activity
663697
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
714540
50
-
stable below, pH 6.0, 15 min
646741
50
-
stable
646743
50
-
60 min, stable
646752
50
-
half-maximum inactivation after 1 h
646773
50
-
gradual inactivation of the enzyme
646774
50
-
stable below
646784
50
alpine bacterium
-
active below 50C
646785
50
half-life: 5 h
663697
50
-
pH 6, 1 h, stable below
664395
50
-
pH 6, 1 h, about 50% loss of activity
665286
50
-
30 min, 20 mM acetate pH 5.0, 95% loss of activity
678783
50
-
1 h, 25% residual activity for wild-type, 27% residual activity for mutant L74Q/V75I/G151D, 42% residual activity for mutant G151D/N222S
678792
50
Gongronella sp.
-
half-life 65 min
681718
50
-
purified enzyme, pH 5.8, half-live is 30 min
707019
50
-
the recombinant chitosanase is stable at temperatures up to 50C above which the enzyme activity decreases rapidly
709824
50
-
the enzyme remains stable at temperatures up to 50C
732902
50 - 55
Gongronella sp.
half-lives of Csn2 at 50C and 55C are 30 min and 11 min, respectively
697126
54
-
wild-type, transition temperature in absence of chitosan
678466
55
-
significant loss in activity
646774
55
half-life: 10 min
663697
60
-
pH 6.0, 15 min, 40% loss of activity
646741
60
-
30 min, pH 5.0, complete inactivation
646748
60
-
60 min, 40% loss of activity
646752
60
-
stable up to
646763
60
-
loss of 75% activity after 15 min
646773
60
half-life: 5 min
663697
60
-
pH 5.5-9.0, stable below
664986
60
-
purified enzyme, pH 5.8, half-live is 13 min
707019
60 - 80
-
the chitosanase maintains its initial activity at less than 60C, the chitosanase is inactivated completely at 80C
715729
61
-
both wild-type and mutants A104L, K164R are active over 90 min
678466
65
-
pH 6, 10 min, about 90% loss of activity
665286
68.6
-
transition temperature in presence of chitosan at 6 g/l
678466
69.5
-
wild-type, transition temperature in presence of chitosan at 6 g/l
678466
70
-
pH 6.0, 15 min, complete loss of activity
646741
70
-
15 min, 30% loss of activity
646743
70
-
60 min, 70% loss of activity
646752
70
-
stable for 60 min
646771
70
-
loss of 95% activity after 15 min
646773
70
-
in presence of substrate remarkable stability at
665017
70
Ficus sp.
-
30 min, enzyme retains almost all of its activity
665277
70
-
optimum for chitosanase acivity
678783
70
-
half-life 26.6 min
681857
70
-
the recombinant chitosanase shows hardly activity after 30 min
709824
70 - 85
the half-life of the enzyme at 70C in the presence of chitosan substrate is more than 20 h. Maximal activity is observed at 80C for 10 min and at 85C for 5 and 3 min incubation times
731200
75
Ficus sp.
-
30 min, about 35% loss of activity
665277
80
-
60 min, 80% loss of activity
646752
80
-
15 min, 55% loss of activity
646754
80
-
stable for 30 min
646771
80
Ficus sp.
-
5 min, about 70% loss of activity
665277
80
-
15 min, almost complete loss of activity
678006
80
-
half-life 18.4 min
681857
80 - 100
the enzyme has half-lives of 2.5 h at 80C, 1 h at 90C and 32 min at 100C. Almost full enzyme activity remains after 1 h at 80C, 30 min at 90C and 10 min at 100C
731521
81.1
-
consensus mutant, transition temperature in presence of chitosan at 6 g/l
678466
83.3
-
mutant A104L, transition temperature in presence of chitosan at 6 g/l
678466
85.1
-
mutant K164R, transition temperature in presence of chitosan at 6 g/l
678466
90
-
half-life 16.7 min, but enzyme retains activity for up to 8 h in presence of 1 mM MnCl2
681857
100
-
10 min, 50% loss of activity
646752
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme retaines 70% activity after incubation with 10 M urea at room temperature for 30 min
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
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
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
LITERATURE
native enzyme 21.25fold
-
-
alpine bacterium
-
to homogeneity
Amycolatopsis sp.CsO-2
2 forms: A and B
-
CM Sephadex C50 gel filtration and Sephadex G-100 gel filtration
-
ammonium sulfate precipitation and Superdex 75 gel filtration
-
ammonium sulfate precipitation, DEAE-Sepharose CL-6B column chromatography, and Sephacryl S-100 gel filtration
-
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
CM-Toyopearl 650 M column chromatography and Resource S column chromatography
-
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
-
ammonium sulfate precipitation, DEAE Sepharose column chromatography, and Sephacryl S-100 gel filtration
-
SuperQ column chromatography and CM Toyopearl column chromatography
-
ammonium sulfate precipitation and Sephacryl S-100 gel filtration
-
2 isoforms: A1-CF1 and A1-CF2
-
-
Ficus sp.
-
f. sp. phaseoli
-
-
Gongronella sp.
-
by gel filtration
Gongronella sp.
glutathione-Sepharose 4B bead chromatography, and Sephacryl S-100 gel filtration
native enzyme 23fold from mycelium by bacitracin affinity chromatography and gel filtration
-
acetone precipitation, Q-Sepharose column chromatography, Hi-Trap Q column chromatography, and hydroxyapatite chromatography
-
Q-Sepharose column chromatography and hydroxyapatite column chromatography
by gel filtration, to homogeneity, 6.4fold
by two consecutive anion exchange chromatography steps and subsequent reverse-phase column chromatography, to homogeneity, 65fold with a yield of 1.7%
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
-
ammonium sulfate precipitation, HiPrep Q column chromatography, and Superdex 75 gel filtration
-
HisTrap column chromatography, and 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
-
acetone fractionation and column chromatography
-
isolation of a bifunctional chitosanase/cellulase from commercial prepapration of cellulase
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant overexpressed from vector pET15b/CSO2 in Escherichia coli BL21(DE3)
Amycolatopsis sp.CsO-2
gene cho, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109
expressed in Escherichia coli BL21 cells
-
expressed in Pichia pastoris GS115 cells
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)
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
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
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
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.
the enzyme is expressed recombinantly as a periplasmic enzyme in Escherichia coli strain BMS172
-
expressed in Escherichia coli BL21(DE3) cells
expression as a fusion protein in Escherichia coli
expression in Escherichia coli
-
expressed in Saccharomyces cerevisiae strain BY4741/sed1DELTA
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
expressed in Escherichia coli BL21(DE3) cells
expressed in Streptomyces lividans strain TK24 and Escherichia coli Gold cells
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
wild-type and mutants subcloned into vector pFD666 and expressed in Streptomyces lividans TK-24
-
EXPRESSION
ORGANISM
UNIPROT
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
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
COMMENTARY
LITERATURE
E22Q
Amycolatopsis sp.CsO-2
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
E37Q
-
the mutation abolishes the antifungal activity of chitosanase
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
E37Q
Bacillus circulans MH-K1
-
the mutation abolishes the antifungal activity of chitosanase
-
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%)
D235A
the mutant shows about 18% of wild type activity
H203A
the mutant shows about 3% of wild type activity
S27A
the mutant shows about 80% of wild type activity
T58A
the mutant shows about 20% of wild type activity
Y37F
the mutant shows about 5% of wild type activity
D235A
-
the mutant shows about 18% of wild type activity
-
D43A
-
inactive
-
H203A
-
the mutant shows about 3% of wild type activity
-
S27A
-
the mutant shows about 80% of wild type activity
-
T58A
-
the mutant shows about 20% of wild type activity
-
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
E302Y
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
N312A
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
N312D
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
N312K
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
N312R
-
site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
W159A
the mutant shows about 30% of wild type activity
W159A/F406A
the mutant shows about 5% of wild type activity
W228A
the mutant shows about 110% of wild type activity
W228A/Y311A
the mutant shows about 30% of wild type activity
Y311A
the mutant shows about 75% of wild type activity
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
-
E302K
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
-
W159A
Paenibacillus fukuinensis D2
-
the mutant shows about 30% of wild type activity
-
W159A/F406A
Paenibacillus fukuinensis D2
-
the mutant shows about 5% of wild type activity
-
W228A
Paenibacillus fukuinensis D2
-
the mutant shows about 110% of wild type activity
-
Y311A
Paenibacillus fukuinensis D2
-
the mutant shows about 75% of wild type activity
-
D41N
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%
D40G
the mutant shows drastic loss of activity
D40G/R42E
the mutant shows drastic loss of activity
D40G/R42K
the mutant shows drastic loss of activity
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%
R42E
the mutant shows drastic loss of activity
R42K
the mutant shows drastic loss of activity
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
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
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
decreased midpoint temperature by about 7C
W28F/W101F
decreased midpoint temperature by about 11C
D201A
-
time-course is almost identical to that obtained by the wild-type
D40E
lower activity than mutant D40G
D40G
reaction time is 20 min. It is distinguished from wild-type by a lower activity, without changing the mechanism of hydrolysis or the mode of interaction with substrate
D40G
-
reduces activity to 2%
D40G/T45D
reaction time is 100 min. It has 0.1% of wild-type specific activity when tested on chitosan substrate
D40G/T45E
has 0.03% of wild-type specific activity when tested on chitosan substrate
D40N
lower activity than mutant D40G
E36A
reaction time is 10 min
E36A/D40G
reaction time is 100 min. Kcat is ca. 18times lower than that of the single mutant D40G. Rate of (GlcN)6 degradation is enhanced by sodium azide
E36D
reaction time is 10 min
E36N
reaction time is 10 min
E36Q
reaction time is 10 min
E36Q/D40G
reaction time is 100 min. Kcat is more than 5times lower than that of the single mutant D40G
T45E
has a very low residual activity. Activity of this mutant can not be enhanced by sodium azide
T45H
results in a complete loss of activity
T45S
reaction time is 20 min. It is quite active, keeps ca. 71% of the specific activity of the wild-type enzyme
V148T
has 10% of wild-type activity when tested on chitosan substrate
K218P
-
mutant enzyme shows 0.16% of wild-type activity
additional information
chimeric chitosanase produced by inserting two peptide loops, each containing a cysteine residue, in opposite walls of the substrate-binding cleft. The two cysteine residues form a disulfide bond crossing the protruding loop, which may alter the binding topology of the substrate and consequently convert the endo-chitosanase into an exo-type enzyme
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
-
F406A
the mutant shows about 50% of wild type activity
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
F406A
Paenibacillus fukuinensis D2
-
the mutant shows about 50% of wild type activity
-
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
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
COMMENTARY
LITERATURE
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
Acinetobacter calcoaceticus TKU024
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
-
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
Aspergillus sp. QD-2
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
-
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
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
food industry
Bacillus cereus D-11
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
-
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
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
-
food industry
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
food industry
Bacillus subtilis TKU002
-
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials
-