3.2.1.4: cellulase
This is an abbreviated version!
For detailed information about cellulase, go to the full flat file.
Word Map on EC 3.2.1.4
-
3.2.1.4
-
cellulose
-
trichoderma
-
biomass
-
reesei
-
xylanase
-
cellulolytic
-
saccharification
-
lignocellulosic
-
cellobiose
-
straw
-
lignin
-
polysaccharide
-
aspergillus
-
glycoside
-
beta-glucosidase
-
corn
-
biofuels
-
pectinase
-
xylan
-
hemicellulose
-
bagasse
-
penicillium
-
endoglucanases
-
bioethanol
-
xylose
-
amylase
-
polygalacturonase
-
sugarcane
-
carbohydrate-binding
-
feedstock
-
viride
-
glucans
-
thermocellum
-
bran
-
carboxymethylcellulose
-
microcrystalline
-
exoglucanase
-
cellulose-binding
-
laccase
-
biorefinery
-
rumen
-
biotechnology
-
analysis
-
novozyme
-
silage
-
endoxylanase
-
compost
-
industry
-
textile industry
-
food industry
-
biofuel production
-
agriculture
-
deconstruct
-
xylobiose
-
diagnostics
-
harzianum
-
degradation
-
chrysosporium
-
synthesis
-
detergent
-
environmental protection
-
xyloglucans
- 3.2.1.4
- cellulose
- trichoderma
- biomass
- reesei
- xylanase
-
cellulolytic
-
saccharification
-
lignocellulosic
- cellobiose
- straw
- lignin
- polysaccharide
- aspergillus
- glycoside
- beta-glucosidase
- corn
-
biofuels
- pectinase
- xylan
- hemicellulose
- bagasse
- penicillium
- endoglucanases
-
bioethanol
- xylose
- amylase
- polygalacturonase
- sugarcane
-
carbohydrate-binding
-
feedstock
- viride
- glucans
- thermocellum
- bran
- carboxymethylcellulose
-
microcrystalline
- exoglucanase
-
cellulose-binding
- laccase
-
biorefinery
- rumen
- biotechnology
- analysis
-
novozyme
-
silage
- endoxylanase
-
compost
- industry
- textile industry
- food industry
- biofuel production
- agriculture
-
deconstruct
- xylobiose
- diagnostics
- harzianum
- degradation
- chrysosporium
- synthesis
- detergent
- environmental protection
- xyloglucans
Reaction
Synonyms
(1->4)-beta-D-glucan 4-glucanohydrolase, 1,4-beta-D-endoglucanase, 1,4-beta-D-glucan-4-glucanohydrolase, 168cel5, 9.5 cellulase, Abscission cellulase, AEG, Ag-EGase III, AgCMCase, alkali cellulase, Alkaline cellulase, AnCel5A, AtCel5, ATEG_07420, avicelase, BC-EG70a, Bc22Cel, BCE1, BcsZ, beta-1,4-endoglucan hydrolase, beta-1,4-endoglucanase, beta-1,4-glucanase, Bgl7A, bifunctional endoglucanase/xylanase, BlCel9, BP_Cel9A, Bx-ENG-1, Bx-ENG-2, Bx-ENG-3, C4endoII, carbomethyl cellulase, Carboxymethyl cellulase, Carboxymethyl-cellulase, carboxymethylcellulase, Cat 1, Caylase, CBH45-1, cbh6A, CBHI, CBHII, CcCel6C, CEL1, Cel1 EGase, Cel12A, Cel1753, Cel28a, Cel44A, Cel45A, Cel48A, Cel5, Cel5A, cel5B, Cel5E, Cel6A, Cel6A (E2), Cel6B, Cel6C, CEL7, Cel7A, Cel7B, Cel8, Cel8A, Cel8M, Cel8Y, Cel9A, CEL9A-50, CEL9A-65, Cel9A-68, CEL9A-82, Cel9A-90, Cel9B, CEL9C1, Cel9K, Cel9M, Cel9Q, CelA, CelB, CelC2 cellulase, CelCM3, CelDR, CelE, CelF, Celf_1230, Celf_3184, CelG, CelG endoglucanase, CelI15, cell-bound bacterial cellulase, CelL15, CelL73, cellic Ctec2, cellobiohydrolase, cellobiohydrolase I, celluase A, Celluclast, celludextrinase, Cellulase, cellulase 12A, cellulase A, cellulase A 3, cellulase Cel48F, cellulase Cel9A, cellulase Cel9M, cellulase CelC2, cellulase CelE, cellulase CM3, Cellulase E1, Cellulase E2, Cellulase E4, Cellulase E5, cellulase EGX, cellulase II, cellulase III, cellulase K, Cellulase SS, cellulase T, Cellulase V1, cellulase Xf818, cellulases I, cellulases III, cellulosin AP, Cellulysin, CelP, celS, CelStrep, celVA, CelX, CenA, CenC, CfCel6A, CfCel6C, CfEG3a, CHU_1280, CHU_2103, CjCel9A, Clocel_2741, CMCase, CMCase-I, CMCax, CMcellulase, Csac_1076, Csac_1078, CSCMCase, ctCel9D-Cel44A, CTendo45, ctendo7, CtGH5, Cthe_0435, CTHT_0045780, CX-cellulase, CyPB, DCC85_10145, DK-85, Dockerin type 1, Dtur_0671, E1 endoglucanase, Econase, EfPh, EG I, EG III, EG1, EG12, EG2, EG25, EG271, EG28, EG3, EG35, EG44, EG47, EG51, Eg5a, EG60, EGA, EGase, EGase II, EGB, EGC, EGCCA, EGCCC, EGCCD, EGCCF, EGCCG, EGD, EGE, EGF, egGH45, EGH, EGI, EGII, EGII/Cel5A, EGIV, EGL, EGL 1, Egl-257, Egl1, Egl499, Egl5a, EglA, eglB, EglC, EGLII, EglS, EGM, EGPf, EGPh, EGSS, EgV, EGX, EGY, EGZ, endo-1,4-B-glucanase, endo-1,4-beta-D-glucanase, endo-1,4-beta-glucanase, endo-1,4-beta-glucanase 1, endo-1,4-beta-glucanase 2, endo-1,4-beta-glucanase E1, endo-1,4-beta-glucanase V1, endo-beta-1,3-1,4-glucanase, endo-beta-1,4-glucanase, endo-beta-1,4-glucanase 1, endo-beta-1,4-glucanase 2, endo-beta-1,4-glucanase CMCax, endo-beta-1,4-glucanase EG27, endo-beta-1,4-glucanase EG45, endo-beta-D-1,4-glucanohydrolase, endo-beta-glucanase, endo-glucanase, ENDO1, ENDO2, endocellulase, endocellulase E1, endocellulases I, endocellulases II, endocellulases III, endocellulases IV, endogenous beta-1,4-endoglucanase, endogenous cellulase, endoglucanase, endoglucanase 1, endoglucanase 35, endoglucanase 47, endoglucanase CBP105, endoglucanase Cel 12A, endoglucanase Cel 5A, endoglucanase Cel 7B, endoglucanase Cel5A, endoglucanase Cel6A, endoglucanase D, endoglucanase EG-I, endoglucanase EG25, endoglucanase EG28, endoglucanase EG44, endoglucanase EG47, endoglucanase EG51, endoglucanase EG60, endoglucanase H, endoglucanase II, endoglucanase IIa, endoglucanase IV, endoglucanase L, endoglucanase M, endoglucanase V, endoglucanase Y, endolytic cellulase, EngA, EngH, EngL, EngM, engXCA, EngY, EngZ, family 7 cellobiohydrolase, FI-CMCASE, FnCel5A, FpCel45, Fpcel45a, GE40, GE40 endoglucanase, GH12 endo-1,4-beta-glucanase, GH124 endoglucanase, GH45 endoglucanase, gh45-1, GH5 cellulase, GH5 endoglucanase, GH6 endoglucanase, GH7 endoglucanase, GH9 termite cellulase, Glu1, Glu2, glycoside hydrolase family 9 endoglucanase, GtGH45, Lp-egl-1, manganese dependent endoglucanase, Maxazyme, Meicelase, mesophilic endoglucanase, mgCel6A, More, MtGH45, nmGH45, Onozuka R10, pancellase SS, PaPopCel1, PF0854, PH1171, PttCel9A, RCE1, RCE2, Roth 3056, RtGH124, Rucel5B, Sl-cel7, Sl-cel9C1, SnEG54, SoCel5, ssgluc, SSO1354, SSO1354 enzyme, SSO1354 protein, SSO1949, SSO2534, STCE1, Sumizyme, T12-GE40, TC Serva, TeEG-I, TeEgl5A, TfCel9A, ThEG, theme C glycoside hydrolase family 9 endo-beta-glucanase, Thermoactive cellulase, thermostable carboxymethyl cellulase, THITE_2110957, TM_1525, TM_1751, umcel5G, umcel9y-1, Vul_Cel5A
ECTree
3.2.1.4 cellulaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.2.1.4 - cellulase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-di-O-methylated cellulase + H2O
?
-
2,3-di-O-methylated cellulase, having a trace amount of unsubstituted glucose units is hydrolyzed. Only the linkages between glucose units and 2,3-di-O-methylated units are cleaved. No hydrolysis of 2,3-di-O-methylcellulose, having every structural unit of them regioselectively substituted
-
-
?
2,4-dinitrophenyl beta-cellotrioside + H2O
2,4-dinitrophenyl beta-cellobioside + D-glucose
cleavage occurs between the second and third sugar residues with no release of chromophore, thus no colour change
-
-
?
4''',6'''-O-benzylidene 2-chloro-4-nitrophenyl-beta-cellotrioside + H2O
4'',6''-O-benzylidene beta-cellobioside + 2-chloro-4-nitrophenyl beta-D-glucoside
4-methylumbelliferyl cellobioside + H2O
4-methylumbelliferone + cellobiose
-
-
-
?
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside + H2O
4,6-O-(3-oxobutylidene)-beta-D-cellotriose + 4-nitrophenyl-beta-D-cellobioside
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
0.16% of the activity with carboxymethyl cellulose
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
?
7.7% of the activity with carboxymethyl cellulose
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
33.2% of the activtiy with carboxymethyl cellulose
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
33.2% of the activity with carboxymethyl cellulose
-
-
?
4-nitrophenyl cellopentaoside + H2O
4-nitrophenol + cellopentaose
-
-
-
?
4-nitrophenyl cellotetraoside + H2O
4-nitrophenol + cellotetraose
-
-
-
?
4-nitrophenyl cellotrioside + H2O
4-nitrophenol + cellotriose
-
-
-
?
4-nitrophenyl D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl D-cellobioside + H2O
4-nitrophenol + D-cellobiose
-
-
-
?
6-chloro-4-methylumbelliferyl beta-cellobioside + H2O
6-chloro-4-methylumbelliferone + cellobiose
-
-
-
?
acid swollen cellulose + H2O
cellobiose + cellotriose
endoglucanase with exohydrolytic activity
-
-
?
alpha-cellulose + H2O
?
-
activity of the catalytic module EG1-CM is 58% of the activity with endoglucanase 1
-
-
?
alpha-chitin + H2O
?
-
due to the binding, it seems chitin would be an inhibitor of Cel6B, Cel9A and Cel48A, but not of Cel6A and Cel5A
-
-
?
avicel + H2O
cellobiose + glucose
-
the main product is cellobiose together with a small amount of glucose, endoglucanase 35
-
-
?
bacterial microcrystalline cellulose + H2O
cellotetraose
-
weak activity
83% cellotetraose + 11% cellotriose + 4% cellobiose
-
?
barley beta-1,4-D-glucan + H2O
?
Thermochaetoides thermophila
best endoglucanase substrate
-
-
?
barley beta-glucan + H2O
cellobiose + cellotriose + D-glucose
best substrate, high activity, product analysis
-
-
?
beta-1,4-D-xylan + H2O
?
Thermochaetoides thermophila
bifunctional endoglucanase/xylanase enzyme
-
-
?
carboxymethyl cellulose + H2O
cellobiose + cellooligosaccharides
-
-
-
-
?
carboxymethyl cellulose + H2O
cellobiose + cellotriose
-
substrate concentration 1%, low activity
-
-
?
carboxymethyl cellulose + H2O
cellotriose + cellobiose + D-glucose
-
enzyme hydrolyzes internal beta-1,4 glycosidic bonds within lichenan as well as carboxymethyl cellulose to release oligosaccharides and glucose
major products
-
?
carboxymethylcellulose + H2O
cellobiose + cello-oligomer
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellooligomers
endo-beta-1,4-glucanase activity. The enzyme shows cellulase and xylanase activity
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellotriose + cellotetraose
-
-
-
?
cello-oligosaccharide + H2O
?
-
insoluble cello-oligosaccharide average degree of polymerization 34 and soluble cello-oligosaccharides longer than cellotriose
-
-
?
cellobioside + H2O
?
-
about 2% of the activity with barley beta-glucan
-
-
?
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose + cellulose + cellopentaose
-
cellobiose is the main product
-
-
?
cellooligosaccharides + H2O
?
random cleavage, slow reaction rates for cellooligosaccharides smaller than G5
-
-
?
cellopentaose + H2O
cellobiose + cellotriose + cellotetraose + cellulose
-
cellobiose is the main product
-
-
?
cellotrioside + H2O
?
-
7.4% of the activity with barley beta-glucan
-
-
?
cellulose + H2O
cellobiose + cellotriose + cellotetraose + cellopentaose
Thermochaetoides thermophila
-
-
-
-
?
curdlan + H2O
?
activity is 26% compared to activity with carboxymethyl-cellulose
-
-
?
debranched arabinan
?
activity is 25% compared to activity with carboxymethyl-cellulose
-
-
?
filter paper + H2O
cellotriose + cellobiose + D-glucose
-
poor substrate
major products
-
?
konjac glucomannan + H2O
cellobiose + cellotriose
-
substrate concentration 1%
-
-
?
lichenan + H2O
cellotriose + cellobiose + D-glucose
-
enzyme hydrolyzes internal beta-1,4 glycosidic bonds within lichenan as well as carboxymethyl cellulose to release oligosaccharides and glucose
major products
-
?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
-
the enzyme liberates disaccharides from the reducing end
-
-
?
N,N',N''-triacetyl-chitotriose + H2O
N,N'-diacetyl-chitobiose + N-acetyl-D-glucosamine
-
the enzyme liberates disaccharides from the reducing end
-
-
?
N-acetyllactosamine + butanol
butyl beta-N-acetyllactosaminide + H2O
-
-
-
-
?
N-acetyllactosamine + ethanol
ethyl beta-N-acetyllactosaminide + H2O
-
-
-
-
?
N-acetyllactosamine + glycerol
glyceryl beta-N-acetyllactosaminide
-
-
-
-
?
N-acetyllactosamine + propanol
propyl beta-N-acetyllactosaminide + H2O
-
-
-
-
?
N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate + H2O
?
N-[2-N-[(S-(4-deoxy-4-dimethylaminophenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate + H2O
?
-
-
-
?
N-[2-N-[(S-(4-deoxy-4-dimethylaminophenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate + H2O
? + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
-
-
?
pachyman + H2O
?
activity is 22% compared to activity with carboxymethyl-cellulose
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + cellotriose
-
substrate concentration 1%, best substrate and high activity
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
sea lettuce + H2O
cellotriose + cellobiose + D-glucose
-
-
major products
-
?
soluble cellulose + H2O
?
-
endo mode of action. At the beginning only high molecular mass products are released suggesting an endowise action of the enzyme. The major product has a degree of polymerization of three, minor quantities of smaller and larger oligosaccharides are also produced. Not active against insoluble cellulose
-
-
?
sulfite-pulped spruce + H2O
cellobiose + cellotriose
-
substrate concentration 1%
-
-
?
xylan + H2O
D-xylose + ?
at 90°C, pH 4 by an enzyme mix consisting of SSO1354 and additional glycosyl hydrolases
-
-
?
yeast glucan + H2O
?
-
best substrate of isoform cellulase I, no substrate of isoforms cellulase II and III
-
-
?
2,4-dinitrophenyl beta-cellobioside + H2O
?
-
-
-
?
2,4-dinitrophenyl beta-cellobioside + H2O
?
-
-
-
?
2,4-dinitrophenyl beta-cellobioside + H2O
?
-
-
-
?
2,4-dinitrophenyl beta-cellobioside + H2O
?
-
-
-
?
4''',6'''-O-benzylidene 2-chloro-4-nitrophenyl-beta-cellotrioside + H2O
4'',6''-O-benzylidene beta-cellobioside + 2-chloro-4-nitrophenyl beta-D-glucoside
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture
-
-
?
4''',6'''-O-benzylidene 2-chloro-4-nitrophenyl-beta-cellotrioside + H2O
4'',6''-O-benzylidene beta-cellobioside + 2-chloro-4-nitrophenyl beta-D-glucoside
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture
-
-
?
4''',6'''-O-benzylidene 2-chloro-4-nitrophenyl-beta-cellotrioside + H2O
4'',6''-O-benzylidene beta-cellobioside + 2-chloro-4-nitrophenyl beta-D-glucoside
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture
-
-
?
4''',6'''-O-benzylidene 2-chloro-4-nitrophenyl-beta-cellotrioside + H2O
4'',6''-O-benzylidene beta-cellobioside + 2-chloro-4-nitrophenyl beta-D-glucoside
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture
-
-
?
4-methylumbelliferyl beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
-
-
-
?
4-methylumbelliferyl beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
-
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
very low activity
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
-
-
-
?
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside + H2O
4,6-O-(3-oxobutylidene)-beta-D-cellotriose + 4-nitrophenyl-beta-D-cellobioside
-
-
-
?
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside + H2O
4,6-O-(3-oxobutylidene)-beta-D-cellotriose + 4-nitrophenyl-beta-D-cellobioside
-
-
-
?
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside + H2O
4,6-O-(3-oxobutylidene)-beta-D-cellotriose + 4-nitrophenyl-beta-D-cellobioside
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
14% of the activity with carboxymethyl cellulose
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
14% of the activity with carboxymethyl cellulose
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
low activity
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
acid-swollen cellulose + H2O
?
-
-
-
?
acid-swollen cellulose + H2O
?
cleaved cellulose randomly
-
-
?
acid-swollen cellulose + H2O
?
activity of truncated enzyme form
-
-
?
acid-swollen cellulose + H2O
?
activity of truncated enzyme form
-
-
?
arabinan + H2O
?
hydrolysed at 53% compared to the hydrolysis of carboxymethylcellulose
-
-
?
avicel + H2O
?
-
8.1% of the activity with carboxymethyl cellulose
-
?
avicel + H2O
?
Actinomyces sp. 40 Korean Native Goat 40
-
8.1% of the activity with carboxymethyl cellulose
-
?
avicel + H2O
?
-
14% of the activity with carboxymethylcellulose
-
-
?
avicel + H2O
?
-
14% of the activity with carboxymethylcellulose
-
-
?
avicel + H2O
?
-
microcrystalline cellulose, shows poor growth and enzyme production, relative activity 5.2%
-
-
?
avicel + H2O
?
Bacillus sp. (in: Bacteria) CTP-09
-
microcrystalline cellulose, shows poor growth and enzyme production, relative activity 5.2%
-
-
?
avicel + H2O
?
21.8% of the activity with carboxymethyl cellulose
-
-
?
avicel + H2O
?
21.8% of the activtiy with carboxymethyl cellulose
-
-
?
avicel + H2O
?
14% of the activity with carboxymethyl-cellulose
-
-
?
avicel + H2O
?
17.7% of the activity with carboxymethyl-cellulose
-
-
?
avicel + H2O
?
-
33% of the activity with carboxymethyl cellulose
-
-
?
avicel + H2O
?
-
33% of the activity with carboxymethyl cellulose
-
-
?
avicel + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
avicel + H2O
?
-
good substrate of isoforms cellulase II and III
-
-
?
avicel + H2O
?
-
microcrystalline cellulose (Avicel) is subjected to 3 different pretreatments (acid, alkaline, and organic solvent) before exposure to amixture of cellulases
-
-
?
avicel + H2O
?
-
activity of the catalytic module EG1-CM is43% of the activity with endoglucanase 1
-
-
?
avicel + H2O
?
55% of the activity with carboxymethyl cellulose
-
-
?
avicel + H2O
cellobiose + ?
the main product is cellobiose
-
-
?
avicel + H2O
cellobiose + ?
the main product is cellobiose
-
-
?
avicel + H2O
cellobiose + cellotriose
-
substrate concentration 1%, low activity
-
-
?
avicel + H2O
cellobiose + cellotriose
cellooligosaccharides production from Avicel is detected only when 0.00185 mkat of Xf818his are employed, and not when 16.67 nkat are used. Endoglucanase with exohydrolytic activity
-
-
?
bacterial microcrystalline cellulose + H2O
?
weak activity
-
-
?
barley beta-glucan + H2O
?
92% of the activity on carboxymethyl cellulose
-
-
?
barley beta-glucan + H2O
?
as AZCL beta-glucan
-
-
?
barley beta-glucan + H2O
?
as AZCL beta-glucan
-
-
?
barley beta-glucan + H2O
?
as AZCL beta-glucan
-
-
?
barley beta-glucan + H2O
?
as AZCL beta-glucan
-
-
?
barley beta-glucan + H2O
?
as AZCL beta-glucan
-
-
?
barley beta-glucan + H2O
?
as AZCL beta-glucan
-
-
?
barley beta-glucan + H2O
?
MG570051
311% of the activity with carboxymethylcellulose
-
-
?
barley beta-glucan + H2O
?
the highest specific activity toward polysaccharides occurs with mixed-linkage (1->3),(1->4)-beta-D-glucans such as barley beta-glucan and lichenan
-
-
?
barley beta-glucan + H2O
?
136% of the activity with carboxymethyl cellulose
-
-
?
barley beta-glucan + H2O
D-glucose + ?
high activity
-
-
?
barley beta-glucan + H2O
D-glucose + ?
high activity
-
-
?
barley glucan + H2O
?
120% of the activity with carboxymethyl-cellulose
-
-
?
barley glucan + H2O
?
143% of the activity with carboxymethyl-cellulose
-
-
?
barley glucan + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
barley glucan + H2O
?
the enzyme hydrolyzes mixed linked beta-(1-3)(1-4) substrates such as barley glucan and lichenan more strongly than carboxymethylcellulose
-
-
?
beechwood xylan + H2O
?
hydrolysed at 84% compared to the hydrolysis of carboxymethylcellulose
-
-
?
beechwood xylan + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
beechwood xylan + H2O
?
10% of the activity with carboxymethyl cellulose
-
-
?
beta-1,4-D-glucan + H2O
?
Thermochaetoides thermophila
bifunctional endoglucanase/xylanase enzyme
-
-
?
beta-glucan + H2O
?
-
24.6% of the activity with carboxymethylcellulose
-
-
?
beta-glucan + H2O
?
-
24.6% of the activity with carboxymethylcellulose
-
-
?
beta-glucan + H2O
?
degree of hydrolysis reaches 10%, products are oligosaccharides with degree of polymerization 2-10
-
-
?
beta-glucan + H2O
?
-
400% of the activity with carboxymethyl cellulose
-
-
?
birchwood xylan + H2O
?
-
2% of the activity with carboxymethyl cellulose
-
-
?
birchwood xylan + H2O
?
hydrolysed at 73% compared to the hydrolysis of carboxymethylcellulose
-
-
?
birchwood xylan + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
birchwood xylan + H2O
?
-
88% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
birchwood xylan + H2O
?
-
88% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
birchwood xylan + H2O
?
44% of the activity with carboxymethylcellulose
-
-
?
carboxymethyl cellulose + H2O
?
-
production of a mixture of cellobiose, cellotriose, cellotetraose and cellopentaose
-
?
carboxymethyl cellulose + H2O
?
-
endo-beta-1,4-glucanase EG27 shows high preference for
-
-
?
carboxymethyl cellulose + H2O
?
-
endo-beta-1,4-glucanase EG45 shows high preference for
-
-
?
carboxymethyl cellulose + H2O
?
18.6% of the activity with barley beta-glucan
-
-
?
carboxymethyl cellulose + H2O
?
18.6% of the activity with barley beta-glucan
-
-
?
carboxymethyl cellulose + H2O
?
-
products are mainly cello-oligosaccharides along with small amounts of glucose and cellobiose
-
?
carboxymethyl cellulose + H2O
?
processive endoglucanase activity
-
-
?
carboxymethyl cellulose + H2O
?
processive endoglucanase activity
-
-
?
carboxymethyl cellulose + H2O
?
-
Cel9A is a nonprocessive enzyme with endo-cellulase activities
-
-
?
carboxymethyl cellulose + H2O
?
13.6% of the activity with barley beta-glucan
-
-
?
carboxymethyl cellulose + H2O
?
13.6% of the activity with barley beta-glucan
-
-
?
carboxymethyl cellulose + H2O
?
-
-
no glucose, cellobiose and short chain celloolifgosaccharides are formed
-
?
carboxymethyl cellulose + H2O
?
-
-
no glucose, cellobiose and short chain celloolifgosaccharides are formed
-
?
carboxymethyl cellulose + H2O
?
-
68% of the activity with barley beta-glucan
-
-
?
carboxymethyl cellulose + H2O
?
activity of truncated enzyme form
-
-
?
carboxymethyl cellulose + H2O
?
activity of truncated enzyme form
-
-
?
carboxymethyl cellulose + H2O
?
release of reducing sugar, degradation
-
-
?
carboxymethyl cellulose + H2O
?
release of reducing sugar, degradation
-
-
?
carboxymethyl cellulose + H2O
?
AZO-carboxymethyl cellulose
-
-
?
carboxymethyl cellulose + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
carboxymethyl cellulose + H2O
?
-
22% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
carboxymethyl cellulose + H2O
?
-
best substrate of isoform cellulase III, no substrate of cellulase II
-
-
?
carboxymethyl cellulose + H2O
?
-
22% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila
bifunctional endoglucanase/xylanase enzyme
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila CT2
-
best substrate tested
-
-
?
carboxymethyl cellulose + H2O
?
endoglucanase with exohydrolytic activity
-
-
?
carboxymethyl cellulose + H2O
cellobiose + cellotriose + ?
-
products are 18% cellotriose, 72% cellobiose and 10% glucose
-
?
carboxymethyl cellulose + H2O
cellobiose + cellotriose + ?
-
-
-
?
carboxymethyl cellulose + H2O
cellobiose + cellotriose + ?
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
high activity
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
high activity
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
high activity
-
-
?
carboxymethyl cellulose + H2O
D-glucose + cellobiose + cellooligosaccharide
-
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + cellobiose + cellooligosaccharide
-
-
-
-
?
carboxymethyl cellulose + H2O
glucose + cellobiose + short oligomers
-
-
-
-
?
carboxymethyl cellulose + H2O
glucose + cellobiose + short oligomers
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
the smallest product is a disaccharide
-
-
?
carboxymethylcellulose + H2O
?
activity with carbomethylcellulose with approxomately 4 carboxymethyl groups per 10 anhydro-glucose units is about 3.5 times better than that with carbomethylcellulose with approximately 8 carboxymethyl groups
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
high specific activity towards carboxymethylcellulose
-
-
?
carboxymethylcellulose + H2O
?
the enzyme hydrolyzes mixed linked beta-(1-3)(1-4) substrates such as barley glucan and lichenan more strongly than carboxymethylcellulose
-
-
?
carboxymethylcellulose + H2O
carboxymethyl glucose + cellobiose + cellotriose
-
-
-
-
?
carboxymethylcellulose + H2O
carboxymethyl glucose + cellobiose + cellotriose
-
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellotriose + cellotetraose + cellopentaose
-
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellotriose + cellotetraose + cellopentaose
-
-
-
-
?
carboxymethylcellulose + H2O
short glucose oligomers + cellobiose + glucose
-
-
-
-
?
carboxymethylcellulose + H2O
short glucose oligomers + cellobiose + glucose
-
-
-
-
?
cellobiose + H2O
2 D-glucose
-
26% of the activity with carboxymethyl cellulose
-
?
cellobiose + H2O
2 D-glucose
Actinomyces sp. 40 Korean Native Goat 40
-
26% of the activity with carboxymethyl cellulose
-
?
cellobiose + H2O
?
-
9.8% of the activity with carboxymethyl cellulose
-
?
cellobiose + H2O
?
-
9.8% of the activity with carboxymethyl cellulose
-
?
cellobiose + H2O
?
-
8.6% of the activity with carboxymethylcellulose
-
-
?
cellobiose + H2O
?
-
25% of the activity with carboxymethyl cellulose
-
-
?
cellohexaose + H2O
2 cellotriose
-
-
+ small amounts of cellobiose and cellotriose
-
?
cellohexaose + H2O
2 cellotriose
Niallia circulans KSM-N257
-
-
+ small amounts of cellobiose and cellotriose
-
?
cellohexaose + H2O
?
Thermochaetoides thermophila
-
the enzyme hydrolyzes cellotetraose, cellopentaose, and cellohexaose at comparable rates
-
-
?
cellohexaose + H2O
cellobiose + cellotriose
-
-
-
?
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose
Bellamya chinensis laeta UM-2014
-
-
-
?
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose
-
-
-
-
?
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose
-
-
-
-
?
cellohexaose + H2O
cellotriose + cellotetraose + cellobiose
major product is cellotriose, minor products are cellobiose and cellotetraose
-
-
?
cellohexaose + H2O
cellotriose + cellotetraose + cellobiose
major product is cellotriose, minor products are cellobiose and cellotetraose
-
-
?
cellopentaose + H2O
?
Thermochaetoides thermophila
-
the enzyme hydrolyzes cellotetraose, cellopentaose, and cellohexaose at comparable rates
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellotetraose
cellopentaose + cellohexaose
-
transfer reaction
-
?
cellotetraose + H2O
2 cellobiose
-
-
glucose, 15%, cellobiose, 64%, cellotriose, 14% and cellotetraose, 3.3%
?
cellotetraose + H2O
2 cellobiose
Bacillus sp. (in: Bacteria) No. 1139
-
-
glucose, 15%, cellobiose, 64%, cellotriose, 14% and cellotetraose, 3.3%
?
cellotetraose + H2O
2 cellobiose
-
-
+ glucose + cellotriose
?
cellotetraose + H2O
2 cellobiose
minimal substrate length, cellotriose and cellobiose are not hydrolyzed
-
-
?
cellotetraose + H2O
2 cellobiose
minimal substrate length, cellotriose and cellobiose are not hydrolyzed
-
-
?
cellotetraose + H2O
2 cellobiose
-
effectively hydrolyzed by endoglucanase E1, limited hydrolysis by endoglucanase E2
-
-
?
cellotetraose + H2O
?
Thermochaetoides thermophila
-
the enzyme hydrolyzes cellotetraose, cellopentaose, and cellohexaose at comparable rates
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
-
a mixture of glucose, 5.5%, cellobiose, 55%, cellotriose, 34%, and traces of cellotetraose
?
cellotriose + H2O
D-glucose + cellobiose
Bacillus sp. (in: Bacteria) No. 1139
-
-
a mixture of glucose, 5.5%, cellobiose, 55%, cellotriose, 34%, and traces of cellotetraose
?
cellotriose + H2O
D-glucose + cellobiose
-
hydrolyzed by endo-beta-1,4-glucanase component YEG2, no hydrolysis with endo-beta-1,4-glucanase component YEG1
+ glucose
?
cellotriose + H2O
D-glucose + cellobiose
-
-
predominant product
?
cellotriose + H2O
D-glucose + cellobiose
-
effectively hydrolyzed by endoglucanase E1, limited hydrolysis by endoglucanase E2
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
hydrolyzed by endoglucanase E1, no activity with endoglucanase E2
+ glucose, endoglucanase E1
?
cellulose + H2O
?
-
endoglucanase I shows very low activity with acid-swollen cellulose
-
-
?
cellulose + H2O
?
-
Walseth cellulose shows 1.1% of the activity with carboxymethylcellulose
-
-
?
cellulose + H2O
?
-
little ability to hydrolyze ordered cellulose
-
-
?
cellulose + H2O
?
-
pretreatment of cellulose with ionic liquids such as 1-butyl-3-methylimidazolium chloride, 1-methylimidazolium chloride, and tris-(2-hydroxyethyl)-methylammonium methylsulfate results in more rapid conversion to glucose than hydrolysis with cellulose that is not pretreated
-
-
?
cellulose + H2O
?
-
amorphous cellulose (relative activity 15.2%), filter paper (shows poor growth and enzyme production, relative activity 3.1%), cotton wool (relative activity 4.3%)
-
-
?
cellulose + H2O
?
Bacillus sp. (in: Bacteria) CTP-09
-
amorphous cellulose (relative activity 15.2%), filter paper (shows poor growth and enzyme production, relative activity 3.1%), cotton wool (relative activity 4.3%)
-
-
?
cellulose + H2O
?
-
acid-swollen
major end product are cellobiose and cellotriose, endoglucanase Z
?
cellulose + H2O
?
-
swollen cellulose
a mixture of cellooligosaccharides
?
cellulose + H2O
?
-
swollen cellulose
a mixture of cellooligosaccharides
?
cellulose + H2O
?
-
maximal activity soluble cellulosic substrate (CMC-Na salt), indicating that the crude enzyme has endoglucanase activity
-
-
?
cellulose + H2O
?
-
maximal activity soluble cellulosic substrate (CMC-Na salt), indicating that the crude enzyme has endoglucanase activity
-
-
?
cellulose + H2O
?
-
Walseth cellulose
products from Walseth cellulose: glucose + cellobiose + cellotriose + cellotetraose
?
cellulose + H2O
?
crystalline and amorphous cellulose
-
-
?
cellulose + H2O
?
-
amorphous cellulose and ball-milled cellulose
-
-
?
cellulose + H2O
?
activity is evaluated on 13 insoluble celluloses characterized for crystallinity and crystal width (by X-ray diffraction), wet porosity (by thermoporometry), and particle size (by light scattering). Looser crystalline packing increases the lengths of released cello-oligomers as well as the maximum endoglucanase specific activity (kcat)
-
-
?
cellulose + H2O
?
-
-
crystalline cellulose is hydrolyzed to glucose and cellobiose
?
cellulose + H2O
?
-
filter paper, 18% activity compared to carboxymethyl cellulose
-
-
?
cellulose + H2O
?
-
acid-swollen
large amounts of cellotriose and a small amount of cellotetraose
?
cellulose + H2O
?
-
Walseth cellulose
mainly glucose, cellobiose and traces of cellotriose
?
cellulose + H2O
?
-
hydrolysis of Solka floc, Avicel, CMC, waste paper, and waste wood refiner
-
-
?
cellulose + H2O
?
-
amorphous cellulose
endoglucanase E1 produces mainly cellobiose and a trace of glucose, endoglucanase E2 produces mainly cellotriose and higher oligomers with some cellobiose and a trace of glucose
?
cellulose + H2O
?
-
the catalytic domains of Cel6A, Cel6B, Cel48A, Cel5A, and Cel9A only show very weak binding to bacterial cellulose
-
-
?
cellulose + H2O
?
-
the family 1 carbohydrate-binding module, CBM, mediates the interaction between enzyme and crystalline cellulose surface via residues Y5, Q7, N29, and Y32, thus CBM is responsible for anchoring the enzyme at discrete points along a cellulose chain to aid in both recognizing cellulose chain ends for initial attachment to cellulose as well as aid in enzymatic catalysis by diffusing between stable wells on a length scale commensurate with the catalytic, processive cycle of Cel7A during cellulose hydrolysis, molecular-level mechanisms of recognition and interaction, overview
-
-
?
cellulose + H2O
cellobiose + ?
the substrate position is fixed by the alignment of one cellobiose unit between the two aromatic amino acid residues at subsites +1 and +2. During the enzyme reaction, the glucose structure of cellulose substrates is distorted at subsite -1, and the beta-1,4-glucoside bond between glucose moieties is twisted between subsites -1 and +1. Subsite -2 specifically recognizes the glucose residue, but recognition by subsites +1 and +2 is loose during the enzyme reaction. Analysis of the enzyme-substrate structure suggests that an incoming water molecule, essential for hydrolysis during the retention process, might be introduced to the cleavage position after the cellobiose product at subsites +1 and +2 is released from the active site
-
-
?
cellulose + H2O
cellobiose + ?
the substrate position is fixed by the alignment of one cellobiose unit between the two aromatic amino acid residues at subsites +1 and +2. During the enzyme reaction, the glucose structure of cellulose substrates is distorted at subsite -1, and the beta-1,4-glucoside bond between glucose moieties is twisted between subsites -1 and +1. Subsite -2 specifically recognizes the glucose residue, but recognition by subsites +1 and +2 is loose during the enzyme reaction. Analysis of the enzyme-substrate structure suggests that an incoming water molecule, essential for hydrolysis during the retention process, might be introduced to the cleavage position after the cellobiose product at subsites +1 and +2 is released from the active site
-
-
?
cellulose + H2O
cellobiose + ?
the secreted protein enables Sulfolobus solfataricus to use cellulose as an external carbon source
-
-
?
cellulose + H2O
cellobiose + ?
the secreted protein enables Sulfolobus solfataricus to use cellulose as an external carbon source
-
-
?
cellulose + H2O
cellooligosaccharide
-
the enzyme plays an important role in maintaining the carbon balance in nature
-
-
?
cellulose + H2O
cellooligosaccharide
-
in bean the 9.5 cellulase appears to function in the shedding of various organs such as fruits, flowers, and leaves. The acid cellulases function in loosening the cellulose fibrils of the cell wall to allow expansion and growth
-
-
?
cellulose + H2O
cellooligosaccharide
Sporotrichum pulverulentum
-
enzyme is involved in degradation of cellulose
-
-
?
cellulose + H2O
cellooligosaccharide
-
induced by carboxymethylcellulose, non-constitutive synthesis
-
-
?
cellulose + H2O
cellooligosaccharide
-
enzyme plays an important role in the carbon cycle
-
-
?
cellulose + H2O
cellooligosaccharide
-
enzyme plays an important role in the carbon cycle
-
-
?
cellulose + H2O
D-glucose + ?
-
enzyme is able to degrade crystalline cellulose to glucose
-
?
cellulose + H2O
D-glucose + ?
enzyme FnCel5A catalyzes the hydrolysis of cellulose to glucose
-
-
?
cellulose + H2O
D-glucose + ?
enzyme FnCel5A catalyzes the hydrolysis of cellulose to glucose
-
-
?
cellulose + H2O
D-glucose + ?
enzyme FnCel5A catalyzes the hydrolysis of cellulose to glucose
-
-
?
cellulose + H2O
D-glucose + ?
at 90°C, pH 4 by an enzyme mix consisting of SSO1354 and additional glycosyl hydrolases
-
-
?
filter paper + H2O
?
-
18% of the activity with carboxymethyl cellulose
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
-
8.4% of the activity with carboxymethyl cellulose
-
-
?
filter paper + H2O
?
-
8.4% of the activity with carboxymethyl cellulose
-
-
?
filter paper + H2O
?
7.6% of the activity with carboxymethyl cellulose
-
-
?
filter paper + H2O
?
7.6% of the activtiy with carboxymethyl cellulose
-
-
?
filter paper + H2O
?
4% of the activity with carboxymethyl-cellulose. CBH6A and EgGH45, synergic effect, showing the highest efficiency in the ratio at 80:20
-
-
?
filter paper + H2O
?
8% of the activity with carboxymethyl-cellulose. CBH6A and EgGH45, synergic effect, showing the highest efficiency in the ratio at 80:20
-
-
?
filter paper + H2O
?
-
best substrate of isoforms cellulase II and III
-
-
?
insoluble cellulose + H2O
?
-
e.g. Avicel, Solka-floc, Sigmacell 50
no glucose, cellobiose and short chain celloolifgosaccharides are formed
-
?
insoluble cellulose + H2O
?
-
e.g. Avicel, Solka-floc, Sigmacell 50
no glucose, cellobiose and short chain celloolifgosaccharides are formed
-
?
laminarin + H2O
?
9.1% of the activity with barley beta-glucan
-
-
?
laminarin + H2O
?
9.1% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
-
6% of the activity with carboxymethylcellulose
-
-
?
lichenan + H2O
?
94% of the activity on carboxymethyl cellulose
-
-
?
lichenan + H2O
?
53.2% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
53.2% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
-
30% of the activity with barley beta-glucan, catalytic domain of endoglucanase G
-
-
?
lichenan + H2O
?
-
30% of the activity with barley beta-glucan, catalytic domain of endoglucanase G
-
-
?
lichenan + H2O
?
60.5% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
60.5% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
MG570051
157% of the activity with carboxymethylcellulose
-
-
?
lichenan + H2O
?
the highest specific activity toward polysaccharides occurs with mixed-linkage (1->3),(1->4)-beta-D-glucans such as barley beta-D-glucan and lichenan
-
-
?
lichenan + H2O
?
activity is 120% compared to activity with carboxymethyl-cellulose
-
-
?
lichenan + H2O
?
130% of the activity with carboxymethyl cellulose
-
-
?
lichenan + H2O
?
130% of the activity with carboxymethyl cellulose
-
-
?
lichenan + H2O
?
-
380% of the activity with carboxymethyl cellulose
-
-
?
lichenan + H2O
?
-
380% of the activity with carboxymethyl cellulose
-
-
?
lichenan + H2O
?
the enzyme hydrolyzes mixed linked beta-(1-3)(1-4) substrates such as barley glucan and lichenan more strongly than carboxymethylcellulose
-
-
?
N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate + H2O
?
-
-
-
?
N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate + H2O
?
-
-
-
?
N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
activity is 25% compared to activity with carboxymethyl-cellulose
-
-
?
oat spelt xylan + H2O
?
hydrolysed at 76% compared to the hydrolysis of carboxymethylcellulose
-
-
?
oat spelt xylan + H2O
?
-
92% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
oat spelt xylan + H2O
?
-
92% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
oat spelt xylan + H2O
?
59% of the activity with carboxymethylcellulose
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
glucose + cellobiose + ?
Bacillus cellulyticus K-12
-
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
glucose + cellobiose + ?
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
glucose + cellobiose + ?
-
cellulase III preferentially attacks the aglycone linkage
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
glucose + cellobiose + ?
-
cellulase II-A preferentially attacks the holoside linkage of p-nitrophenyl beta-D-cellobioside, cellulase II-B attacks mainly the aglycone linkage. Synthesis of cellotriose from p-nitrophenyl beta-D-cellobioside by transfer of a glucosyl residue, possibly to cellobiose produced in the reaction mixture
-
-
?
p-nitrophenyl cellobiose + H2O
p-nitrophenol + cellobiose
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
endoglucanase EG25
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
endoglucanase EG28
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
endoglucanase EG44
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
endoglucanase EG47
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
endoglucanase EG51
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
endoglucanase EG60
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
fluorimetric determination in cellulase activity assay using calcofluor white
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid-swollen cellulose + H2O
?
Thermochaetoides thermophila CT2
-
low activity
-
-
?
phosphoric acid-treated wheat straw + H2O
?
-
74% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
phosphoric acid-treated wheat straw + H2O
?
-
74% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
soluble cellodextrin + H2O
?
-
-
no glucose, cellobiose and short chain cellooligosaccharides are formed
-
?
soluble cellodextrin + H2O
?
-
-
no glucose, cellobiose and short chain cellooligosaccharides are formed
-
?
xylan + H2O
?
-
6.1% of the activity with carboxymethyl cellulose
-
?
xylan + H2O
?
Actinomyces sp. 40 Korean Native Goat 40
-
6.1% of the activity with carboxymethyl cellulose
-
?
xylan + H2O
?
beechwood xylan, 34% , and birchwood xylan, 31% of the activity on carboxymethyl cellulose, respectively
-
-
?
xylan + H2O
?
-
20% of the activity with carboxymethyl cellulose
-
?
xylan + H2O
?
-
20% of the activity with carboxymethyl cellulose
-
?
xylan + H2O
?
-
22.5% of the activity with carboxymethylcellulose
-
-
?
xylan + H2O
?
-
22.5% of the activity with carboxymethylcellulose
-
-
?
xylan + H2O
?
-
20.3% of the activity with carboxymethyl cellulose
-
-
?
xylan + H2O
?
3.3% of the activity with carboxymethyl cellulose
-
-
?
xyloglucan + H2O
?
-
71% of the activity with carboxymethyl cellulose
-
?
xyloglucan + H2O
?
-
71% of the activity with carboxymethyl cellulose
-
?
xyloglucan + H2O
?
a beta-1,4-1,6-glucan, 40% activity compared to barley beta-glucan
-
-
?
6-O-methylcellulose + H2O
additional information
-
-
6-O-methylcellulose having every structural unit of them regioselectively substituted
glycosidic bond between two adjacent substituted units can be cleaved to give oligomers with a degree of polymerization of ca. 8
?
carboxymethyl cellulose + H2O
additional information
-
-
-
short glucose oligomers, cellobiose and a very small amount of glucose
-
?
carboxymethyl cellulose + H2O
additional information
-
-
-
short glucose oligomers, cellobiose and a very small amount of glucose
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
endoglucanase 1b: cellotriose, 45%, cellotetraose, 31%, cellobiose, 17%, and cellopentaose, 8%. Endoglucanase 2: cellotriose, 50%, and cellotetraose, 30%
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
Bacillus sp. (in: Bacteria) No. 1139
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
Bacillus sp. (in: Bacteria) No. 1139
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
glucose + cellobiose
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
catalytic domain of endoglucanase G
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
catalytic domain of endoglucanase G
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
glucose + cellobiose + cellotriose + cellotetraose
?
carboxymethylcellulose + H2O
additional information
-
-
-
various cellooligosaccharides
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
mainly glucose with small amounts of cellobiose and cellotriose
?
carboxymethylcellulose + H2O
additional information
-
-
-
mainly glucose with small amounts of cellobiose and cellotriose
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
hydrolyzed by cellulase I and III, no hydrolysis with cellulase II
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
endoglucanase E1 exhibits higher activity
endoglucanase E2 produces glucose, cellobiose, cellotriose and higher oligosaccharides. The major end product produced by endoglucanase E1 is cellobiose and small amounts of glucose
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
cellohexaose + H2O
additional information
-
-
-
cellotriose + glucose + cellobiose + cellotetraose
?
cellohexaose + H2O
additional information
-
-
-
cellotriose + cellobiose + cellotriose
?
cellohexaose + H2O
additional information
-
Bacillus cellulyticus K-12
-
-
cellobiose + cellotetraose
?
cellohexaose + H2O
additional information
-
-
-
cellobiose + cellotetraose
?
cellohexaose + H2O
additional information
-
-
-
cellotriose + cellobiose + cellotetraose
?
cellohexaose + H2O
additional information
-
-
-
cellotriose is formed and then slowly degraded
?
cellohexaose + H2O
additional information
-
-
cellulase A, B, and C
-
-
?
cellohexaose + H2O
additional information
-
-
-
cellotriose + cellobiose + cellotetraose
?
cellopentaose + H2O
additional information
-
-
enzyme form EGB and EGC
-
-
?
cellopentaose + H2O
additional information
-
-
-
cellobiose + cellotriose + glucose
?
cellopentaose + H2O
additional information
-
-
-
cellotetraose + glucose
?
cellopentaose + H2O
additional information
-
-
-
cellobiose + cellotriose
?
cellopentaose + H2O
additional information
-
-
-
cellobiose + cellotriose
?
cellopentaose + H2O
additional information
-
-
cellulase A, B, and C
-
-
?
cellopentaose + H2O
additional information
-
-
hydrolyzed by endo-beta-1,4-glucanase component YEG1 and YEG2
cellobiose + cellotriose
?
cellopentaose + H2O
additional information
-
-
-
cellobiose + cellotriose
?
cellopentaose + H2O
additional information
-
-
-
cellobiose + cellotriose
?
cellopentaose + H2O
additional information
-
-
beta-configuration of the anomeric carbon atoms is retained
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl-beta-D-glucoside
-
-
?
additional information
?
-
-
modular enzyme that contains a family 30 carbohydrate-binding modules, CBM, and a family 9 catalytic module at its N-terminal moiety. The CBM is extremely important not only because it mediates the binding of the enzyme to the substrate but also because it participates in the catalytic function of the enzyme or contributes to maintain the correct tertiary structure of the family 9 catalytic module for expressing enzyme activity
-
-
?
additional information
?
-
-
substrates are acid swollen cellulose, lichenan, beta-glucan, carboxymethyl cellulose, galactomannans, oat spelt xylan, avicel, and steam exploded bagasse, no activity glucomannan and laminarin
-
-
?
additional information
?
-
-
final hydrolysed product produced from carboxymethyl cellulose by chimera 1 is glucose confirming both beta-1,4-endoglucanase and beta-1,4-glucosidase activities, while the products of CtGH5-F194A point mutant are cellobiose and cello-oligosaccharides. Product indentification by thin layer chromatography. Enzymatic hydrolysis of 1% w/v Sorghum stalk pretreated by 1% NaOH by mutant CtGH5-F194A with or without wild-type enzyme CtGH1, which exhibits beta-glucosidase activity. No activity of the wild-type enzyme and mutant F194A with 4-nitrophenyl beta-D-glucoside, which is a substrate of the beta-glucosidase activity of chimeric mutant CtGH1-CtGH5-F194A
-
-
?
additional information
?
-
-
modular enzyme that contains a family 30 carbohydrate-binding modules, CBM, and a family 9 catalytic module at its N-terminal moiety. The CBM is extremely important not only because it mediates the binding of the enzyme to the substrate but also because it participates in the catalytic function of the enzyme or contributes to maintain the correct tertiary structure of the family 9 catalytic module for expressing enzyme activity
-
-
?
additional information
?
-
no substrae: cellobiose
-
-
?
additional information
?
-
-
the enzyme is able to hydrolyse sugarcane bagasse, rice husk, and wheat bran, with the highest production of reducers/fermentable sugars within 24 h of saccharification for wheat bran (137.21 mg/g). Saccharification of agroindustrial residues, overview
-
-
?
additional information
?
-
Amphobotrys ricini URM 5627
-
the enzyme is able to hydrolyse sugarcane bagasse, rice husk, and wheat bran, with the highest production of reducers/fermentable sugars within 24 h of saccharification for wheat bran (137.21 mg/g). Saccharification of agroindustrial residues, overview
-
-
?
additional information
?
-
-
endo-beta-1,4-glucanase EG27 shows no activity with p-nitrophenyl-beta-D-cellobiose, salicin and starch
-
-
?
additional information
?
-
-
endo-beta-1,4-glucanase EG45 shows no activity with p-nitrophenyl-beta-D-cellobiose, salicin and starch
-
-
?
additional information
?
-
enzyme displays weak activity on weak on locust bean galactomannan, avicel, and filter paper
-
-
?
additional information
?
-
-
enzyme displays weak activity on weak on locust bean galactomannan, avicel, and filter paper
-
-
?
additional information
?
-
enzyme displays weak activity on weak on locust bean galactomannan, avicel, and filter paper
-
-
?
additional information
?
-
hydrolysis of rice and corn straws
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl-beta-D-glucoside
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl-beta-D-glucoside
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
-
enzyme displays both beta-glucosidase, EC 3.2.1.21, and cellulase activities
-
-
?
additional information
?
-
-
enzyme displays both beta-glucosidase, EC 3.2.1.21, and cellulase activities
-
-
?
additional information
?
-
-
trans-glucosidase activity also observed
-
-
?
additional information
?
-
-
investigation of substrate specificity
-
-
?
additional information
?
-
-
starch as a substrate shows a relative activity of 0% and xlycan shows a relative activity of 0.9%
-
-
?
additional information
?
-
-
the organism possesses carboxymethyl cellulase and cellulase activities, overview
-
-
?
additional information
?
-
enzyme hydrolyzes soluble cellulose substrates containing beta-1,4-linkages, such as carboxylmethyl cellulose and konjac glucomannan, but has no exoglucanase and beta-glucosidase activities
-
-
?
additional information
?
-
-
enzyme hydrolyzes soluble cellulose substrates containing beta-1,4-linkages, such as carboxylmethyl cellulose and konjac glucomannan, but has no exoglucanase and beta-glucosidase activities
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) BG-CS10
enzyme hydrolyzes soluble cellulose substrates containing beta-1,4-linkages, such as carboxylmethyl cellulose and konjac glucomannan, but has no exoglucanase and beta-glucosidase activities
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) CTP-09
-
investigation of substrate specificity
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) CTP-09
-
starch as a substrate shows a relative activity of 0% and xlycan shows a relative activity of 0.9%
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) DUSELR13
-
the organism possesses carboxymethyl cellulase and cellulase activities, overview
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) No. 1139
-
trans-glucosidase activity also observed
-
-
?
additional information
?
-
-
wild-type and mutant can not hydrolyze Avicel, laminarin and chitosan
-
-
?
additional information
?
-
-
the enzyme shows multisubstrate specificity, showing significantly higher activity with lichenan and beta-glucan and lower activity with laminarin, hydroxyethylcellulose, and steam exploded bagasse
-
-
?
additional information
?
-
-
no substrates: 4-nitrophenyl beta-D-glucopyranoside, cellulose
-
-
?
additional information
?
-
-
no substrates: alpha-glucan, cellobiose and xylan
-
-
?
additional information
?
-
-
the enzyme shows multisubstrate specificity, showing significantly higher activity with lichenan and beta-glucan and lower activity with laminarin, hydroxyethylcellulose, and steam exploded bagasse
-
-
?
additional information
?
-
-
wild-type and mutant can not hydrolyze Avicel, laminarin and chitosan
-
-
?
additional information
?
-
-
no substrates: alpha-glucan, cellobiose and xylan
-
-
?
additional information
?
-
-
no substrates: 4-nitrophenyl beta-D-glucopyranoside, cellulose
-
-
?
additional information
?
-
Bellamya chinensis laeta
no substrate: cellotriose, insoluble cellulose, avicel, birchwood xylan, oat grass xylan, laminarin, soluble chitin
-
-
?
additional information
?
-
Bellamya chinensis laeta UM-2014
no substrate: cellotriose, insoluble cellulose, avicel, birchwood xylan, oat grass xylan, laminarin, soluble chitin
-
-
?
additional information
?
-
Bgl7A can effectively hydrolyze beta-1,4 bonds and some beta-1,3 linkages in beta-glucan. Belonging to the group of non-specific endoglucanase, Bgl7A can hydrolyze not only beta-glucan and cellulose but also laminarin and oat spelt xylan
-
-
?
additional information
?
-
poor activity with laminarin and oat spelt xylan, no activity with Avicel
-
-
?
additional information
?
-
no activity with tamarind xyloglucan, barley (1-3)(1-4)-beta-D-glucan, wheat arabinoxylan or birchwood xylan
-
-
?
additional information
?
-
-
inverting glycoside hydrolases catalyze bond cleavage using a single-displacement mechanism involving the participation of two acidic amino acid residues positioned opposite each other across the active site cleft or tunnel
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-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
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-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
no activity on Avicel or xylan
-
-
?
additional information
?
-
no activity on Avicel or xylan
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-
?
additional information
?
-
-
glucanase hydrolyses beta-1,4-glycosidic bonds
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-
?
additional information
?
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glucanase hydrolyses beta-1,4-glycosidic bonds
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?
additional information
?
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-
CcCel6C exhibits high cellobiohydrolase activity
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?
additional information
?
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hydrolyzing internal beta-1,4-glycosidic bonds and resulting in a smear of polymers with different lengths. The hydrolytic products of tCfEG are one unit sugar less than those produced by nCfEG
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?
additional information
?
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-
hydrolyzing internal beta-1,4-glycosidic bonds and resulting in a smear of polymers with different lengths. The hydrolytic products of tCfEG are one unit sugar less than those produced by nCfEG
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-
?
additional information
?
-
carboxymethyl cellulose sodium salt is a better substrate than insoluble cellulose substrate such as Avicel (0 U/mg), SIGMACELL cellulose (0 U/mg), and CM cellulose
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-
?
additional information
?
-
no substrates: cellobiose and cellotriose
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-
?
additional information
?
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-
no substrates: cellobiose and cellotriose
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-
?
additional information
?
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EBI-244 is active on a range of high molecular weight carbohydrate substrates containing beta-1,4-linked glucose, including carboxymethyl cellulose, Avicel, and filter paper, it is active toward 4-nitrophenyl-cellobioside but inactive toward 4-nitrophenyl-glucoside
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-
?
additional information
?
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enzyme shows high endo-beta-1,4-mannanase activity versus various mannans, but low endo-beta-1,4 glucanase activity towards carboxymethylcellulose, andd negligible activity towards glucomannans
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-
?
additional information
?
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enzyme shows high endo-beta-1,4-mannanase activity versus various mannans, but low endo-beta-1,4 glucanase activity towards carboxymethylcellulose, andd negligible activity towards glucomannans
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-
?
additional information
?
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-
when the oligosaccharides are modified by reduction with sodium borotritide, the second linkage from the reducing end becomes significantly susceptible to the enzyme and is preferentially cleaved
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-
?
additional information
?
-
the enzyme shows high affinity for carboxymethyl cellulose, but is also active with other substrates like beta-1,4-linked polysaccharides, including xyloglucan, glucomannan, beta-glucan, lichenin, and galactomannan
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?
additional information
?
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-
the enzyme shows high affinity for carboxymethyl cellulose, but is also active with other substrates like beta-1,4-linked polysaccharides, including xyloglucan, glucomannan, beta-glucan, lichenin, and galactomannan
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-
?
additional information
?
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the enzyme shows high affinity for carboxymethyl cellulose, but is also active with other substrates like beta-1,4-linked polysaccharides, including xyloglucan, glucomannan, beta-glucan, lichenin, and galactomannan
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?
additional information
?
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the enzyme shows high affinity for carboxymethyl cellulose, but is also active with other substrates like beta-1,4-linked polysaccharides, including xyloglucan, glucomannan, beta-glucan, lichenin, and galactomannan
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-
?
additional information
?
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the enzyme has a unique catalytic efficiency on beta-1,4-glucans rather than mixed beta-1,3/1,4-glucans as compared to other GH45 endoglucanases. No activity on Avicel and 4-nitrophenyl beta-D-cellobioside
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-
?
additional information
?
-
the enzyme has a unique catalytic efficiency on beta-1,4-glucans rather than mixed beta-1,3/1,4-glucans as compared to other GH45 endoglucanases. No activity on Avicel and 4-nitrophenyl beta-D-cellobioside
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-
?
additional information
?
-
-
glucanase hydrolyses mainly beta-1,4-glycosidic bonds but is also capable of significant hydrolysis of beta-1,3-glycosidic bonds
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-
?
additional information
?
-
-
glucanase hydrolyses mainly beta-1,4-glycosidic bonds but is also capable of significant hydrolysis of beta-1,3-glycosidic bonds
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?
additional information
?
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-
the organism possesses carboxymethyl cellulase and cellulase activities, overview
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?
additional information
?
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-
the organism possesses carboxymethyl cellulase and cellulase activities, overview
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?
additional information
?
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-
substrate specificity, overview. The GtGH45 is able to convert all tested oligosaccharides to glucose, however, small amounts of cellobiose, cellotriose, and cellotetraose are detected in the reaction products, indicating that the enzyme cannot convert efficiently small oligosaccharides probably due their mode of recognition in the enzyme catalytic cleft. The degradation of C5 and C6 by GtGH45 is almost complete with glucose being a main product
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?
additional information
?
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enzyme is strictly specific for the beta-1,4-glucoside linkage exhibiting activity toward barley beta-glucan, lichenan, and carboxymethyl cellulose sodium salt, but not toward laminarin (1,3-beta-glucan), birchwood xylan, avicel, and not toward 4-nitrophenyl beta-D-glucoside or 4-nitrophenyl cellobioside. Cel6C cleaves the internal glycosidic linkages of cellooligosaccharides randomly, the predominant product of polysaccharide hydrolysis is cellobiose
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-
?
additional information
?
-
enzyme is strictly specific for the beta-1,4-glucoside linkage exhibiting activity toward barley beta-glucan, lichenan, and carboxymethyl cellulose sodium salt, but not toward laminarin (1,3-beta-glucan), birchwood xylan, avicel, and not toward 4-nitrophenyl beta-D-glucoside or 4-nitrophenyl cellobioside. Cel6C cleaves the internal glycosidic linkages of cellooligosaccharides randomly, the predominant product of polysaccharide hydrolysis is cellobiose
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-
?
additional information
?
-
the enzyme also shows chitosanase activity. Colloidal chitosan, chitosan and glycol chitosan are hydrolyzed by Cel8A at 15-40% the activity of cellulose
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-
?
additional information
?
-
the enzyme also shows chitosanase activity. Colloidal chitosan, chitosan and glycol chitosan are hydrolyzed by Cel8A at 15-40% the activity of cellulose
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-
?
additional information
?
-
Cel7B has greater activity than the endoglucanases Cel45A and Cel7A against crystalline cellulose, whereas in the case of amorphous substrate the order is reversed
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-
?
additional information
?
-
Cel7B has greater activity than the endoglucanases Cel45A and Cel7A against crystalline cellulose, whereas in the case of amorphous substrate the order is reversed
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-
?
additional information
?
-
Cel7B has greater activity than the endoglucanases Cel45A and Cel7A against crystalline cellulose, whereas in the case of amorphous substrate the order is reversed
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-
?
additional information
?
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-
Cel7B has greater activity than the endoglucanases Cel45A and Cel7A against crystalline cellulose, whereas in the case of amorphous substrate the order is reversed
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-
?
additional information
?
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-
no substrate: 4-methylumbelliferyl-beta-D-lactoside
-
-
?
additional information
?
-
no substrate: 4-methylumbelliferyl-beta-D-lactoside
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-
?
additional information
?
-
-
no substrate: 4-methylumbelliferyl-beta-D-lactoside
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-
?
additional information
?
-
no substrate: 4-methylumbelliferyl-beta-D-lactoside
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-
?
additional information
?
-
-
no degradation of oat spelt xylan and larch wood xylan
-
-
?
additional information
?
-
-
no degradation of oat spelt xylan and larch wood xylan
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-
?
additional information
?
-
-
no substrates: starch, xylan, cellobiose, filter paper
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-
?
additional information
?
-
enzyme is most active against lichenan and beta-glucans and lesser active toward filter paper, carboxymethyl cellulose, and phosphoric acid-swollen cellulose
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-
?
additional information
?
-
enzyme is most active against lichenan and beta-glucans and lesser active toward filter paper, carboxymethyl cellulose, and phosphoric acid-swollen cellulose
-
-
?
additional information
?
-
-
no hydrolysis of cellobioside, cellotrioside, cellotetraoside, laminarin, curdlan, xylan, p-nitrophenyl beta-D-cellotrioside and p-nitrophenyl beta-D-cellotetraoside
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-
?
additional information
?
-
Niallia circulans KSM-N257
-
no hydrolysis of cellobioside, cellotrioside, cellotetraoside, laminarin, curdlan, xylan, p-nitrophenyl beta-D-cellotrioside and p-nitrophenyl beta-D-cellotetraoside
-
-
?
additional information
?
-
-
no activity with laminarin, avicel, pullulan and pachyman
-
-
?
additional information
?
-
MG570051
low hydrolytic activities, toward birchwood xylan and laminarin
-
-
?
additional information
?
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-
effect of carbon source on enzyme activity
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-
?
additional information
?
-
-
effect of carbon source on enzyme activity
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-
?
additional information
?
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-
distribution of cellulase between the residual substrate and supernatant during the course of enzymatic hydrolysis of steam-exploded wheat straw
-
-
?
additional information
?
-
-
distribution of cellulase between the residual substrate and supernatant during the course of enzymatic hydrolysis of steam-exploded wheat straw
-
-
?
additional information
?
-
-
cellulase preparations that perform best on hardwood also show superior performance on the softwood substrates
-
-
?
additional information
?
-
-
amino acids E209 and E319 act as proton donor and nucleophile in substrate catalytic domain
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-
?
additional information
?
-
amino acids E209 and E319 act as proton donor and nucleophile in substrate catalytic domain
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-
?
additional information
?
-
-
very poor or no substrates: laminarin, xyloglucan, birchwood xylan, arabinan, arabinoxylan, 4-nitrophenyl-beta-D-glucoside. Amino acids E209 and E319 act as proton donor and nucleophile in the catalytic domain
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-
?
additional information
?
-
very poor or no substrates: laminarin, xyloglucan, birchwood xylan, arabinan, arabinoxylan, 4-nitrophenyl-beta-D-glucoside. Amino acids E209 and E319 act as proton donor and nucleophile in the catalytic domain
-
-
?
additional information
?
-
-
very poor substrates: laminarin, xyloglucan. No substrates: birchwood xylan, arabinan, arabinoxylan, 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
very poor substrates: laminarin, xyloglucan. No substrates: birchwood xylan, arabinan, arabinoxylan, 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
very poor substrates: laminarin, xyloglucan, no substrates: birchwood xylan, arabinan, arabinoxylan, mannan, 4-nitrophenyl beta-D-glucopyranoside
-
-
?
additional information
?
-
-
very poor substrates: laminarin, xyloglucan, no substrates: birchwood xylan, arabinan, arabinoxylan, mannan, 4-nitrophenyl beta-D-glucopyranoside
-
-
?
additional information
?
-
no substrates: avicel, arabinoxylan and xyloglucan
-
-
?
additional information
?
-
no activity against birchwood xylan, 4-nitrophenyl cellobiose, 4-nitrophenyl beta-D-glucoside
-
-
?
additional information
?
-
no activity against birchwood xylan, 4-nitrophenyl cellobiose, 4-nitrophenyl beta-D-glucoside
-
-
?
additional information
?
-
-
no activity with crystalline cellulose or cellobiose
-
-
?
additional information
?
-
-
beta-1,4-endoglucanases show activities of the cleavage of the cellulose backbone due to an endocleavage. Oligosaccharides of different lengths as well as cellobiose and glucose are formed
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-
?
additional information
?
-
EglA hydrolyzes shorter cellodextrins (DP <5) as well as the amorphous portions of polysaccharides which contain only beta-1,4 bonds such as carboxymethyl cellulose, microcrystalline cellulose, Whatman paper, and cotton linter. Kinetics studies with cellooliogsaccharides and p-nitrophenyl-cellooligosaccharides indicated that the enzyme had three glucose binding subsites (-I, -II, and -III) for the nonreducing end and two glucose binding subsites (+I and +II) for the reducing end from the scissile glycosidic linkage. No activity is detected on solely beta-1,3-linked oligosaccharides or polysaccharides
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-
?
additional information
?
-
with substrate cellulose, the substrate position is fixed by the alignment of one cellobiose unit between the two aromatic amino acid residues at subsites +1 and +2. During the enzyme reaction, the glucose structure of cellulose substrates is distorted at subsite -1, and the beta-1,4-glucoside bond between glucose moieties is twisted between subsites -1 and +1. Subsite -2 specifically recognizes the glucose residue, but recognition by subsites +1 and +2 is loose during the enzyme reaction. This type of recognition is important for creation of the distorted boat form of the substrate at subsite -1
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-
?
additional information
?
-
-
with substrate cellulose, the substrate position is fixed by the alignment of one cellobiose unit between the two aromatic amino acid residues at subsites +1 and +2. During the enzyme reaction, the glucose structure of cellulose substrates is distorted at subsite -1, and the beta-1,4-glucoside bond between glucose moieties is twisted between subsites -1 and +1. Subsite -2 specifically recognizes the glucose residue, but recognition by subsites +1 and +2 is loose during the enzyme reaction. This type of recognition is important for creation of the distorted boat form of the substrate at subsite -1
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-
?
additional information
?
-
-
hydrolysis of phosphoric-acid swollen filter paper
-
-
?
additional information
?
-
enzyme displays broad substrate specificity and exhibits high activity on substrates containing beta-1,4-glycosidic bonds and beta-1,3-glycosidic bonds such as barley beta-glucan, laminarin, lichenan, carboxymethyl cellulose, carob bean gum, and birchwood xylan
-
-
?
additional information
?
-
no substrates: avicel, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-cellobioside
-
-
?
additional information
?
-
-
hydrolysis of phosphoric-acid swollen filter paper
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
enzyme does not release reducing sugars from Avicel microcrystalline cellulose, cellobiose, polygalacturonate, locust bean gum, xylan, Rhizobium leguminosarum bv. trifolii acidic heteropolysaccharide EPS types I, II, or III, or Sinorhizobium meliloti succinoglycan exopolysaccharide. Enzyme has a high substrate specificity for noncrystalline cellulose
-
-
?
additional information
?
-
-
enzyme does not release reducing sugars from Avicel microcrystalline cellulose, cellobiose, polygalacturonate, locust bean gum, xylan, Rhizobium leguminosarum bv. trifolii acidic heteropolysaccharide EPS types I, II, or III, or Sinorhizobium meliloti succinoglycan exopolysaccharide. Enzyme has a high substrate specificity for noncrystalline cellulose
-
-
?
additional information
?
-
enzyme does not release reducing sugars from Avicel microcrystalline cellulose, cellobiose, polygalacturonate, locust bean gum, xylan, Rhizobium leguminosarum bv. trifolii acidic heteropolysaccharide EPS types I, II, or III, or Sinorhizobium meliloti succinoglycan exopolysaccharide. Enzyme has a high substrate specificity for noncrystalline cellulose
-
-
?
additional information
?
-
-
no activity with avicell, xylan, galactan, arabinan, mannan or laminarin
-
-
?
additional information
?
-
-
no activity with Avicel, cotton, laminarin, and cellobiose
-
-
?
additional information
?
-
-
no hydrolysis of laminarin
-
-
?
additional information
?
-
-
no activity with cellobiose
-
-
?
additional information
?
-
no activity with p-nitrophenyl cellobiose
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl cellobiose
-
-
?
additional information
?
-
-
no cleavage of cellotetraose, cellotriose and p-nitrophenyl-cellobiose
-
-
?
additional information
?
-
the crude enzyme releases reducing sugars from acid-pretreated straw at 75-85°C
-
-
?
additional information
?
-
the crude enzyme releases reducing sugars from acid-pretreated straw at 75-85°C
-
-
?
additional information
?
-
the crude enzyme releases reducing sugars from acid-pretreated straw at 75-85°C
-
-
?
additional information
?
-
no hydrolysis of p-nitrophenyl-beta-D-cellobioside and p-nitrophenyl-beta-D-cellotrioside, no exocellulase activity
-
-
?
additional information
?
-
-
no hydrolysis of p-nitrophenyl-beta-D-cellobioside and p-nitrophenyl-beta-D-cellotrioside, no exocellulase activity
-
-
?
additional information
?
-
the enzyme does not hydrolyse 4-nitrophenyl beta-D-cellobioside and 4-nitrophenyl beta-D-cellotrioside. No activity could be detected with crystalline cellulose at both acidic and neutral pH values
-
-
?
additional information
?
-
the enzyme does not hydrolyse 4-nitrophenyl beta-D-cellobioside and 4-nitrophenyl beta-D-cellotrioside. No activity could be detected with crystalline cellulose at both acidic and neutral pH values
-
-
?
additional information
?
-
-
the enzyme does not hydrolyse 4-nitrophenyl beta-D-cellobioside and 4-nitrophenyl beta-D-cellotrioside. No activity could be detected with crystalline cellulose at both acidic and neutral pH values
-
-
?
additional information
?
-
the enzyme has a beta-1,4 hydrolytic mode of action. It shows no significant activity on PCM3/pachyman, microcrystalline cellulose, or on oat xylan. Concentrated solutions (8090% v/v) of ionic liquids such as 1-ethyl-3-methylimidazolium acetate and 1,3-dimethylimidazolium dimethylphosphate are able to dissolve crystalline cellulose like AvicelW and cell wall polysaccharides, making them more accessible to hydrolytic enzymes
-
-
?
additional information
?
-
-
the enzyme has a beta-1,4 hydrolytic mode of action. It shows no significant activity on PCM3/pachyman, microcrystalline cellulose, or on oat xylan. Concentrated solutions (8090% v/v) of ionic liquids such as 1-ethyl-3-methylimidazolium acetate and 1,3-dimethylimidazolium dimethylphosphate are able to dissolve crystalline cellulose like AvicelW and cell wall polysaccharides, making them more accessible to hydrolytic enzymes
-
-
?
additional information
?
-
no substrates: PCM3/pachyman, avicel, oat xylan
-
-
?
additional information
?
-
-
no substrates: PCM3/pachyman, avicel, oat xylan
-
-
?
additional information
?
-
no substrates: cellotriose, cellobiose, p-nitrophenyl beta-D-cellobioside and p-nitrophenyl beta-D-cellotrioside, xylan, laminarin and lichenan, crystalline cellulose
-
-
?
additional information
?
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no substrates: cellotriose, cellobiose, p-nitrophenyl beta-D-cellobioside and p-nitrophenyl beta-D-cellotrioside, xylan, laminarin and lichenan, crystalline cellulose
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additional information
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no substrates: cellotriose, cellobiose, p-nitrophenyl beta-D-cellobioside and p-nitrophenyl beta-D-cellotrioside, xylan, laminarin and lichenan, crystalline cellulose
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additional information
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the enzyme does not hydrolyse 4-nitrophenyl beta-D-cellobioside and 4-nitrophenyl beta-D-cellotrioside. No activity could be detected with crystalline cellulose at both acidic and neutral pH values
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additional information
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the enzyme does not hydrolyse 4-nitrophenyl beta-D-cellobioside and 4-nitrophenyl beta-D-cellotrioside. No activity could be detected with crystalline cellulose at both acidic and neutral pH values
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additional information
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the enzyme does not hydrolyse 4-nitrophenyl beta-D-cellobioside and 4-nitrophenyl beta-D-cellotrioside. No activity could be detected with crystalline cellulose at both acidic and neutral pH values
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additional information
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the enzyme has a beta-1,4 hydrolytic mode of action. It shows no significant activity on PCM3/pachyman, microcrystalline cellulose, or on oat xylan. Concentrated solutions (8090% v/v) of ionic liquids such as 1-ethyl-3-methylimidazolium acetate and 1,3-dimethylimidazolium dimethylphosphate are able to dissolve crystalline cellulose like AvicelW and cell wall polysaccharides, making them more accessible to hydrolytic enzymes
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additional information
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no substrates: PCM3/pachyman, avicel, oat xylan
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additional information
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carboxymethyl cellulose and beta-glucan are the best substrates with relative activities of 100% and 83%, respectively, birch wood xylan and oat spelt xylan have moderate activities of 68% and 60%, respectively, which otherwise supports low level of cellulase activity, Avicel has the lowest activity of 12%, substrate specificity, overview
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additional information
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the enzyme does not degrade curdran, xylan, laminarin and pectin (0.5% each) at all
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additional information
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the enzyme does not degrade curdran, xylan, laminarin and pectin (0.5% each) at all
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additional information
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possible role of the enzyme in the softening of pericarp tissue and in the liquefaction of locules that takes place during ripening. Cel1 EGase responds to pathogen infection and supports a relationship between EGases, plant defense responses and fruit ripening. mRNA abundance is down-regulated in response to fungal infection. It is rapidly reduced 1 day after pathagen infection and completely suppressed 4 days after infection
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additional information
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enzyme is essential for growth and development of potato cyst nematodes
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additional information
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possible role of the enzyme in the softening of pericarp tissue and in the liquefaction of locules that takes place during ripening. Cel1 EGase responds to pathogen infection and supports a relationship between EGases, plant defense responses and fruit ripening. mRNA abundance is down-regulated in response to fungal infection. It is rapidly reduced 1 day after pathagen infection and completely suppressed 4 days after infection
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additional information
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bioconversion of the pretreated Arundo donax lignocellulosic biomass by wild-type and mutant enzymes
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additional information
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beta-1,3-linkages, alpha-1,6-linkages and beta-1,6-linkages are also susceptible to hydrolysis
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additional information
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no substrates: laminarin, curdlan
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additional information
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no substrates: laminarin, curdlan
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additional information
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no substrates: beta-1,4-mannan, beta-1,4-glycol, chitosan or chitin
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additional information
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Cel9A presents both exo- and endo-cellulase activities, reaction mode, existence of an active conformer prior to ligand binding, overview
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additional information
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Thermochaetoides thermophila
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the enzyme does not hydrolyze cellobiose and cellotriose
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additional information
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Thermochaetoides thermophila
synergistic biodegradation of waste papers using a combination of thermostable endoglucanase CTendo45 and cellobiohydrolase CtCel6 from Chaetomium thermophilum. CtCel6 significantly enhances the bioconversion process, and CTendo45 synergistically increases the degradation, with a maximum degree of synergistic effect of 1.67 when the mass ratio of CTendo45/CtCel6 is 5:3. Enzymatic hydrolysis of different paper materials, e.g. filter paper and office paper giving high activity, or newspaper and cardboard resulting in low activity, foolscap paper gives moderate activity. For newspaper, the recalcitrance to the enzymatic action may be caused by the high contents of hemicelluloses, lignin and various inorganic components
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additional information
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Thermochaetoides thermophila
the bifunctional enzyme also shows endoxylanase activity (EC 3.2.1.8) hydrolyzing beta-1,4-D-xylan from beechwood. Substrate specificity, overview. No endoglucanase activity on (+)-arabinogalactan, D-galacto-D-mannan, amylose, chitin, and sucrose. The enzyme shows activity with pretreated wheat straw and filter paper. CTendo7 produces cellooligosaccharides and xylooligosaccharides from the continuous enzymatic saccharification of carboxymethyl cellulose-Na and xylan, respectively
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additional information
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Thermochaetoides thermophila CBS 144.50
synergistic biodegradation of waste papers using a combination of thermostable endoglucanase CTendo45 and cellobiohydrolase CtCel6 from Chaetomium thermophilum. CtCel6 significantly enhances the bioconversion process, and CTendo45 synergistically increases the degradation, with a maximum degree of synergistic effect of 1.67 when the mass ratio of CTendo45/CtCel6 is 5:3. Enzymatic hydrolysis of different paper materials, e.g. filter paper and office paper giving high activity, or newspaper and cardboard resulting in low activity, foolscap paper gives moderate activity. For newspaper, the recalcitrance to the enzymatic action may be caused by the high contents of hemicelluloses, lignin and various inorganic components
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additional information
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Thermochaetoides thermophila DSM 1495
synergistic biodegradation of waste papers using a combination of thermostable endoglucanase CTendo45 and cellobiohydrolase CtCel6 from Chaetomium thermophilum. CtCel6 significantly enhances the bioconversion process, and CTendo45 synergistically increases the degradation, with a maximum degree of synergistic effect of 1.67 when the mass ratio of CTendo45/CtCel6 is 5:3. Enzymatic hydrolysis of different paper materials, e.g. filter paper and office paper giving high activity, or newspaper and cardboard resulting in low activity, foolscap paper gives moderate activity. For newspaper, the recalcitrance to the enzymatic action may be caused by the high contents of hemicelluloses, lignin and various inorganic components
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additional information
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Thermochaetoides thermophila IMI 039719
synergistic biodegradation of waste papers using a combination of thermostable endoglucanase CTendo45 and cellobiohydrolase CtCel6 from Chaetomium thermophilum. CtCel6 significantly enhances the bioconversion process, and CTendo45 synergistically increases the degradation, with a maximum degree of synergistic effect of 1.67 when the mass ratio of CTendo45/CtCel6 is 5:3. Enzymatic hydrolysis of different paper materials, e.g. filter paper and office paper giving high activity, or newspaper and cardboard resulting in low activity, foolscap paper gives moderate activity. For newspaper, the recalcitrance to the enzymatic action may be caused by the high contents of hemicelluloses, lignin and various inorganic components
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additional information
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no substrates: xylan, avicel, alpha-cellulose, filter paper, laminarin, curdlan
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additional information
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hydrolysis of filter paper
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additional information
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hydrolysis of cotton
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additional information
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hydrolysis of filter paper
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additional information
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substrate specificity, overview. Enzyme MtGH45 is unable to hydrolyze C3 and C4 oligosaccharides, cellobiose and cellotriose are detected as the main products when the enzyme is incubated with cellopentaose, which is completely hydrolyzed and the incubation with cellohexaose generates cellobiose, cellotriose, and cellotetraose as main products
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additional information
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enzyme exhibits both endoglucanase and xylanase activites, reactions of EC 3.2.1.4 and 3.2.1.8, respectively
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additional information
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transglycosylation activity with smaller soluble cellooligosaccharides
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additional information
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substrate-binding mode of cellulase 12A, overview. A network of interactions exists between the enzyme and its substrate. The sugar residues bound to the enzyme appear to be more ordered in the 22 and 21 subsites than in the 11, 12 and 23 subsites. In the E134C crystals the bound 21 sugar at the cleavage site consistently show the alpha-anomeric configuration, implicating an intermediate-like structure
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additional information
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substrate-binding mode of cellulase 12A, overview. A network of interactions exists between the enzyme and its substrate. The sugar residues bound to the enzyme appear to be more ordered in the 22 and 21 subsites than in the 11, 12 and 23 subsites. In the E134C crystals the bound 21 sugar at the cleavage site consistently show the alpha-anomeric configuration, implicating an intermediate-like structure
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additional information
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no activity against starch and Avicel. The recombinant enzyme saccharifies pre-treated wheat straw and bagasse to 3.32% and 3.2%, respectively after 6 h incubation at 85°C
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additional information
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no activity against starch and Avicel. The recombinant enzyme saccharifies pre-treated wheat straw and bagasse to 3.32% and 3.2%, respectively after 6 h incubation at 85°C
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additional information
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among the processings of medicinal and aromatic plants, distillation waste of Cymbopogon winterianus, and bioprocessings of Artemisia annua (an industrial pharmaceutically important plant and source of artemisnin, an antimalarial compound) are selected on the basis of their capability to support higher levels of production of total cellulases, whereas garden waste, primarily consisting of Cynodon dactylon, is considered as the control, representing other lignocellulosic waste. Marc of Artemisia annua, a waste produced in huge amounts after the processing of the Artemisia annua herb, is found to be the suitable substrate for this fungus for maximizing the production of all three constituents of cellulase
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additional information
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among the processings of medicinal and aromatic plants, distillation waste of Cymbopogon winterianus, and bioprocessings of Artemisia annua (an industrial pharmaceutically important plant and source of artemisnin, an antimalarial compound) are selected on the basis of their capability to support higher levels of production of total cellulases, whereas garden waste, primarily consisting of Cynodon dactylon, is considered as the control, representing other lignocellulosic waste. Marc of Artemisia annua, a waste produced in huge amounts after the processing of the Artemisia annua herb, is found to be the suitable substrate for this fungus for maximizing the production of all three constituents of cellulase
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additional information
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among the processings of medicinal and aromatic plants, distillation waste of Cymbopogon winterianus, and bioprocessings of Artemisia annua (an industrial pharmaceutically important plant and source of artemisnin, an antimalarial compound) are selected on the basis of their capability to support higher levels of production of total cellulases, whereas garden waste, primarily consisting of Cynodon dactylon, is considered as the control, representing other lignocellulosic waste. Marc of Artemisia annua, a waste produced in huge amounts after the processing of the Artemisia annua herb, is found to be the suitable substrate for this fungus for maximizing the production of all three constituents of cellulase
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additional information
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free cellulase compared with cellulase immobilized onto Si wafers and amino-terminated surfaces, amount of glucose produced by free cellulase is about 20% higher than that obtained from immobilized cellulase
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additional information
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the fungal enzyme binds specifically to cyst wall cellulose of Acanthamoeba ssp., which causes keratitis in human cornea, overview
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additional information
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cellulase preparations that perform best on hardwood also show superior performance on the softwood substrates
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additional information
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among the processings of medicinal and aromatic plants, distillation waste of Cymbopogon winterianus, and bioprocessings of Artemisia annua (an industrial pharmaceutically important plant and source of artemisnin, an antimalarial compound) are selected on the basis of their capability to support higher levels of production of total cellulases, whereas garden waste, primarily consisting of Cynodon dactylon, is considered as the control, representing other lignocellulosic waste. Marc of Artemisia annua, a waste produced in huge amounts after the processing of the Artemisia annua herb, is found to be the suitable substrate for this fungus for maximizing the production of all three constituents of cellulase
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?
additional information
?
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among the processings of medicinal and aromatic plants, distillation waste of Cymbopogon winterianus, and bioprocessings of Artemisia annua (an industrial pharmaceutically important plant and source of artemisnin, an antimalarial compound) are selected on the basis of their capability to support higher levels of production of total cellulases, whereas garden waste, primarily consisting of Cynodon dactylon, is considered as the control, representing other lignocellulosic waste. Marc of Artemisia annua, a waste produced in huge amounts after the processing of the Artemisia annua herb, is found to be the suitable substrate for this fungus for maximizing the production of all three constituents of cellulase
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additional information
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the low-molecular weight enzyme form is able to form free fibres from filter paper
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additional information
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the hydrolase exhibited chitosanase activity and cellulase activity
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additional information
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no activity towards the insoluble substrates crystalline cellulose and Avicel, and against curdlan, laminarin, xyloglucan, and xylan
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additional information
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enzyme displays highest specific activity against beta-1,4-glycosidic bonds of various linear glucan polysaccharides. Poor or no substrates: avicel, pachyman, laminarin, starch
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additional information
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no substrate: 4-nitrophenyl cellobioside
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additional information
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Umcel9y-1 is an efficient endoglucanase and also exhibits high activities of exoglucanase and transglycosylation. The transglycosylation products of Umcel9y-1 including sophorose, laminaribiose, and gentiobiose, and transglycosylation are detected under all activated conditions. The decreasing order of catalytic efficiency for polysaccharides, cellooligosaccharides, and aryl-beta-glycosides is p-nitrophenyl-D-cellobioside, barley glucan, cellopentaose, cellotetraose, cellotriose, hydroxyethylcellulose, cellohexaose, laminarin, and carboxymethylcellulose, respectively
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additional information
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he later dominance of the dimeric product suggests that the trimer is slowly converted
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additional information
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the enzyme is active with beta-D-glucans containing (1->3)- and (1->4)-bonds (EC 3.2.1.73, licheninase) and with beta-D-glucans containing only (1->4)-bonds (EC 3.2.1.4, cellulase). It shows an exclusive endoacting mechanism. No activity with 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-cellobioside, avicel, curdlan, laminarin, cellulose, carboxymethyl cellulose, and xylan
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additional information
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poor activity against filter paper and avicel
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additional information
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Rucel5B is active towards carboxymethyl cellulose, barley glucan, lichenan, pNPC, PASC, avicel and Whatman NO.1 filter paper, but not active towards laminarin, beta-1,6-glucan and birchwood xylan
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additional information
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no activity against crystalline forms of cellulose such as filter-paper or avicel and the beta-1,3-linked glucan laminarin. No activity with xylan
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additional information
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no hydrolysis of cellulose, cotton, oat splet xylan and birchwood xylan
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additional information
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enzymatic deinking experiments, the ink removal rate in samples treated with the catalytic module is only slightly higher (about 8%), than that of untreated controls, whereas that of the EG1-treated samples is 100% higher. Bio-stoning of denim with EG1-CM results in increases of 48% and 40% in weight loss and indigo dye removal, respectively compared with untreated controls. These increases are considerably lower than the corresponding values of 219% and 133% obtained when samples are treated with EG1
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additional information
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Xf818 carries out transglycosylation. The enzyme is unable to hydrolyse alpha-cellulose and laminarin (a beta-1,3 linked glucan)
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additional information
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Xf818 carries out transglycosylation. The enzyme is unable to hydrolyse alpha-cellulose and laminarin (a beta-1,3 linked glucan)
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additional information
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the enzyme consists of an N-terminal signal peptide, two glycosyl hydrolase family 5 catalytic modules, two novel carbohydrate-binding modules, two linker sequences, and a C-terminal sequence with an unknown function. Removal of the carbohydrate-binding modules from rCel5A reduces the catalytic activities with various polysaccharides remarkably
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additional information
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the enzyme consists of an N-terminal signal peptide, two glycosyl hydrolase family 5 catalytic modules, two novel carbohydrate-binding modules, two linker sequences, and a C-terminal sequence with an unknown function. Removal of the carbohydrate-binding modules from rCel5A reduces the catalytic activities with various polysaccharides remarkably
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xylan + H2O
additional information
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hydrolysis with endoglucanase B, no action with endoglucanase A and C
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xylan + H2O
additional information
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6% of the activity with barley beta-glucan with the insoluble xylan from oats spelt, 27% of the activity with barley beta-glucan with the soluble xylan from oats spelt, catalytic domain of endoglucanase G
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xylan + H2O
additional information
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main products: cellobiose + cellotetraose
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