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Information on EC 3.2.1.73 - licheninase
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EC Tree
3.2.1.73 licheninaseIUBMB Comments
Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.
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Word Map
- 3.2.1.73
- cellulases
-
cellulolytic
- trichoderma
- knee
- reesei
- cellobiohydrolase
- exoglucanase
- thermocellum
- avicel
-
carboxymethyl
-
lignocellulosic
-
cellulosic
-
arthroscopic
-
saccharification
- beta-glucosidase
- carboxymethylcellulose
-
cellulose-binding
- straw
-
microcrystalline
-
glutenins
- cellulosome
- bagasse
- cellotriose
- lichenan
- xyloglucans
- cellulomonas
- cellotetraose
- xylanases
-
3.2.1.4
-
hemicellulases
- cmcase
-
patellar
- endo-beta-1,4-glucanase
-
patellofemoral
- succinogenes
- endoxylanase
-
dockerins
- humicola
-
fpase
- fibrobacter
-
cellulose-degrading
-
lysholm
-
lignocellulolytic
- mannanase
- cellodextrins
- meniscal
- cellobiase
- thermobifida
-
xylanolytic
- brewing
- synthesis
- endocellulase
- agriculture
- biofuel production
- degradation
- food industry
- analysis
- industry
- nutrition
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
endoglucanase, plica, glu-1, glu-3, endo-beta-glucanase, 1,3-1,4-beta-glucanase, 1,3-1,4-beta-d-glucanase, bglc8h, af-egl7, xyniii, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(1->3,1->4)-beta-glucanase isoenzyme EII
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-
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1,3-1,4-beta-D-glucan 4-glucanohydrolase
1,3-1,4-beta-D-glucan glucanohydrolase
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-
-
-
1,3-1,4-beta-D-glucan-4-glucano hydrolase
1,3-1,4-beta-D-glucanase
1,3-1,4-beta-glucanase
1,3;1,4-beta-glucan 4-glucanohydrolase
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1,3;1,4-beta-glucan endohydrolase
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Af-EGL7
Afu6g01800
Beg1
beta-(1,3-1,4)-glucanase
beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase
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-
-
-
beta-1,3-1,4 glucanase
beta-1,3-1,4-D-glucanase
beta-1,3-1,4-glucanase
beta-1,3;1,4-glucanase
beta-glucanase
Bg1314
bgc
bgi
Bgl
bgl5-1
BglA
BglA13
BglA16
BglA51
BglBB
bglBC1
BglM2
BglS
BglT
BglTO
Bglu16A
bifunctional xylanase/endoglucanase
RuCelA, a bifunctional xylanase/endoglucanase, EC 3.2.1.8 and EC 3.2.1.73
BLB369 endo-beta-1,3-1,4-glucanase
Cel5F
CP7 beta-1,3-1,4-glucanase
CtGlu16A
CtLic16A
E-LICHN
EG1
EGL
endo-(1,3;1,4)-beta-glucanase
endo-beta-1,3-1,4 glucanase
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-
-
-
endo-beta-1,3-1,4-glucanase
endo-beta-glucanase
Fisuc_2961
FSU_0226
Gcs2
GH7 endo-1,4-beta-glucanase
glu369
Gluc5_26A
GluIII
GluUS570
lam1
laminarinase
Lic16A
Lic8H
LicA
LicB
Lichenase
LicMB
LicS
McLic1
mHG
Mixed linkage beta-glucanase
-
-
-
-
PlicA
PtLic16A
Ra0505
TaGlu34
TF-glu
TM1752
US8_01508
XynIII
XynZ
1,3-1,4-beta-D-glucan 4-glucanohydrolase
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-
-
-
laminarinase
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Lichenase
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Lichenase
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the multifunctional enzyme domain GH44 possesses cellulase, xylanase, and lichenase activities
Lichenase
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the multifunctional enzyme domain GH44 possesses cellulase, xylanase, and lichenase activities
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XynIII
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bifunctional xylanase showing also beta-(1,3-1,4)-glucanase activity
XynIII
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bifunctional xylanase showing also beta-(1,3-1,4)-glucanase activity
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose + 4 H2O = 5 beta-D-glucopyranose
beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose + 4 H2O = 5 beta-D-glucopyranose
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-
-
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beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose + 4 H2O = 5 beta-D-glucopyranose
mechanism, kinetic model
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beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose + 4 H2O = 5 beta-D-glucopyranose
allosteric activation mechanism, feedback inhibition
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beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose + 4 H2O = 5 beta-D-glucopyranose
beta-1,3-1,4-glucanase catalyzes strict endo-hydrolysis of the beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in the mixed-linked beta-glucans via a double-displacement mechanism
beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose + 4 H2O = 5 beta-D-glucopyranose
the enzyme might carry out the hydrolysis via retaining mechanism with E113 and E118 serving as the nucleophile and general acid/base, respectively,catalytic mechanism, overview
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beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose + 4 H2O = 5 beta-D-glucopyranose
the enzyme might carry out the hydrolysis via retaining mechanism with E113 and E118 serving as the nucleophile and general acid/base, respectively,catalytic mechanism, overview
beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose + 4 H2O = 5 beta-D-glucopyranose
beta-1,3-1,4-glucanase catalyzes strict endo-hydrolysis of the beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in the mixed-linked beta-glucans via a double-displacement mechanism
Acetivibrio thermocellus DSM 1237
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beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose + 4 H2O = 5 beta-D-glucopyranose
the enzyme might carry out the hydrolysis via retaining mechanism with E113 and E118 serving as the nucleophile and general acid/base, respectively,catalytic mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
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SYSTEMATIC NAME
IUBMB Comments
(1->3)-(1->4)-beta-D-glucan 4-glucanohydrolase
Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.
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CAS REGISTRY NUMBER
COMMENTARY
37288-51-0
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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
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
2,4-dinitrophenol + beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
-
-
?
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
3,4-dinitrophenol + beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
-
-
?
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucopyranoside + H2O
4-methylumbelliferone + 3-O-beta-cellobiosyl-beta-D-glucopyranoside
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-
-
?
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
4-methylumbelliferone + 3-O-beta-cellobiosyl-beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
-
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
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-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc + F-
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-
-
-
?
4-methylumbelliferyl-(1,3)-beta-D-glucooligosaccharides + H2O
4-methylumbelliferol + beta-D-oligosaccharides
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-
-
-
?
4-methylumbelliferyl-beta-D-Gal-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
?
-
Gal substrate has a 1.3fold higher kcat/KM-value than Glc substrate
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r
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc + H2O
4-methylumbelliferone + beta-D-Glc-(1-3)-beta-D-Glc
-
-
-
-
?
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
4-methylumbelliferone + beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
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-
-
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?
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
?
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Gal substrate has a 1.3fold higher kcat/KM-value than Glc substrate
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-
r
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
4-methylumbelliferone + beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
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-
-
-
?
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
4-methylumbelliferone + beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
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?
4-nitrophenyl beta-D-cellobioside + H2O
?
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1% of the activity with carboxymethyl-cellulose
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?
4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-2-deoxy-beta-D-erythro-pentopyranoside + H2O
?
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2-deoxy analog is better substrate than corresponding 2-hydroxy substrate
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?
4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-arabinopyranoside + H2O
?
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2-deoxy analog is better substrate than corresponding 2-hydroxy substrate
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?
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + F-
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?
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc + F-
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?
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-glucopyranoside
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
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?
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-xylopyranoside
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Xyl + F-
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?
alpha-laminaribiosyl fluoride + 4-nitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc
4-nitrophenyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc + F-
-
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?
alpha-laminaribiosyl fluoride + 4-nitrophenyl-beta-D-glucopyranoside
4-nitrophenyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
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?
alpha-laminaribiosyl fluoride + 4-nitrophenyl-beta-D-xylopyranoside
4-nitrophenyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Xyl + F-
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?
alpha-laminaribiosyl fluoride + methyl beta-D-Glc-(1-3)-beta-D-Glc
methyl beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + F-
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?
alpha-laminaribiosyl fluoride + methyl beta-D-Glc-(1-4)-beta-D-Glc
methyl beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc + F-
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?
barley beta-glucan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose + ?
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?
barley beta-glucan + H2O
beta-D-glucose + cellobiose + ?
enzyme NFEg16A efficiently hydrolyzes the substrate at a high concentration of 15 mg/mL, and releases glucose and cellobiose as its main end products
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?
barley beta-glucan + H2O
Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH
cellohexaose + H2O
cellobiose + cellotriose
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no release of D-glucose
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?
chitosan + H2O
?
81.3% of the activity with barley beta-D-glucan
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?
Glcbeta(1-3)Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glc + H2O
glucose + Glcbeta(1-3)Glcbeta(1-4)Glcbeta(1-4)Glc
-
-
-
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?
Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-3)Glcbeta(1-4)Glcbeta(1-4)Glc-OMe + H2O
?
-
-
-
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?
Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-3)Glc + H2O
?
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-
-
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?
Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta-O-4-methylumbeliferone + H2O
?
-
-
-
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?
glucan tetrasaccharide + H2O
D-glucose + glucan trisaccharide
containing two beta-1,4-linkages separated by one beta-1,3-linkage, i.e. G4G3G4G
containing one beta-1,4-linkage separated by one beta-1,3-linkage, i.e. G4G3G, which is not further degraded
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?
laminaritriose + H2O
D-glucose + laminaribiose
the smallest oligosaccharide that can be degraded by the enzyme
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?
lichenan + H2O
cellobiose + Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH
oat beta-glucan + H2O
beta-glucan oligosaccharides
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92% of the activity with barley beta-glucan
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?
avicel + H2O
?
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50% of the activity with carboxymethyl-cellulose
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?
barley beta-glucan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose
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oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
barley beta-glucan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose
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-
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
barley beta-glucan + H2O
?
best substrate, 1% w/v substrate concentration, best substrate
-
-
?
barley beta-glucan + H2O
?
best substrate, 1% w/v substrate concentration, best substrate
-
-
?
barley beta-glucan + H2O
?
best substrate, 1% w/v substrate concentration, best substrate
-
-
?
barley beta-glucan + H2O
?
Aspergillus fumigatus CBS 101355
best substrate, 1% w/v substrate concentration, best substrate
-
-
?
barley beta-glucan + H2O
?
Aspergillus fumigatus FGSC A1100
best substrate, 1% w/v substrate concentration, best substrate
-
-
?
barley beta-glucan + H2O
?
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
63% of the activity with oat gum
-
-
?
barley beta-glucan + H2O
?
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
best substrate
-
-
?
barley beta-glucan + H2O
?
best substrate
-
-
?
barley beta-glucan + H2O
?
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
Rasamsonia emersonii CBS 841.70
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
-
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the enzyme produces glucosyl beta-1,3 glucosyl beta-1,4 glucose as the major end product, glucosyl beta-1,4 glucosyl beta-1,3 glucose is not detected
-
?
barley beta-glucan + H2O
?
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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the enzyme produces glucosyl beta-1,3 glucosyl beta-1,4 glucose as the major end product, glucosyl beta-1,4 glucosyl beta-1,3 glucose is not detected
-
?
barley beta-glucan + H2O
?
endo-beta-glucanase BP_Cel9A hydrolyzes beta-1,3-1,4-linked barley beta-glucan, best substrate
-
-
?
barley beta-glucan + H2O
beta-glucan oligosaccharides
Bacillus sp. (in: Bacteria) KCCM 90078
-
-
-
-
?
barley beta-glucan + H2O
beta-glucan oligosaccharides
-
-
-
-
?
barley beta-glucan + H2O
beta-glucan oligosaccharides
-
-
-
-
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
-
-
oligosaccharides (mainly trisaccharide and tetrasaccharide) followed by disaccharide (cellobiose) and glucose are formed as the major products of hydrolysis after a prolonged incubation of 4 h
-
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
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-
oligosaccharides (mainly trisaccharide and tetrasaccharide) followed by disaccharide (cellobiose) and glucose are formed as the major products of hydrolysis after a prolonged incubation of 4 h
-
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
-
best substrate
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
-
best substrate
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
best substrate
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
best substrate
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
barley beta-glucan + H2O
Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH
-
final products
-
?
barley beta-glucan + H2O
Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH
-
final products
-
?
barley-beta-glucan + H2O
?
KM079629
best substrate, azo-barley-glucan as the substrate
-
-
?
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose
-
-
?
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
from oat and barley
-
-
?
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose
-
-
?
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
from oat and barley
-
-
?
beta-1,3-1,4-glucan + H2O
?
-
from Hordeum vulgare, best substrate
-
-
?
beta-1,3-1,4-glucan + H2O
?
source of substrate: barley
-
-
?
beta-1,3/1,4-glucan + H2O
?
best substrate is 1,3/1,4-beta-glucan from Hordeum vulgare, and almost equally active from Avena sativa
-
-
?
beta-1,3/1,4-glucan + H2O
?
best substrate is 1,3/1,4-beta-glucan from Hordeum vulgare, and almost equally active from Avena sativa
-
-
?
beta-D-glucan + H2O
?
source: barley, best substrate
hydrolysis products from barley beta-glucan are 6.8 micromol/ml glucose and 16.3 micromol/ml cellobiose
-
?
beta-D-glucan + H2O
?
-
the two extremely different folds adopted by GHF16 and GHF17 enzymes, beta-jellyroll and (beta/alpha)8, respectively, accommodate mixed beta-1,3 and beta-1,4 beta-D-glucans or lichenan
-
-
?
carboxymethyl cellulose + H2O
?
1% w/v substrate concentration, low activity
-
-
?
carboxymethyl cellulose + H2O
?
1% w/v substrate concentration, low activity
-
-
?
carboxymethyl cellulose + H2O
?
1% w/v substrate concentration, low activity
-
-
?
carboxymethyl cellulose + H2O
?
Aspergillus fumigatus CBS 101355
1% w/v substrate concentration, low activity
-
-
?
carboxymethyl cellulose + H2O
?
Aspergillus fumigatus FGSC A1100
1% w/v substrate concentration, low activity
-
-
?
carboxymethyl cellulose + H2O
?
9.8% of the activity with beta-D-glucan
-
-
?
carboxymethyl cellulose + H2O
?
32.2% of the activity with barley beta-D-glucan
-
-
?
carboxymethyl cellulose + H2O
?
22.4% activity compared to barley beta-glucan
-
-
?
carboxymethyl-cellulose + H2O
?
-
a negligible amount of hydrolysis of carboxymethyl-cellulose is observed
-
-
?
carboxymethyl-cellulose + H2O
?
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
a negligible amount of hydrolysis of carboxymethyl-cellulose is observed
-
-
?
carboxymethylcellulose + H2O
?
52% of the activity with oat gum
-
-
?
carboxymethylcellulose + H2O
?
-
18% of the activity with beta-1,3-1,4-glucan from Hordeum vulgare
-
-
?
cellopentaose + H2O
cellobiose + D-glucose
-
with N-terminal deletion mutant, products are cellotriose and cellobiose
-
?
cellopentaose + H2O
cellobiose + D-glucose
-
with N-terminal deletion mutant, products are cellotriose and cellobiose
-
?
cellulose + H2O
?
-
7% of the activity with beta-1,3-1,4-glucan from Hordeum vulgare
-
-
?
cellulose + H2O
?
filter paper
main products are cellobiose and cellotriose
-
?
Glc-beta(1,4)-Glc-beta(1,4)-Glc-beta(1,3)-Glc + H2O
cellobiose + laminaribiose
-
with N-terminal deletion mutant, products are cellotriose and D-glucose
-
?
Glc-beta(1,4)-Glc-beta(1,4)-Glc-beta(1,3)-Glc + H2O
cellobiose + laminaribiose
-
with N-terminal deletion mutant, products are cellotriose and D-glucose
-
?
laminarin + H2O
?
-
70% of the activity with carboxymethyl-cellulose
-
-
?
laminarin + H2O
?
-
20.5% activity compared to barley beta-glucan
-
-
?
laminarin + H2O
?
Paenibacillus barengoltzii CAU904
-
20.5% activity compared to barley beta-glucan
-
-
?
laminarin + H2O
?
4.1% of the activity with barley beta-D-glucan
-
-
?
laminarin + H2O
?
0.12% activity compared to barley beta-glucan
-
-
?
laminarin + H2O
?
the wild-type enzyme displays a bent topology adapted to the binding of helical-shaped laminarin
-
-
?
lichenan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose
-
-
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
lichenan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose
-
-
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
lichenan + H2O
?
-
500% of the activity with carboxymethyl-cellulose
-
-
?
lichenan + H2O
?
72% of the activity with beta-D-glucan
hydrolysis products from lichenan are 9.1 micromol/ml glucose and 9.9 micromol/ml cellobiose, and 0.45 micromol/ml cellotetraose
-
?
lichenan + H2O
?
-
the two extremely different folds adopted by GHF16 and GHF17 enzymes, beta-jellyroll and (beta/alpha)8, respectively, accommodate mixed beta-1,3 and beta-1,4 beta-D-glucans or lichenan
-
-
?
lichenan + H2O
?
-
85% of the activity with beta-1,3-1,4-glucan from Hordeum vulgare
-
-
?
lichenan + H2O
?
a beta-1,3/1,4-glucan from Cetraria islandica, half as active as barley or oat beta-1,3/1,4-glucans
-
-
?
lichenan + H2O
?
a beta-1,3/1,4-glucan from Cetraria islandica, half as active as barley or oat beta-1,3/1,4-glucans
-
-
?
lichenan + H2O
?
68.8% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
14.5% of the activity with barley beta-D-glucan
-
-
?
lichenan + H2O
?
136.4% activity compared to barley beta-glucan
-
-
?
lichenan + H2O
?
-
68.2% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
Thermoascus aurantiacus CAU830
-
68.2% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
-
-
the enzyme produces glucosyl beta-1,3 glucosyl beta-1,4 glucose as the major end product, glucosyl beta-1,4 glucosyl beta-1,3 glucose is not detected
-
?
lichenan + H2O
?
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
the enzyme produces glucosyl beta-1,3 glucosyl beta-1,4 glucose as the major end product, glucosyl beta-1,4 glucosyl beta-1,3 glucose is not detected
-
?
lichenan + H2O
?
67% activity compared to barley beta-glucan
-
-
?
lichenan + H2O
beta-D-Glc-(1->3)-beta-D-Glc-(1->4)-beta-D-Glc + ?
beta-D-Glc-(1->4)-beta-D-Glc-(1->3)-beta-D-Glc is not detected as product
-
-
?
lichenan + H2O
beta-D-Glc-(1->3)-beta-D-Glc-(1->4)-beta-D-Glc + ?
beta-D-Glc-(1->4)-beta-D-Glc-(1->3)-beta-D-Glc is not detected as product
-
-
?
lichenan + H2O
cellobiose + Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH
-
final products
-
?
lichenan + H2O
cellobiose + Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH
-
final products
-
?
lichenan + H2O
cellotriose + ?
95.2% activity compared to barley beta-glucan
oligosaccharides, mainly trisaccharide
-
?
lichenan + H2O
cellotriose + ?
95.2% activity compared to barley beta-glucan
oligosaccharides, mainly trisaccharide
-
?
lichenan + H2O
cellotriose + cellotetraose + ?
-
93.5% activity compared to barley beta-glucan
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
lichenan + H2O
cellotriose + cellotetraose + ?
-
93.5% activity compared to barley beta-glucan
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
lichenin + H2O
?
-
49.8% activity compared to barley beta-glucan
-
-
?
lichenin + H2O
?
-
50% of the activity with barley beta-glucan
-
-
?
lichenin + H2O
?
Paenibacillus barengoltzii CAU904
-
49.8% activity compared to barley beta-glucan
-
-
?
lichenin + H2O
?
Paenibacillus barengoltzii CAU904
-
50% of the activity with barley beta-glucan
-
-
?
oat beta-glucan + H2O
?
-
92.3% activity compared to barley beta-glucan
-
-
?
oat beta-glucan + H2O
?
-
92.4% of the activity with barley beta-glucan
-
-
?
oat beta-glucan + H2O
?
Thermoascus aurantiacus CAU830
-
92.4% of the activity with barley beta-glucan
-
-
?
sugarcane exploded bagasse + H2O
?
1% w/v substrate concentration, sugarcane exploded bagasse biomass (SEB). SEB is a highly heterogeneous material that consists of 47.5% cellulose, 9.0% hemicellulose, and 34.3% lignin
-
-
?
sugarcane exploded bagasse + H2O
?
1% w/v substrate concentration, sugarcane exploded bagasse biomass (SEB). SEB is a highly heterogeneous material that consists of 47.5% cellulose, 9.0% hemicellulose, and 34.3% lignin
-
-
?
sugarcane exploded bagasse + H2O
?
1% w/v substrate concentration, sugarcane exploded bagasse biomass (SEB). SEB is a highly heterogeneous material that consists of 47.5% cellulose, 9.0% hemicellulose, and 34.3% lignin
-
-
?
sugarcane exploded bagasse + H2O
?
Aspergillus fumigatus CBS 101355
1% w/v substrate concentration, sugarcane exploded bagasse biomass (SEB). SEB is a highly heterogeneous material that consists of 47.5% cellulose, 9.0% hemicellulose, and 34.3% lignin
-
-
?
sugarcane exploded bagasse + H2O
?
Aspergillus fumigatus FGSC A1100
1% w/v substrate concentration, sugarcane exploded bagasse biomass (SEB). SEB is a highly heterogeneous material that consists of 47.5% cellulose, 9.0% hemicellulose, and 34.3% lignin
-
-
?
xylan + H2O
?
-
500% of the activity with carboxymethyl-cellulose
-
-
?
xyloglucan + H2O
?
high activity, xyloglucan from tamarind seed, 1% w/v substrate concentration
-
-
?
xyloglucan + H2O
?
high activity, xyloglucan from tamarind seed, 1% w/v substrate concentration
-
-
?
xyloglucan + H2O
?
high activity, xyloglucan from tamarind seed, 1% w/v substrate concentration
-
-
?
xyloglucan + H2O
?
Aspergillus fumigatus CBS 101355
high activity, xyloglucan from tamarind seed, 1% w/v substrate concentration
-
-
?
xyloglucan + H2O
?
Aspergillus fumigatus FGSC A1100
high activity, xyloglucan from tamarind seed, 1% w/v substrate concentration
-
-
?
xyloglucan + H2O
?
40% activity compared to barley beta-glucan
-
-
?
barley beta-glucan + H2O
additional information
-
-
-
pentose, triose, tetarose and a high molecular weight polysaccharide with 1,3 linkage
-
?
barley beta-glucan + H2O
additional information
-
-
-
pentose, triose, tetrose and a high molecular weight polysaccharide with 1,3 linkage
-
?
barley beta-glucan + H2O
additional information
-
-
-
pentose, triose, tetarose and a high molecular weight polysaccharide with 1,3 linkage
-
?
barley beta-glucan + H2O
additional information
-
-
-
pentose, triose, tetrose and a high molecular weight polysaccharide with 1,3 linkage
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from oat
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
main products are triose and tetraose
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
oligosaccharides are formed as the major products, no glucose
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from oat
oligosaccharides are formed as the major products, no glucose
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
carboxymethyl beta-glucan + H2O
additional information
-
-
carboxymethyl beta-glucan from barley
trisaccharide, 53%, tetrasaccharide, 25%
?
lichenin + H2O
additional information
-
-
-
main products are triose and tetraose
?
lichenin + H2O
additional information
-
-
lichenin from Cetralia islandica and from Usnea barbata
-
-
?
additional information
?
-
-
no activity against beta-1,4- or beta-1,3 homopolymers of gluco- or manno-configured polysaccharides
-
-
?
additional information
?
-
-
lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose
-
-
?
additional information
?
-
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
?
additional information
?
-
-
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
?
additional information
?
-
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
?
additional information
?
-
-
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Acetivibrio thermocellus DSM 1237
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
?
additional information
?
-
Acetivibrio thermocellus DSM 1237
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus DSM 1237
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Acetivibrio thermocellus NBRC 103400
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus NBRC 103400
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Acetivibrio thermocellus NCIMB 10682
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus NCIMB 10682
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Acetivibrio thermocellus NRRL B-4536
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus NRRL B-4536
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Acetivibrio thermocellus VPI 7372
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus VPI 7372
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose
-
-
?
additional information
?
-
the enzyme exhibits higher activity toward beta-glucan than toward xyloglucan and carboxymethyl cellulose suggesting that the enzyme corresponds to a beta-1,3-1,4-glucanase. No activity with Avicel and beechwood xylan
-
-
?
additional information
?
-
-
the enzyme exhibits higher activity toward beta-glucan than toward xyloglucan and carboxymethyl cellulose suggesting that the enzyme corresponds to a beta-1,3-1,4-glucanase. No activity with Avicel and beechwood xylan
-
-
?
additional information
?
-
the enzyme exhibits higher activity toward beta-glucan than toward xyloglucan and carboxymethyl cellulose suggesting that the enzyme corresponds to a beta-1,3-1,4-glucanase. No activity with Avicel and beechwood xylan
-
-
?
additional information
?
-
the enzyme exhibits higher activity toward beta-glucan than toward xyloglucan and carboxymethyl cellulose suggesting that the enzyme corresponds to a beta-1,3-1,4-glucanase. No activity with Avicel and beechwood xylan
-
-
?
additional information
?
-
Aspergillus fumigatus CBS 101355
the enzyme exhibits higher activity toward beta-glucan than toward xyloglucan and carboxymethyl cellulose suggesting that the enzyme corresponds to a beta-1,3-1,4-glucanase. No activity with Avicel and beechwood xylan
-
-
?
additional information
?
-
Aspergillus fumigatus FGSC A1100
the enzyme exhibits higher activity toward beta-glucan than toward xyloglucan and carboxymethyl cellulose suggesting that the enzyme corresponds to a beta-1,3-1,4-glucanase. No activity with Avicel and beechwood xylan
-
-
?
additional information
?
-
-
does not hydrolyze carboxymethyl-cellulose or avicel cellulose
-
-
?
additional information
?
-
-
the enzyme is a conformation-retaining and is only active toward glucan containing beta-1,3-1,4-linkages. No activity with laminarin and carboxymethyl cellulose
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
does not hydrolyze carboxymethyl-cellulose or avicel cellulose
-
-
?
additional information
?
-
-
the enzyme is a conformation-retaining and is only active toward glucan containing beta-1,3-1,4-linkages. No activity with laminarin and carboxymethyl cellulose
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Aspergillus terreus ASKU 10
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans
-
-
?
additional information
?
-
native and recombinant enzymes are both inactive on laminarin, cellulose, xylan, or mannan
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans
-
-
?
additional information
?
-
native and recombinant enzymes are both inactive on laminarin, cellulose, xylan, or mannan
-
-
?
additional information
?
-
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
?
additional information
?
-
-
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
antifungal enzyme activity assay
-
-
?
additional information
?
-
antifungal enzyme activity assay
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
activity against 1% carboxymethylcellulose is not observed
-
-
?
additional information
?
-
-
no activity with carboxymethyl cellulose and laminarin, isozymes EG1 and EG2 exhibit no activity for pure beta-1,3 bond and for pure beta-1,4 glucan forms
-
-
?
additional information
?
-
-
enzyme exhibits strict specificity for beta-1,3-1,4-D-glucans
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Bacillus licheniformis EGW039 / CGMCC 0635
-
activity against 1% carboxymethylcellulose is not observed
-
-
?
additional information
?
-
Bacillus licheniformis EGW039 / CGMCC 0635
-
no activity on cellulose
-
-
?
additional information
?
-
-
enzyme exhibits strict specificity for beta-1,3-1,4-D-glucans
-
-
?
additional information
?
-
-
no activity with carboxymethyl cellulose and laminarin, isozymes EG1 and EG2 exhibit no activity for pure beta-1,3 bond and for pure beta-1,4 glucan forms
-
-
?
additional information
?
-
no substrates: laminarin and carboxymethylcellulose
-
-
?
additional information
?
-
-
no substrates: laminarin and carboxymethylcellulose
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Bacillus pumilus US570
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Bacillus pumilus US570
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
no hydrolysis of carboxymethylpachyman
-
-
?
additional information
?
-
-
no hydrolysis of carboxymethylcellulose
-
-
?
additional information
?
-
beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans
-
-
?
additional information
?
-
thin layer product identification
-
-
?
additional information
?
-
beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans
-
-
?
additional information
?
-
thin layer product identification
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Bacillus sp. N137
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Bacillus sp. N137
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
no activity against carboxymethylcellulose, xylan, laminarin, dextrin
-
-
?
additional information
?
-
the enzyme hydrolyzes plant cell wall beta-glucans
-
-
?
additional information
?
-
-
the enzyme hydrolyzes plant cell wall beta-glucans
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
the enzyme hydrolyzes plant cell wall beta-glucans
-
-
?
additional information
?
-
-
no activity against carboxymethylcellulose, xylan, laminarin, dextrin
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Bacillus subtilis NCIB 8565
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Bacillus subtilis NCIB 8565
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
no activity with carboxymethyl cellulose, xylan, laminarin, and soluble starch, substrate specificity, overview
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
no activity with carboxymethyl cellulose, xylan, laminarin, and soluble starch, substrate specificity, overview
-
-
?
additional information
?
-
enzyme displays low activity on avicel, cellobiose, filter paper, p-nitrophenyl beta-D-cellobioside, and p-nitrophenyl beta-D-glucoside, and no activity against microcrystalline cellulose or salicin
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
carboxymethylcellulose and starch are no substrates
-
-
?
additional information
?
-
poor substrates: laminarin, oat spelt xylan. No substrate: avicel
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
carboxymethylcellulose and arabinoxylan are no substrates
-
-
?
additional information
?
-
-
carboxymethylcellulose, arabinoxylan, laminarin, and starch are no substrates
-
-
?
additional information
?
-
-
no hydrolysis of carboxymethylpachyman
-
-
?
additional information
?
-
-
no hydrolysis of carboxymethylcellulose
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
also active with laminarin, poor activity with Avicel, rice straw, and xylan, no activity with 4-nitrophenyl-beta-D-hexoside derivatives, substrate specificity, overview
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
the enzyme shows strict substrate specificity for barley beta-glucan, oat beta-glucan and lichenan, but is not active with other tested polysaccharides and synthetic 4-nitrophenyl derivates
-
-
?
additional information
?
-
-
the enzyme shows strict substrate specificity for barley beta-glucan, oat beta-glucan and lichenan, but is not active with other tested polysaccharides and synthetic 4-nitrophenyl derivates
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
the enzyme shows strict substrate specificity for barley beta-glucan, oat beta-glucan and lichenan, but is not active with other tested polysaccharides and synthetic 4-nitrophenyl derivates
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Niallia circulans ATCC 21367
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Niallia circulans ATCC 21367
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
purified recombinant EGL2 protein hydrolyzes beta-1,3/1,4-glucans, but not beta-1,3/1,6-linked or beta-1,3-linked glucopolysaccharides, e.g. laminarin from Laminaria digitata or Eisenia bicyclis, or curdlan from Alcaligenes faecalis, nor carboxymethylcellulose
-
-
?
additional information
?
-
-
purified recombinant EGL2 protein hydrolyzes beta-1,3/1,4-glucans, but not beta-1,3/1,6-linked or beta-1,3-linked glucopolysaccharides, e.g. laminarin from Laminaria digitata or Eisenia bicyclis, or curdlan from Alcaligenes faecalis, nor carboxymethylcellulose
-
-
?
additional information
?
-
purified recombinant EGL1 protein hydrolyzes beta-1,3/1,4-glucans, but not beta-1,3/1,6-linked or beta-1,3-linked glucopolysaccharides, e.g. laminarin from Laminaria digitata or Eisenia bicyclis, or curdlan from Alcaligenes faecalis, nor carboxymethylcellulose
-
-
?
additional information
?
-
strictly specific for beta-1,3-1,4-glucans. No substrates are: Avicel, carboxymethyl-cellulose, cellulose, filter paper, beta-1,3-glucan, laminarin, and birchwood xylan
-
-
?
additional information
?
-
-
strictly specific for beta-1,3-1,4-glucans. No substrates are: Avicel, carboxymethyl-cellulose, cellulose, filter paper, beta-1,3-glucan, laminarin, and birchwood xylan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanase strictly cleaves the beta-1,4-D-glucosidic bonds adjacent to beta-1,3-linkages in mixed linked beta-glucans
-
-
?
additional information
?
-
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan
-
-
?
additional information
?
-
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan. Computer modeling of active-site bound oligosaccharides, overview
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-glucanase does not act toward avicel, carboxymethylcellulose, cellulose, filter paper, beta-1,3-glucan, hydroxyethyl-cellulose, laminarin, starch, pullulan, birchwood xylan, locust bean gum, cellobiose, and xylobiose. No activity for p-nitrophenyl-beta-D-glucopyranoside, p-nitrophenyl-beta-D-xylopyranoside, p-nitrophenyl-beta-D-fucopyranoside, p-nitrophenyl-beta-D-galactopyranoside, and p-nitrophenyl-beta-D-mannopyranoside
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan. Computer modeling of active-site bound oligosaccharides, overview
-
-
?
additional information
?
-
-
beta-glucanase does not act toward avicel, carboxymethylcellulose, cellulose, filter paper, beta-1,3-glucan, hydroxyethyl-cellulose, laminarin, starch, pullulan, birchwood xylan, locust bean gum, cellobiose, and xylobiose. No activity for p-nitrophenyl-beta-D-glucopyranoside, p-nitrophenyl-beta-D-xylopyranoside, p-nitrophenyl-beta-D-fucopyranoside, p-nitrophenyl-beta-D-galactopyranoside, and p-nitrophenyl-beta-D-mannopyranoside
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan. Computer modeling of active-site bound oligosaccharides, overview
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
no detectable hydrolysis activity is observed towards xylan, pullulan, soluble starch, carboxymethyl cellulose, and artificially synthesized 4-nitrophenyl-glycosides
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Paenibacillus barengoltzii CAU904
-
no detectable hydrolysis activity is observed towards xylan, pullulan, soluble starch, carboxymethyl cellulose, and artificially synthesized 4-nitrophenyl-glycosides
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
the enzyme specifically catalyzes the hydrolysis of beta-1,4-glycosidic bonds located prior to beta-1,3-glycosidic linkages in 1,3-1,4-beta-glucan
-
-
?
additional information
?
-
enzyme substrate specificity, overview. No activity with laminarin, carboxymethyl cellulose, xylan and soluble starch
-
-
?
additional information
?
-
enzyme hydrolyzes mixed-linked beta-1,3-1,4-glucans and chitosan as well as carboxymethyl cellulose, showing activities of EC 3.2.1.6 and EC 3.2.1.74
-
-
?
additional information
?
-
the enzyme specifically catalyzes the hydrolysis of beta-1,4-glycosidic bonds located prior to beta-1,3-glycosidic linkages in 1,3-1,4-beta-glucan
-
-
?
additional information
?
-
enzyme substrate specificity, overview. No activity with laminarin, carboxymethyl cellulose, xylan and soluble starch
-
-
?
additional information
?
-
-
no activity with carboxymethyl cellulose, laminarin, xylan, scleroglucan, and starch, substrate specificity, overview. The enzyme is inactive toward alpha-1,4, alpha-1,6, beta-1,4 and beta-1,6 linkages
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
no activity with carboxymethyl cellulose, laminarin, xylan, scleroglucan, and starch, substrate specificity, overview. The enzyme is inactive toward alpha-1,4, alpha-1,6, beta-1,4 and beta-1,6 linkages
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Rasamsonia emersonii CBS 841.70
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
thin layer chromatography product analysis, overview. Poor activity with laminarin, no activity with birchwood xylan, carboxymethyl cellulose, pullulan, soluble starch, locust bean gum, cellulose, Avicel, beta-1,3-glucan, 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-beta-D-xylopyranoside, and 4-nitrophenyl-beta-D-galactopyranoside, substrate specificity, overview
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
thin layer chromatography product analysis, overview. Poor activity with laminarin, no activity with birchwood xylan, carboxymethyl cellulose, pullulan, soluble starch, locust bean gum, cellulose, Avicel, beta-1,3-glucan, 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-beta-D-xylopyranoside, and 4-nitrophenyl-beta-D-galactopyranoside, substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme shows only residual activity against 1,3-beta-glucan (laminarin) or no activity at all against 1,4-beta-glucan (cellulose), chitin, xylan, or manan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Rhodothermus marinus ITI378
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Rhodothermus marinus ITI378
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
carboxymethylcellulose and arabinoxylan are no substrates
-
-
?
additional information
?
-
-
does not hydrolyze laminaripentaose and cellopentaose
-
-
?
additional information
?
-
-
reported fungal eta-1,3-1,4-glucanases exhibit strict substrate specificity toward barley beta-glucan, oat beta-glucan and lichenan, of which the structures are all beta-(1,4)-linked glucose interrupted with beta-(1,3)-linkages. beta-1,3-1,4-Glucanases (lichenases) specifically hydrolyze the beta-1,4 glycosidic linkages adjacent to beta-1,3 bonds, yielding disaccharides, trisaccharides and tetrasaccharides as the major products. Enzyme TaGlu34 hydrolyzes barley beta-glucan and lichanan to produce mainly disaccharide and trisaccharide without formation of tetrasaccharide. Production of glucan oligosaccharides from oat bran by TaGlu34
-
-
?
additional information
?
-
-
no activity towards other tested polysaccharides including laminarin, CMC, birchwood xylan, pullulan, soluble starch and locust bean gum, and 4-nitrophenyl derivates such as 4-nitrophenyl-beta-xylopyranoside, 4-nitrophenyl-beta-galactopyranoside, 4-nitrophenyl alpha-galactopyranoside, 4-nitrophenyl beta-glucopyranoside and 4-nitrophenyl-alpha-glucopyranoside
-
-
?
additional information
?
-
Thermoascus aurantiacus CAU830
-
reported fungal eta-1,3-1,4-glucanases exhibit strict substrate specificity toward barley beta-glucan, oat beta-glucan and lichenan, of which the structures are all beta-(1,4)-linked glucose interrupted with beta-(1,3)-linkages. beta-1,3-1,4-Glucanases (lichenases) specifically hydrolyze the beta-1,4 glycosidic linkages adjacent to beta-1,3 bonds, yielding disaccharides, trisaccharides and tetrasaccharides as the major products. Enzyme TaGlu34 hydrolyzes barley beta-glucan and lichanan to produce mainly disaccharide and trisaccharide without formation of tetrasaccharide. Production of glucan oligosaccharides from oat bran by TaGlu34
-
-
?
additional information
?
-
Thermoascus aurantiacus CAU830
-
no activity towards other tested polysaccharides including laminarin, CMC, birchwood xylan, pullulan, soluble starch and locust bean gum, and 4-nitrophenyl derivates such as 4-nitrophenyl-beta-xylopyranoside, 4-nitrophenyl-beta-galactopyranoside, 4-nitrophenyl alpha-galactopyranoside, 4-nitrophenyl beta-glucopyranoside and 4-nitrophenyl-alpha-glucopyranoside
-
-
?
additional information
?
-
Thermomonospora sp.
-
no activity towards avicel, laminarin, gum arabic, p-nitrophenyl glucoside, and p-nitrophenyl xylopyranoside
-
-
?
additional information
?
-
-
does not display any activity on crystalline cellulose or laminarin
-
-
?
additional information
?
-
no activity with crystalline cellulose, carbocymethyl cellulose, Avicel, curdlan, starch, pustulan, birchwood xylan or laminarin
-
-
?
additional information
?
-
no activity with crystalline cellulose, carbocymethyl cellulose, Avicel, curdlan, starch, pustulan, birchwood xylan or laminarin
-
-
?
additional information
?
-
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
does not display any activity on crystalline cellulose or laminarin
-
-
?
additional information
?
-
-
the purified enzyme fraction shows no activity on laminarin and xylan
-
-
?
additional information
?
-
-
the purified enzyme fraction shows no activity on laminarin and xylan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
no activitiy using beta-1,3-glucan, laminarin, or Avicel as substrates
-
-
?
additional information
?
-
enzyme NFEg16A does not show clear activity against nature product of laminarin and carboxymethylcellulose-Na, but shows activity on barley beta-glucan, which might indicate that it is a true beta-1,3-1,4-glucanase (EC 3.2.1.73)
-
-
?
additional information
?
-
the enzyme specifically cleaves beta-1,4-linkages next to beta-1,3-linkages and is active on linear 1,3-beta-D-glucans with 3-6 monomers and on a glucan tetrasaccharide containing two beta-1,4-linkages separated by one beta-1,3-linkage. Enzyme-substrate complex structure analysis using wild-type and mutant enzymes with glucan oligomers, binding structure and substrate recognition, overview
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose
-
-
?
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose
-
-
?
additional information
?
-
-
lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose
-
-
?
additional information
?
-
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
?
additional information
?
-
-
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus DSM 1237
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
?
additional information
?
-
Acetivibrio thermocellus DSM 1237
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus NBRC 103400
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus NCIMB 10682
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus NRRL B-4536
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus VPI 7372
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Aspergillus terreus ASKU 10
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Bacillus pumilus US570
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans
-
-
?
additional information
?
-
beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Bacillus sp. N137
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
the enzyme hydrolyzes plant cell wall beta-glucans
-
-
?
additional information
?
-
-
the enzyme hydrolyzes plant cell wall beta-glucans
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
the enzyme hydrolyzes plant cell wall beta-glucans
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Bacillus subtilis NCIB 8565
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Niallia circulans ATCC 21367
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanase strictly cleaves the beta-1,4-D-glucosidic bonds adjacent to beta-1,3-linkages in mixed linked beta-glucans
-
-
?
additional information
?
-
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
the enzyme specifically catalyzes the hydrolysis of beta-1,4-glycosidic bonds located prior to beta-1,3-glycosidic linkages in 1,3-1,4-beta-glucan
-
-
?
additional information
?
-
the enzyme specifically catalyzes the hydrolysis of beta-1,4-glycosidic bonds located prior to beta-1,3-glycosidic linkages in 1,3-1,4-beta-glucan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Rasamsonia emersonii CBS 841.70
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Rhodothermus marinus ITI378
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
reported fungal eta-1,3-1,4-glucanases exhibit strict substrate specificity toward barley beta-glucan, oat beta-glucan and lichenan, of which the structures are all beta-(1,4)-linked glucose interrupted with beta-(1,3)-linkages. beta-1,3-1,4-Glucanases (lichenases) specifically hydrolyze the beta-1,4 glycosidic linkages adjacent to beta-1,3 bonds, yielding disaccharides, trisaccharides and tetrasaccharides as the major products. Enzyme TaGlu34 hydrolyzes barley beta-glucan and lichanan to produce mainly disaccharide and trisaccharide without formation of tetrasaccharide. Production of glucan oligosaccharides from oat bran by TaGlu34
-
-
?
additional information
?
-
Thermoascus aurantiacus CAU830
-
reported fungal eta-1,3-1,4-glucanases exhibit strict substrate specificity toward barley beta-glucan, oat beta-glucan and lichenan, of which the structures are all beta-(1,4)-linked glucose interrupted with beta-(1,3)-linkages. beta-1,3-1,4-Glucanases (lichenases) specifically hydrolyze the beta-1,4 glycosidic linkages adjacent to beta-1,3 bonds, yielding disaccharides, trisaccharides and tetrasaccharides as the major products. Enzyme TaGlu34 hydrolyzes barley beta-glucan and lichanan to produce mainly disaccharide and trisaccharide without formation of tetrasaccharide. Production of glucan oligosaccharides from oat bran by TaGlu34
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
Fe2+
K+
Mg2+
Mn2+
Na+
NaCl
Ni2+
Zn2+
additional information
Ca2+
-
enhances the isozyme EG1 and EG2 activities by 32.7% and 12%, respectively, at 2.5 mM. Ca2+ enhances the substrate binding affinity of the enzyme and stabilize the conformation of the catalytic site
Ca2+
three Ca2+ binding sites are found in the mutant W203F structure. The primary calcium is coordinated to seven atoms in a pentagonal-bipyramidal arrangement: three backbone carbonyl oxygen atoms (Asn164, Asn189 and Gly222), one Odelta2 atom of Asn164 and three water molecules. The primary calcium binding site present in the mutant W203F structure is similar to that for the wild-type
Ca2+
Ca2+ increases the activity and thermostability of BGlc8H with substrate lichenan
Cu2+
-
inhibits isozyme EG1 by 35%, but slightly activates isozyme EG2 at 2.5 mM
Mn2+
activates by 233%, best at 10 mM, slightly inhibitory at 20 mM
NaCl
1.5fold activation at 0.5 M, the enzyme is acid-, alkali- and salt-tolerant, the purified recombinant His-tagged enzyme retains over 90% activity in 4 M NaCl at 25°C for 24 h
additional information
-
Ca2+ stabilizes the enzyme at higher temperatures
additional information
-
no effects by 10 mM of Na+, K+, Ca2+, and Mg2+
additional information
-
poor effects on both isozymes by Mg2+ and EDTA at 2.5 mM
additional information
metal ions such as Mn2+, Na+, K+, Mg2+ and Zn2+ show little or no effect on the enzyme activity
additional information
metal ions are required for enzyme activity and also disulfide linkage may be involved in catalytic activity
additional information
the enzyme activity is not or poorly affected by EDTA, Tween-80, Triton X-100, H2O2, NaOCl, and diverse washing powders and soaps, overview
additional information
-
the enzyme activity is not or poorly affected by EDTA, Tween-80, Triton X-100, H2O2, NaOCl, and diverse washing powders and soaps, overview
additional information
not influenced by Na+, K+, Mg2+, or Zn2+
additional information
-
Ca2+, Cu2+, Ni2+, Ba2+, EDTA, and 2-mercaptoethanol show no obvious effect on the enzyme activity
additional information
the impact of metal ions Ca2+ and Mg2+ is more significant at higher temperatures
additional information
no or poor effects by NaCl, NH4Cl, NiCl2, ZnSO4 and EDTA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3,4)-epoxybutyl beta-D-cellobioside
-
identification of Glu105 at the active site
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
beta-mercaptoethanol
-
inhibits the enzyme activity at 4 mM by 82.7%
H2O2
-
at 0.5% w/v hydrogen peroxide, isozymes EG1 and EG2 retain 82.8% and 90.28% of their activities, respectively. At 1% w/v hydrogen peroxide, isozyme EG2 retains 60% activity, while isozyme EG1 is completely inhibited
Na+
-
inhibits the enzyme activity at 4 mM by 47.3%; inhibits the enzyme activity at 4 mM by 80.3%
NaCl
-
30%, halflife of wild-type 230 h, mutant K48A 694 h, mutant K48L 693 h, respectively
sodium perborate
-
isozymes EG1 and EG2 retain 58% and 66.8% of their activities after 1 h of incubation at 40°C in the presence of 0.2% w/v sodium perborate, respectively
Co2+
-
inhibits isozyme EG1 by 35%, and isozyme EG2 also slightly, at 2.5 mM
Cu2+
-
inhibits isozyme EG1 by 28%, but slightly activates isozyme EG2 at 2.5 mM
EDTA
5 or 10 mM of EDTA reduce barley beta-glucan hydrolysis by 39% and 34%, respectively
epoxyalkyl cellobiosides
-
irreversible active-site directed inactivation, stereospecific requirements for inhibition
-
epoxyalkyl cellobiosides
-
irreversible active-site directed inactivation, stereospecific requirements for inhibition
-
Mn2+
activates by 233% at 5 mM, best at 10 mM, slightly inhibitory at 20 mM
SDS
-
the strong anionic surfactant at 0.1% and 0.5% causes a moderate inhibition of 27.5% and 30.7% of isozyme EG2 activity. Isozyme EG1 is highly stable against SDS and retains 100% of its activity in the presence of 0.1% and 0.5% SDS
additional information
-
poor inhibition at 10 mM by Co2+ and EDTA
-
additional information
-
no significant effects are found for Ca2+, Mg2+, glycerol, D-sorbitol, boric acid, and EDTA
-
additional information
-
the isozymes are highly stable in the presence of non-ionic surfactants such as Tween 80 and Triton X-100
-
additional information
-
not inhibited by Li+; not inhibited by Li+, not significantly by Fe2+
-
additional information
-
no inhibition up to a concentration of 10% SDS-PAGE
-
additional information
-
substrate inhibition for 4-methylumbelliferyl laminaribiose, but not for 4-methylumbelliferyl cellobiose
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beet pulp
-
mutants show higher levels of activity compared to wild type
-
solk floc
-
mutants show higher levels of activity compared to wild type
-
wheat bran
-
mutants show higher levels of activity compared to wild type
-
additional information
-
in contrast to barley beta-glucanase, TFs beta-glucanase possesses a unique and compact active site which requires induced-fit substrate binding for enzymatic cleavage
-
additional information
Phe205, Gly207, and Asn208 in the type II turn of the connecting loop may play a role in the catalytic function of beta-glucanase
-
additional information
-
Phe205, Gly207, and Asn208 in the type II turn of the connecting loop may play a role in the catalytic function of beta-glucanase
-
additional information
-
the J18 strain produces the maximum level of extracellular beta-glucanase (135.6 U/ml) when grown in a medium containing corncob (5%, w/v) at 50°C for 4 days
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
0.7
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
1
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
0.5
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
0.6
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
0.34
beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35°C
0.15
beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35°C
5.3
Glcbeta3Glcbeta-methylumbelliferone
-
pH 7.0, 37°C, 50 mM sodium phosphate buffer
0.37
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
-
pH 6.9, 30°C
0.5
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
-
pH 7.2, 30°C
0.6
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
-
pH 7.8, 30°C
0.271
azo blue barley beta-glucan
-
mutant E46P/S43E/H205P/S40E, pH 6.5, 40°C
-
0.278
azo blue barley beta-glucan
-
mutant N31C/T187C/P102C/N125C, pH 6.5, 40°C
-
0.27
azo-barley glucan
mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P, pH 6.5, 40°C
-
0.2775
Barley beta-glucan
-
mutant N31C/T187C/P102C/N125C, at pH 6.5 and 40°C
additional information
barley beta-D-glucan
Km value of wild-type 13.5 mg/ml, mutant C17R/Q87T/D152G/Y307H/V330A/N344D 13.3 mg/ml, respectively, pH 5.0, 60°C
additional information
barley beta-D-glucan
Km value of wild-type 19.7 mg/ml, mutant C17R/Q87T/D152G/Y307H/V330A/N344D 16.3 mg/ml, respectively, pH 5.0, 40°C
additional information
Barley beta-glucan
-
4.36 mg/ml with substrate barley beta-glucan
additional information
Barley beta-glucan
-
wild-type, 2.1 mg/ml, mutant K48A 1.6 mg/ml, mutant K48L 1.4 mg/ml, respectively, pH 6.0, 50°C
additional information
Barley beta-glucan
Km value 2.23 mg/ml, pH 6.0, 55°C
additional information
Barley beta-glucan
-
Km value 2.23 mg/ml, pH 6.0, 55°C
additional information
Barley beta-glucan
-
Km value 7.42 mg/ml, pH 6.5, 60°C
additional information
Barley beta-glucan
Km value of wild-type 2.1 mg/ml, of mutant K48A 1.6 mg/ml, of mutant K48L 1.4 mg/ml, respectively, pH 6.0, 50°C
additional information
Barley beta-glucan
Km: 0.67 mg/ml, pH 6.6, 70°C
additional information
carboxymethylcellulose
Km-value: 2.71 g/l at 50°C, pH5.0
-
additional information
lichenan
Km value 1.82 mg/ml, pH 6.0, 55°C
additional information
lichenan
Km value 4 mg/ml for wild-type, 3.21 mg/ml for mutant K142N/Q203L/N214D
additional information
lichenin
Km value of wild-type 0.91 mg/ml, mutant T113S 0.69 mg/ml, mutant M44V/N53H 0.67 mg/ml, mutant N157D 0.70 mg/ml, respectively, pH 6.4, 40°C
additional information
additional information
-
wild-type and mutant enzymes
-
additional information
additional information
KM value for native enzyme, substrate beta-D-glucan, is 1.5 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1.2 mg/ml
-
additional information
additional information
-
KM value for native enzyme, substrate beta-D-glucan, is 1.5 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1.2 mg/ml
-
additional information
additional information
KM value for native enzyme, substrate beta-D-glucan, is 2.7 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1.2 mg/ml
-
additional information
additional information
-
KM value for native enzyme, substrate beta-D-glucan, is 2.7 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1.2 mg/ml
-
additional information
additional information
KM-value for wild-type, substrate lichenan, 2.88 mg/ml
-
additional information
additional information
-
KM-value for wild-type, substrate lichenan, 2.88 mg/ml
-
additional information
additional information
KM079629
0.45 mg/ml with lichenan at pH 6.0, 50°C
-
additional information
additional information
0.69 mg/ml with barley beta-glucan, 1.11 mg/ml with oat beta-glucan, and 0.63 with lichenan, pH 10.0, 55°C
-
additional information
additional information
-
0.69 mg/ml with barley beta-glucan, 1.11 mg/ml with oat beta-glucan, and 0.63 with lichenan, pH 10.0, 55°C
-
additional information
additional information
0.86 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
0.86 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
0.86 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
0.86 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
-
0.86 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
0.90 mg/ml barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
0.90 mg/ml barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
0.90 mg/ml barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
0.90 mg/ml barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
-
0.90 mg/ml barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
0.94 mg/ml with barley beta-glucan, at recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
0.94 mg/ml with barley beta-glucan, at recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
0.94 mg/ml with barley beta-glucan, at recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
0.94 mg/ml with barley beta-glucan, at recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
-
0.94 mg/ml with barley beta-glucan, at recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
1.19 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
1.19 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
1.19 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
1.19 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
-
1.19 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40°C
-
additional information
additional information
-
1.65 mg/ml with beta-1,3-1,4-glucan, at pH 6.0, 70°C
-
additional information
additional information
10.0 mg/ml with barley beta-glucan, pH 6.0, 40°C, recombinant enzyme
-
additional information
additional information
2.0 mg/ml with barley beta-glucan and 1.4 mg/ml with lichenan at pH 5.5, 60°C
-
additional information
additional information
-
2.1 mg/ml for isozyme EG1 and 1.8 mg/ml for isozyme EG2 with lichenan at pH 5.0, 50°C
-
additional information
additional information
2.25 mg/ml for wild-type enzyme, 2.44 mg/ml for mutant V18Y, 3.67 mg/ml for mutant W203Y, and 3.29 mg/ml for mutant V18Y/W203Y, with lichenan, pH 5.0, 50°C, calculated as reducing sugar released from substrate
-
additional information
additional information
-
3.69 mg/ml for the wild-type enzyme and 3.30 mg/ml for mutant D56G/D221G/C263S, with barley beta-glucan at pH 5.0, 70°C
-
additional information
additional information
3.7 mg/ml at pH 6.2, 55°C with barley beta-glucan, recombinant enzyme
-
additional information
additional information
-
5.3 mg/ml for mutant TFsW203F with lichenan, pH 6.0-7.0, 45°C. Kinetic properties of parental TFsW203F and mutant hybrid glucanases, overview
-
additional information
additional information
-
5.96 mg/ml with lichenan at pH 5.5, 50°C
-
additional information
additional information
-
7.9 mg/ml for recombinant wild-type enzyme, 7.2 mg/ml for recombinant optimally-modified enzyme, with AZO blue beta-glucan at pH 6.5, 40°C
-
additional information
additional information
-
Michaelis-Menten kinetics, 0.62 mg/ml with barley beta-glucan at pH 5.0, 60°C,and 0.38 mg/ml with lichenan at pH 5.0, 60°C
-
additional information
additional information
-
0.62 mg/ml with barley beta-glucan, pH 5.0, 60°C
-
additional information
additional information
-
0.67 mg/ml with barley beta-glucan, pH 4.0, 75°C
-
additional information
additional information
-
0.69 mg/ml with barley beta-glucan, 1.11 mg/ml with oat beta-glucan, and 0.63 mg/ml with lichenan, pH 5.0, 60°C
-
additional information
additional information
-
22.39 mg/ml with barley beta-glucan, pH 4.0-5.0, 50-60°C
-
additional information
additional information
-
5.957 mg/ml with lichenan, pH 3.0, 50-60°C
-
additional information
additional information
-
Km and Vmax values of the purified TaGlu34 for barley beta-D-glucan and oat beta-glucan are determined to be 2.09 mg/ml and 13.18 mmol/min/mg, and 1.36 mg/ml and 0.0165 mmol/min/mg, respectively
-
additional information
additional information
Km for carboxymethyl cellulose is 209.7 mg/ml and for barley beta-glucan 113.9 mg/ml in presence of 5 mM Mn2+
-
additional information
additional information
-
Km for carboxymethyl cellulose is 209.7 mg/ml and for barley beta-glucan 113.9 mg/ml in presence of 5 mM Mn2+
-
additional information
additional information
-
Km is 13.38 mg/ml and Vmax is 0.1429 mM/min/mg with lichenan, pH 4.8, 80°C
-
additional information
additional information
Km is 2.4 mg/ml and Vmax is 9.981 mmol/min/mg, with barley beta-glucan, pH 7.0, 70°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13.5
beta-1,3-1,4-glucan
-
pH 4.0, 75°C, substrate from Hordeum vulgare
0.91
beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35°C
1.35
beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35°C
43.32
carboxymethyl cellulose
pH 5.0, 55°C, recombinant enzyme
-
5.3
carboxymethylcellulose
-
pH 4.0, 75°C, substrate from Hordeum vulgare
-
2.25
1,3-1,4-beta-D-glucan
wild-type, expressed in Escherichia coli, pH 5.0, 50°C
-
2.44
1,3-1,4-beta-D-glucan
mutant V18Y, expressed in Escherichia coli, pH 5.0, 50°C
-
3.29
1,3-1,4-beta-D-glucan
mutant V18Y/W203Y, expressed in Escherichia coli, pH 5.0, 50°C
-
3.67
1,3-1,4-beta-D-glucan
mutant W203Y, expressed in Escherichia coli, pH 5.0, 50°C
-
186
azo blue barley beta-glucan
-
mutant N31C/T187C/P102C/N125C, pH 6.5, 40°C
-
187
azo blue barley beta-glucan
-
mutant E46P/S43E/H205P/S40E, pH 6.5, 40°C
-
109
AZO blue beta-glucan
-
recombinant wild-type enzyme, pH 6.5, 40°C
-
267
AZO blue beta-glucan
-
recombinant optimally-modified enzyme, pH 6.5, 40°C
-
189
azo-barley glucan
mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P, pH 6.5, 40°C
-
63.06
Barley beta-glucan
recombinant enzyme, pH 6.0, 40°C
68.19
Barley beta-glucan
recombinant enzyme, pH 6.0, 40°C
81.6
Barley beta-glucan
-
calculated as D-glucose units released from beta-glucan
83.89
Barley beta-glucan
recombinant enzyme, pH 6.0, 40°C
133.3
Barley beta-glucan
recombinant enzyme, pH 6.0, 40°C
143
Barley beta-glucan
-
pH 5.0, 70°C, mutant D56G/D221G/C263S
186.3
Barley beta-glucan
-
mutant N31C/T187C/P102C/N125C, at pH 6.5 and 40°C
710
Barley beta-glucan
mutant enzyme C17R/Q87T/D152G/Y307H/V330A/N344D, at pH 5.0 and 60°C
3628
Barley beta-glucan
mutant enzyme C17R/Q87T/D152G/Y307H/V330A/N344D, at pH 5.0 and 40°C
20.3
Beta-D-glucan
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, pH 6.0, 70°C
20.3
Beta-D-glucan
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, pH 6.0, 70°C
3.71
lichenan
-
calculated as D-glucose units released from lichenan
44
lichenan
mutant W203R, calculated as D-glucose units released from lichenan
109
lichenan
mutant Q70I, calculated as D-glucose units released from lichenan
131
lichenan
mutant F40I, 45°C, pH not specified in the publication
154
lichenan
mutant R137Q, 40°C, pH not specified in the publication
166.4
lichenan
-
calculated as D-glucose units released from lichenan
244
lichenan
mutant Q70A, calculated as D-glucose units released from lichenan
322
lichenan
mutant Y42L, 45°C, pH not specified in the publication
349
lichenan
mutant R137M, 40°C, pH not specified in the publication
371
lichenan
mutant Q70N, calculated as D-glucose units released from lichenan
401
lichenan
mutant L62G, 45°C, pH not specified in the publication
504
lichenan
mutant N72Q, calculated as D-glucose units released from lichenan
608
lichenan
mutant G207-, calculated as D-glucose units released from lichenan
639
lichenan
mutant Q70D, calculated as D-glucose units released from lichenan
641
lichenan
mutant Q70E, calculated as D-glucose units released from lichenan
699
lichenan
mutant D206R, calculated as D-glucose units released from lichenan
756
lichenan
mutant N139A, 45°C, pH not specified in the publication
785
lichenan
mutant E85I, calculated as D-glucose units released from lichenan
820
lichenan
mutant N72A, calculated as D-glucose units released from lichenan
865
lichenan
mutant F205L, calculated as D-glucose units released from lichenan
883
lichenan
mutant D202L, calculated as D-glucose units released from lichenan
911
lichenan
mutant K200M, calculated as D-glucose units released from lichenan
942
lichenan
mutant N208G, calculated as D-glucose units released from lichenan
992
lichenan
mutant E47I, 45°C, pH not specified in the publication
1037
lichenan
mutant R209M, calculated as D-glucose units released from lichenan
1141
lichenan
mutant K200F, calculated as D-glucose units released from lichenan
1277
lichenan
mutant T204F, calculated as D-glucose units released from lichenan
1296
lichenan
wild-type, calculated as D-glucose units released from lichenan
1353
lichenan
mutant G201S, calculated as D-glucose units released from lichenan
1422
lichenan
mutant E85D, calculated as D-glucose units released from lichenan
1435
lichenan
mutant Q70R, calculated as D-glucose units released from lichenan
1788
lichenan
mutant K64A, 50°C, pH not specified in the publication
1833
lichenan
mutant K64M, 50°C, pH not specified in the publication
1860
lichenan
mutant D206N, calculated as D-glucose units released from lichenan
1955
lichenan
mutant G207N, calculated as D-glucose units released from lichenan
2060
lichenan
mutant D206M, calculated as D-glucose units released from lichenan
2170
lichenan
mutant N44L, 55°C, pH not specified in the publication
2562
lichenan
mutant D202N, calculated as D-glucose units released from lichenan
2663
lichenan
mutant Q81N, calculated as D-glucose units released from lichenan
2924
lichenan
pH 5.0, 50°C, wild-type enzyme, calculated as reducing sugar released from substrate
3026
lichenan
mutant N44Q, 55°C, pH not specified in the publication
3224
lichenan
pH 5.0, 50°C, mutant V18Y, calculated as reducing sugar released from substrate
3641
lichenan
mutant Q81I, calculated as D-glucose units released from lichenan
3920
lichenan
truncated enzyme, calculated as D-glucose units released from lichenan
5003
lichenan
pH 5.0, 50°C, mutant W203Y, calculated as reducing sugar released from substrate
5090
lichenan
pH 5.0, 50°C, mutant V18Y/W203Y, calculated as reducing sugar released from substrate
5476
lichenan
mutant W203F, calculated as D-glucose units released from lichenan
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
672
azo blue barley beta-glucan
-
mutant N31C/T187C/P102C/N125C, pH 6.5, 40°C
-
691
azo blue barley beta-glucan
-
mutant E46P/S43E/H205P/S40E, pH 6.5, 40°C
-
691
azo-barley glucan
mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P, pH 6.5, 40°C
-
672.6
Barley beta-glucan
-
mutant N31C/T187C/P102C/N125C, at pH 6.5 and 40°C
additional information
Barley beta-glucan
kcat/Km value 2583 ml/mg/s, pH 6.0, 55°C
additional information
Barley beta-glucan
-
kcat/Km value 2583 ml/mg/s, pH 6.0, 55°C
additional information
Barley beta-glucan
kcat/Km value of wild-type 3.6 ml/mg/s, of mutant K48A 4.7 ml/mg/s, of mutant K48L 5.2 ml/mg/s, respectively, pH 6.0, 50°C
additional information
lichenan
kcat/Km value 1436 ml/mg/s, pH 6.0, 55°C
additional information
additional information
Kcat/KM value for native enzyme, substrate beta-D-glucan, is 369 mg/ml/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1014 mg/ml/min
-
additional information
additional information
-
Kcat/KM value for native enzyme, substrate beta-D-glucan, is 369 mg/ml/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1014 mg/ml/min
-
additional information
additional information
kcat/KM value for native enzyme, substrate beta-D-glucan, is 51 ml/mg/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1014 ml/mg/min
-
additional information
additional information
-
kcat/KM value for native enzyme, substrate beta-D-glucan, is 51 ml/mg/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1014 ml/mg/min
-
additional information
additional information
kcat/KM-value for wild-type, substrate lichenan, 1358 ml/mg/s
-
additional information
additional information
-
kcat/KM-value for wild-type, substrate lichenan, 1358 ml/mg/s
-
additional information
additional information
Km for carboxymethyl cellulose is 0.207 mg/ml/s and for barley beta-glucan 1.404 mg/ml/s in presence of 5 mM Mn2+
-
additional information
additional information
-
Km for carboxymethyl cellulose is 0.207 mg/ml/s and for barley beta-glucan 1.404 mg/ml/s in presence of 5 mM Mn2+
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.5
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
0.9
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
6
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
2.5
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
1.4
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
20.7
Ca2+
mutant W203F, pH 6.0, temperature not specified in the publication
23.9
Ca2+
wild-type, pH 6.0, temperature not specified in the publication
98.7
imidazole
wild-type, pH 6.0, temperature not specified in the publication
117
imidazole
mutant W203F, pH 6.0, temperature not specified in the publication
100.7
Tris
mutant W203F, pH 6.0, temperature not specified in the publication
255.4
Tris
wild-type, pH 6.0, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.4
10800
-
expressed in Pichia pastoris X-33, sodium citrate buffer, pH 6.0, 50°C, 10 min
12502
-
purified native enzyme, pH 6.0, 65°C, substrate oat beta-glucan
1280
-
recombinant enzyme, using barley beta-glucan as a substrate, at 50°C and pH 6.0
1335
-
recombinant enzyme, using lichenan as a substrate, at 50°C and pH 6.0
13527
-
purified native enzyme, pH 6.0, 65°C, substrate barley beta-glucan
15 - 25
mutant N139A, 45°C, pH not specified in the publication
1746
18.89
Thermomonospora sp.
-
enzyme from culture filtrate, using xylan as a substrate, at 50°C, pH 7.0
2.7
-
purified recombinant linear enzyme and wild-type enzyme, substrate barley-beta-glucan, pH and temperature not specified in the publication
2065
23
purified enzyme without addition of agents and metal ions, with lichenan as the substrate, pH 10.0, 55°C
24
purified recombinant His-tagged enzyme, substrate barley beta-glucan, pH 6.0, 30°C
2434
2479
-
recombinant enzyme after 8.74fold purification, using barley beta-glucan as a substrate
2490
25
Thermomonospora sp.
-
enzyme from culture filtrate, using lichenan as a substrate, at 50°C, pH 7.0
26530
purified recombinant enzyme, pH 6.0, 40°C, substrate barley beta-glucan
2717
-
recombinant wild-type enzyme, pH 6.5, 40°C, substrate AZO blue beta-glucan
283.8
-
recombinant enzyme from crude extract, using barley beta-glucan as a substrate
28820 - 33480
purified native enzyme, substrate barley beta-glucan, pH 5.5, 60°C
29
32100
purified recombinant enzyme, pH 6.0, 40°C, substrate barley beta-glucan
3370
-
recombinant optimally-modified enzyme, pH 6.5, 40°C, substrate AZO blue beta-glucan
3722
39520
purified recombinant enzyme, pH 6.0, 40°C, substrate barley beta-glucan
41210
purified recombinant enzyme, pH 6.0, 40°C, substrate barley beta-glucan
4274
mutant K20S/N31C/CS40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P, pH 6.5, 40°C
43 - 46
mutant N44L, 55°C, pH not specified in the publication
43.2
purified enzyme without addition of agents and metal ions, with oat beta-D-glucan as the substrate, pH 10.0, 55°C
52.7
purified enzyme without addition of agents and metal ions, with barley beta-D-glucan as the substrate, pH 10.0, 55°C
598.6
Thermomonospora sp.
-
after 31.6fold purification, using xylan as a substrate, at 50°C, pH 7.0
60 - 61
mutant N44Q, 55°C, pH not specified in the publication
6520
mutant V18Y, expressed in Escherichia coli, pH 5.0, 50°C
70
7055
purified recombinant His-tagged enzyme, substrate barley beta-glucan, pH 6.2, 55°C
7500
purified recombinant enzyme, substrate barley beta-glucan, pH 6.0, 40°C
77.7
purified enzyme with addition of Co2+, with barley beta-D-glucan as the substrate, pH 10.0, 55°C
792.2
Thermomonospora sp.
-
after 31.6fold purification, using lichenan as a substrate, at 50°C, pH 7.0
7980
-
expressed in Escherichia coli, sodium citrate buffer, pH 6.0, 50°C, 10 min
85.3
purified recombinant enzyme, pH 6.5, 60°C, substrate barley beta-glucan
8726
9263
mutant W203Y, expressed in Escherichia coli, pH 5.0, 50°C
9967
mutant V18Y/W203Y, expressed in Escherichia coli, pH 5.0, 50°C
additional information
10.4
-
hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
10.4
-
hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
1746
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate lichenan, pH 6.0, 70°C
1746
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate lichenan, pH 6.0, 70°C
2434
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, pH 6.0, 70°C
2434
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, pH 6.0, 70°C
29
-
purified native enzyme, substrate is Hordeum vulgare beta-1,3-1,4-glucan
3722
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase
3722
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase
additional information
-
2.2 U/ml, pH 5.0, 60°C, substrate barley beta-glucan
additional information
-
100.3 U/ml, substrate barley beta-glucan, pH 5.0, 60°C
additional information
135.6 U/ml, substrate barley beta-glucan, pH 7.0, 70°C
additional information
-
45.0 U/ml, pH 3.0, 50-60°C, substrate lichenan
additional information
-
1.5 U/ml, pH and temperature not specified in the publication, substrate barley beta-glucan
additional information
-
20.3 U/ml, pH 4.8, 80°C, substrate barley beta-glucan
additional information
-
6230 U/ml, pH and temperature not specified in the publication
additional information
6230 U/ml, pH and temperature not specified in the publication
additional information
-
8.5 U/ml, pH 4.0-5.0, 50-60°C, substrate barley beta-glucan
additional information
-
9023.62 U/gds, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.5
three activity peaks at pH 1.5, 3.5, and 5.0. At pH 1.5, 61% of the activity at pH 5.0
10
3.5
three activity peaks at pH 1.5, 3.5, and 5.0. At pH 3.5, 91% of the activity at pH 5.0
4 - 5
4.5
5.5
5.6
5.6 - 6.6
6 - 7
6 - 8
6.4
6.5
6.6
7 - 8
7.6
8 - 9
8.5
additional information
-
amino acid residues at positions 56 and 263 are important in determining optimal pH activity
5
three activity peaks at pH 1.5, 3.5, and 5.0. Maximum activity at pH 5.0
5.6 - 6.6
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase
6
recombinant mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme, substrate lichenan
7 - 8
-
hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
7 - 8
-
hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
3 - 11
over 50% of maximal activity within this range, profile overview
3 - 5.5
-
79% and 73% of the maximum activity, respectively, at pH 3.5 and pH 4.5
3 - 6
3 - 6.5
3.5 - 10
recombinant His-tagged enzyme, activity range, profile, overview
4 - 10
-
isozyme EG1, more than 80% of maximal activity within pH range pH 4.0-7.0, 50% at pH 10.0. Isozyme Eg2 shows over 70% of maximal activity at pH 4.0-10.0
4 - 11
4 - 8
4.5 - 8
6 - 10
6 - 11
-
pH 6.0: about 55% of maximal activity, pH 11.0: about 45% of maximal activity
6 - 7
-
wild-type enzyme and mutant enzymes W101F, W101Y, E103D, D105N and E107D
6 - 8
maximal activity at pH 6.0, 95% activity at pH 7.0, and 66% activity at pH 8.0
3 - 10
-
activity range, wild-type and mutant enzymes, profile overview
3 - 6
-
pH 3.0: about 50% of maximal activity, pH 6.0: about 40% of maximal activity
3 - 6.5
activity range, over 50% of maximal activity at pH 4.0-5.5, profile overview
4 - 8
-
over 50% of maximal activity within this range, profile overview
4.5 - 8
-
activity range, wild-type and optimally-modified enzymes, overview
4.5 - 8
activity range, over 80% activity within the range of pH 5.0-7.5, recombinant enzyme
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
40
45
50
50 - 55
50 - 60
55
60
65
65 - 70
70
75
80
50
recombinant mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme, substrate lichenan
70
mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 90
over 50% of maximal activity within this range, profile overview. The enzyme shows 75, 88, 90 and 80% activity at 20, 40, 60 and 80°C, respectively
20 - 70
30 - 60
-
30°C, about 30% of maximal activity with oat beta-D-glucan, about 45% of maximal activity with lichenin, 60°C: about 20% of maximal activity with lichenin and oat beta-D-glucan as substrate
30 - 70
30 - 80
35 - 65
-
activity range, wild-type and optimally-modified enzymes, overview
35 - 70
mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P, more than 80% of maximum activity
37 - 65
40 - 60
40 - 65
40 - 80
40 - 90
-
activity range, wild-type and mutant enzymes, profile overview
45 - 65
-
45°C: about 80% of maximal activity, 65°C: about 90% of maximal activity
45 - 85
-
over 50% of maximal activity within this range, profile overview
45 - 90
-
at temperatures of 60°C and 85°C, the enzyme activity is 85% and 80% of maximal activity, respectively
5 - 40
the enzyme shows 88% and 77% of maximal activity at 20°C and 40°C, and 63% and 38% of maximal activity at 10°C and at 5°C
55 - 90
-
55°C: about 50% of maximal activity, 90°C: about 30% of maximal activity
20 - 70
-
the remaining activity decreased to 20% at 20-40°C and is completely destroyed at 50-70°C
30 - 70
recombinant His-tagged enzyme, activity range, profile, overview
30 - 80
40% of maximal activity at 30°C, 80% at 45°C and 60°C, about 35% at 70°C, and 20% at 80°C, profile overview
40 - 60
-
40°C: about 60% of maximal activity, 60°C: about 20% of maximal activity
40 - 60
-
about 50% activity at 40°C, about 65% activity at 45°C, about 80% activity at 50°C, 100% activity at 55°C, about 75% activity at 60°C, about 15% activity at 65°C
40 - 65
-
40°C: about 60% of maximal activity, 65°C: about 50% of maximal activity
40 - 65
-
40°C: about 80% of maximal activity, 65°C: about 60% of maximal activity
40 - 80
-
40°C: about 40% of maximal activity, 80°C: about 30% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Ruminiclostridium thermocellum
UniProt
brenda
Acetivibrio thermocellus DSM 1237
Bacillus amyloliquefaciens BLB369
i.e. Bacillus velezensis, isolated from rhizosphere soil sample
UniProt
brenda
i.e. Bacillus amyloliquefaciens subsp. plantarum or Bacillus velezensis
UniProt
brenda
uncultured bacterium from Chinese Nong-flavor daqu
UniProt
brenda
i.e. Bacillus velezensis, isolated from rhizosphere soil sample
UniProt
brenda
parental enzymes and hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase
-
-
brenda
parental enzymes, hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
-
-
brenda
hybrid from B. macerans and B. amyloliquefaciens
-
-
brenda
-
-
-
brenda
isolated from Asian giant hornet, Vespa mandarinia, nest, gene bgl5-1
UniProt
brenda
sequence of mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
UniProt
brenda
isolated from Asian giant hornet, Vespa mandarinia, nest, gene bgl5-1
UniProt
brenda
i.e. Bacillus amyloliquefaciens subsp. plantarum or Bacillus velezensis
UniProt
brenda
BglA13; isolated from the feces of water buffalo, gene bglA13
UniProt
brenda
BglA16; isolated from the feces of water buffalo, gene bglA16
UniProt
brenda
BglA51; isolated from the feces of water buffalo, gene bglA51
UniProt
brenda
BglM2; isolated from the feces of water buffalo, gene bglM2
UniProt
brenda
BglA13; isolated from the feces of water buffalo, gene bglA13
UniProt
brenda
BglA16; isolated from the feces of water buffalo, gene bglA16
UniProt
brenda
BglA51; isolated from the feces of water buffalo, gene bglA51
UniProt
brenda
BglM2; isolated from the feces of water buffalo, gene bglM2
UniProt
brenda
parental enzymes and hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase
-
-
brenda
parental enzymes, hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
-
-
brenda
wild-type and mutant enzymes W101F, W101Y, E103D, E103Q, D105N, D105K, E107D, E107Q, and E107H
-
-
brenda
RuCelA, a bifunctional xylanase/endoglucanase, EC 3.2.1.8 and EC 3.2.1.73; isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isoenzyme II is synthesized exclusively in the aleurone layer, isoenzyme III is detected in scutellum and aleurone layer
brenda
gene OsEGL1 is expressed in seedling, and young and adult plant roots
brenda
-
isoenzyme I is synthesized predominantly in the scutellum, isoenzyme III is detected in scutellum and aleurone layer
brenda
additional information
-
enzyme level increases with leaf development and decreases with leaf aging, depletion of sugars results in increase of enzyme protein and activity, elevated carbohydrate contents causes a rapid decrease in enzyme abundance
brenda
-
second leaf, enzyme protein increases upon incubation in the dark and disappears upon illumination or feeding with sucrose
brenda
-
submerged culture, optimization of enzyme production, under optimized conditions viz. 5% w/v corncob as carbon source, 1% w/v peptone as nitrogen source, initial pH of 5.0, 1% w/v of Tween 40, cultivation temperature of 50°C, and incubation time of 7 d, the highest beta-1,3-1,4-glucanase activity of 3741 U/ml is obtained
brenda
Thermoascus aurantiacus CAU830
-
submerged culture, optimization of enzyme production, under optimized conditions viz. 5% w/v corncob as carbon source, 1% w/v peptone as nitrogen source, initial pH of 5.0, 1% w/v of Tween 40, cultivation temperature of 50°C, and incubation time of 7 d, the highest beta-1,3-1,4-glucanase activity of 3741 U/ml is obtained
-
brenda
-
transfer from antural light/dark cycle into darkness induces eisozyme EI
brenda
additional information
-
optimization of production of beta-glucanase with barley flour as the sole carbon source
brenda
additional information
-
optimization of production of beta-glucanase with barley flour as the sole carbon source
-
brenda
additional information
-
the optimum temperature for the fungal growth is 28°C, the fungus does not grow above 42°C
brenda
additional information
-
submerged fermentation with 2.5% corncob
brenda
additional information
submerged fermentation with 5% corncob
brenda
additional information
-
strain Pol6 produces high level of extracellular lichenase when grown in a medium containing oat flour (2%, w/v) at 30°C for 7 days. Highest lichenases activity is obtained on the cellulose (50 U/ml) and oat flour (45 U/ml) as a carbon sources
brenda
additional information
-
strain Pol6 produces high level of extracellular lichenase when grown in a medium containing oat flour (2%, w/v) at 30°C for 7 days. Highest lichenases activity is obtained on the cellulose (50 U/ml) and oat flour (45 U/ml) as a carbon sources
-
brenda
additional information
-
submerged fermentation with 2% wheat bran/beet pulp (ratio 1:1)
brenda
additional information
Rasamsonia emersonii CBS 841.70
-
submerged fermentation with 2% wheat bran/beet pulp (ratio 1:1)
-
brenda
additional information
high-level extracellular enzyme production of 6230 U/mL on oat flour at 3% w/v as a carbon source at 50 °C
brenda
additional information
submerged fermentation with 3% oat flour
brenda
additional information
-
high-level extracellular enzyme production of 6230 U/mL on oat flour at 3% w/v as a carbon source at 50 °C
-
brenda
additional information
-
submerged fermentation with 0.5% chitin
brenda
additional information
isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
N-terminal signal peptide at residues 1-20 (MDSKRGVVAAVLALLPLVSA), enzyme Af-EGL7 is secreted
-
brenda
-
N-terminal signal peptide at residues 1-20 (MDSKRGVVAAVLALLPLVSA), enzyme Af-EGL7 is secreted
-
-
brenda
-
N-terminal signal peptide at residues 1-20 (MDSKRGVVAAVLALLPLVSA), enzyme Af-EGL7 is secreted
-
-
brenda
Aspergillus fumigatus CBS 101355
-
N-terminal signal peptide at residues 1-20 (MDSKRGVVAAVLALLPLVSA), enzyme Af-EGL7 is secreted
-
-
brenda
Aspergillus fumigatus FGSC A1100
-
N-terminal signal peptide at residues 1-20 (MDSKRGVVAAVLALLPLVSA), enzyme Af-EGL7 is secreted
-
-
brenda
enzyme NFEg16A has a signal peptide
-
brenda
additional information
-
the wild-type enzyme contains a signal peptide
-
brenda
additional information
KM079629
the enzyme contains a signal peptide
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
beta-1,3-1,4-glucanases from various microorganisms and plants belong to glycoside hydrolase families 16 and 17, respectively
evolution
the beta-1,3-1,4-glucanases are family-16 glycosyl hydrolases that hydrolyze 1,4-beta-D-glycosidic linkages in beta-D-glucans containing mixed 1,3 and 1,4 linkages, which are abundant polysaccharide components found in the cell walls of grasses and the endosperm of cereals
evolution
the enzyme belongs to the glycohydrolase family GH16
evolution
KM079629
the enzyme belongs to the glycosyl hydrolase family 8 containing the amino acid sequence ATDGDLDIAYALLLASLQW
evolution
the enzyme is a member of the glycosylhydrolase faamily GH16
evolution
the enzyme is a member of the glycosylhydrolase family GH16 containing the conserved motif EIDIEF and signal peptide
evolution
the presence of expansion and several predicted secondary structures in the 3' untranslated regions of genes bglA16 and bglM2 suggest that these two genes were duplicated recently, whereas genes bglA13 and bglA16, which contain very short 3'UTRs, were replicated earlier. The activities and some characteristics of enzymes have changed during the horizontal gene transfer event. Duplicated beta-glucanase genes bglA16 and bglM2 increase the reaction efficiency of beta-glucanases and suggest that the catalytic efficiency of beta-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms in Neocallimastix patriciarum J11
evolution
the enzyme belongs to the GH16 endo-beta-1,3-1,4-glucanases family
evolution
the enzyme belongs to the glycosyl hydrolase family 7, GH7
evolution
the enzyme belongs to the theme C glycoside hydrolase family 9, GH9. Theme C glucanases exhibit an N-terminal Ig domain
evolution
Acetivibrio thermocellus DSM 1237
-
beta-1,3-1,4-glucanases from various microorganisms and plants belong to glycoside hydrolase families 16 and 17, respectively
-
evolution
-
the beta-1,3-1,4-glucanases are family-16 glycosyl hydrolases that hydrolyze 1,4-beta-D-glycosidic linkages in beta-D-glucans containing mixed 1,3 and 1,4 linkages, which are abundant polysaccharide components found in the cell walls of grasses and the endosperm of cereals
-
evolution
Bacillus amyloliquefaciens BLB369
-
the enzyme belongs to the GH16 endo-beta-1,3-1,4-glucanases family
-
evolution
-
the enzyme is a member of the glycosylhydrolase family GH16 containing the conserved motif EIDIEF and signal peptide
-
evolution
Aspergillus fumigatus CBS 101355
-
the enzyme belongs to the glycosyl hydrolase family 7, GH7
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 7, GH7
-
evolution
-
the enzyme belongs to the glycohydrolase family GH16
-
evolution
Aspergillus fumigatus FGSC A1100
-
the enzyme belongs to the glycosyl hydrolase family 7, GH7
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 7, GH7
-
evolution
-
the presence of expansion and several predicted secondary structures in the 3' untranslated regions of genes bglA16 and bglM2 suggest that these two genes were duplicated recently, whereas genes bglA13 and bglA16, which contain very short 3'UTRs, were replicated earlier. The activities and some characteristics of enzymes have changed during the horizontal gene transfer event. Duplicated beta-glucanase genes bglA16 and bglM2 increase the reaction efficiency of beta-glucanases and suggest that the catalytic efficiency of beta-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms in Neocallimastix patriciarum J11
-
physiological function
-
fibrolytic enzyme which plays an important role in the hydrolysis of polysaccharide components. It is responsible for precisely hydrolyzing beta-1,4-glycosidic bonds adjacent to the beta-1,3-linkages in lichenan or mixed-linked beta-D-glucans, yielding mainly cellotriose, cellotetraose and cellopentaose
physiological function
overexpression of barley (1->3,1->4)-beta-glucanase isoenzyme EII under the control of a promoter of barley D-Hordein gene Hor3-1 in barley cultivar Golden Promise. The T2 generation of transgenic lines shows increased activity of glucanase in grains. Total beta-glucan content is reduced by more than 95.73% in transgenic grains compared with the wild-type control. Overexpression leads to an increase in 1000-grain weight, which might be due to elevated amounts of starch in the grain
physiological function
Streptomyces lydicus A01 expressing the enzyme shows substantially high glucanase activity, and has similar natamycin production and chitinase activity as the wild-type strain A01. Compared to the wild-type strain A01, the antifungal effects of Streptomyces lydicus AG01 on Botrytis cinerea, including inhibition of spore germination and mycelial growth, are highly improved. This is likely attributed to the heterologous expression of glucanase, which acts synergistically with natamycin and chitinase to increase the antifungal activity of the strain
physiological function
endo-beta-1,3-1,4-glucanases are glycoside hydrolases involved in the enzymatic depolymerization of 1,3-1,4-beta-glucans and show antifungal activity against some fungi. Bacillus amyloliquefaciens BLB369 has a high antagonistic activity against phytopathogenic fungi. The purified recombinant enzyme has the ability to inhibit the growth of the phytopathogenic fungus Alternaria alternata
physiological function
the enzyme protects plants against pathogenic fungi
physiological function
Bacillus amyloliquefaciens BLB369
-
endo-beta-1,3-1,4-glucanases are glycoside hydrolases involved in the enzymatic depolymerization of 1,3-1,4-beta-glucans and show antifungal activity against some fungi. Bacillus amyloliquefaciens BLB369 has a high antagonistic activity against phytopathogenic fungi. The purified recombinant enzyme has the ability to inhibit the growth of the phytopathogenic fungus Alternaria alternata
-
physiological function
-
the enzyme protects plants against pathogenic fungi
-
physiological function
-
Streptomyces lydicus A01 expressing the enzyme shows substantially high glucanase activity, and has similar natamycin production and chitinase activity as the wild-type strain A01. Compared to the wild-type strain A01, the antifungal effects of Streptomyces lydicus AG01 on Botrytis cinerea, including inhibition of spore germination and mycelial growth, are highly improved. This is likely attributed to the heterologous expression of glucanase, which acts synergistically with natamycin and chitinase to increase the antifungal activity of the strain
-
additional information
-
both the loss of the signal peptide (29 amino acids) and the addition of the His-tag to the peptide backbone do not affect the specific activity of linear enzyme
additional information
-
Glu56, Asp58 and Glu60 residues located in the active site cavity of the enzyme play key roles in enzyme catalysis, functioning as general acid-base residues, structure and functional relationships of Fsbeta-glucanase
additional information
-
in silico analysis and structure homology modelling of the enzyme's catalytic domain, LicBM3, secondary structure
additional information
involvement of Glu269 in the catalytic machinery of the enzyme
additional information
-
molecular structure modeling and analysis
additional information
-
N-terminal amino acid sequences of isozymes EG1 and EG2 are GAAPIKKGTTKLN and DINGGGATLPQK, respectively
additional information
-
the enzyme adopts a typical beta-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. Both catalytic residues E113 and E118 are embedded in the strand beta9. The ligand binding cleft is formed by the inner beta-sheets, four associated loops and one alpha-helix, which connect the strands beta2 to beta3 (residues 20-29), beta8 to beta9 (105-112), beta11 to beta12 (150164) and beta16 to alpha6 (250-260). The outer beta-sheets did not involve in the active site formation but might play a structural role in overall folding. Existence of a detailed interaction network in the active site and the intermediate-like configuration, overview
additional information
the enzyme adopts a typical beta-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. Both catalytic residues E113 and E118 are embedded in the strand beta9. The ligand binding cleft is formed by the inner beta-sheets, four associated loops and one alpha-helix, which connect the strands beta2 to beta3 (residues 20-29), beta8 to beta9 (105-112), beta11 to beta12 (150164) and beta16 to alpha6 (250-260). The outer beta-sheets did not involve in the active site formation but might play a structural role in overall folding. Existence of a detailed interaction network in the active site and the intermediate-like configuration, overview
additional information
the enzyme amino acid sequence shares a conserved motif EIDIEF. The predicted three-dimensional homology model of the enzyme shows the presence of catalytic residues Glu105, Glu109, and Asp107, single disulfide bridge between Cys32 and Cys61 and three calcium binding site residues Pro9, Gly45 and Asp207. Molecular modelling and molecular dynamics simulation studies reveal that the absence of calcium ion fluctuate the active site residues which are responsible for thermostability. Molecular three-dimensional model of the enzyme with bound Ca2+, overview
additional information
the two glutamic acids in the EIDIEF motif are key residues involved in the hydrolytic activity
additional information
-
the two glutamic acids in the EIDIEF motif are key residues involved in the hydrolytic activity
additional information
residues 424-460 from the carbohydrate-binding domain, CBM1 domain
additional information
-
residues 424-460 from the carbohydrate-binding domain, CBM1 domain
additional information
the enzyme has an endo-1,3-1,4-beta-glucanase domain
additional information
the putative catalytic residues are Asp147, Asp150 and Glu517
additional information
-
the two glutamic acids in the EIDIEF motif are key residues involved in the hydrolytic activity
-
additional information
Aspergillus fumigatus CBS 101355
-
residues 424-460 from the carbohydrate-binding domain, CBM1 domain
-
additional information
-
residues 424-460 from the carbohydrate-binding domain, CBM1 domain
-
additional information
-
the enzyme adopts a typical beta-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. Both catalytic residues E113 and E118 are embedded in the strand beta9. The ligand binding cleft is formed by the inner beta-sheets, four associated loops and one alpha-helix, which connect the strands beta2 to beta3 (residues 20-29), beta8 to beta9 (105-112), beta11 to beta12 (150164) and beta16 to alpha6 (250-260). The outer beta-sheets did not involve in the active site formation but might play a structural role in overall folding. Existence of a detailed interaction network in the active site and the intermediate-like configuration, overview
-
additional information
-
involvement of Glu269 in the catalytic machinery of the enzyme
-
additional information
-
the enzyme amino acid sequence shares a conserved motif EIDIEF. The predicted three-dimensional homology model of the enzyme shows the presence of catalytic residues Glu105, Glu109, and Asp107, single disulfide bridge between Cys32 and Cys61 and three calcium binding site residues Pro9, Gly45 and Asp207. Molecular modelling and molecular dynamics simulation studies reveal that the absence of calcium ion fluctuate the active site residues which are responsible for thermostability. Molecular three-dimensional model of the enzyme with bound Ca2+, overview
-
additional information
-
N-terminal amino acid sequences of isozymes EG1 and EG2 are GAAPIKKGTTKLN and DINGGGATLPQK, respectively
-
additional information
Aspergillus fumigatus FGSC A1100
-
residues 424-460 from the carbohydrate-binding domain, CBM1 domain
-
additional information
-
residues 424-460 from the carbohydrate-binding domain, CBM1 domain
-
Show AA Sequence and Transmembrane Helices (1345 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
-
discrepancy between molecular weight determined by gel filtration and low speed equilibrium sedimentation is probably due to a moderate interaction between the enzyme and the Sephadex polmer, gel filtration
239000
x * 239000, about, sequence calculation, x * 25000, recombinant His-tagged enzyme, SDS-PAGE
24000
25000
26000
26900
x * 26900, about, sequence calculation, x * 24000, recombinant enzyme, SDS-PAGE
27000
27470
x * 27470, sequence calculation. x * 45000, recombinant tagged enzyme, SDS-PAGE
28000
29000
30000
31000
41694
KM079629
x * 45133, sequence calculation, x * 41694, recombinant enzyme without signal peptide, SDS-PAGE
45000
x * 27470, sequence calculation. x * 45000, recombinant tagged enzyme, SDS-PAGE
45133
KM079629
x * 45133, sequence calculation, x * 41694, recombinant enzyme without signal peptide, SDS-PAGE
45170
x * 45170, calculated, x * 60000-80000, SDS-PAGE of recombinant enzyme, x * 48000, SDS-PAGE after Endo H treatment
48000
x * 45170, calculated, x * 60000-80000, SDS-PAGE of recombinant enzyme, x * 48000, SDS-PAGE after Endo H treatment
50000
-
1 * 30000, isozyme EG1, SDS-PAGE, 1 * 50000, isozyme EG2, SDS-PAGE
55000
90000
-
SDS-PAGE, J2 is composed of three protein subunits of 40, 32 and 18 kDa
96000
x * 28000, recombinant enzyme, SDS-PAGE, x * 96000, recombinant CotA-BglS chimeric mutant enzyme, SDS-PAGE
24000
x * 26900, about, sequence calculation, x * 24000, recombinant enzyme, SDS-PAGE
25000
x * 239000, about, sequence calculation, x * 25000, recombinant His-tagged enzyme, SDS-PAGE
27000
-
discrepancy between molecular weight determined by gel filtration and low speed equilibrium sedimentation is probably due to a moderate interaction between the enzyme and the Sephadex polmer, low speed sedimentation without reaching equilibrium
27000
-
1 * 27000, recombinant mature circular enzyme variant LicA-C1 without intein sequences, SDS-PAGE
28000
-
recombinant enzyme with a six-His tag at the N terminus, SDS-PAGE
28000
x * 28000, about, recombinant catalytic domain, SDS-PAGE
28000
x * 28000, recombinant enzyme, SDS-PAGE, x * 96000, recombinant CotA-BglS chimeric mutant enzyme, SDS-PAGE
30000
-
1 * 30000, isozyme EG1, SDS-PAGE, 1 * 50000, isozyme EG2, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 52000, recombinant enzyme, SDS-PAGE, x * 48000, about, sequence calculation
?
-
x * 52000, recombinant enzyme, SDS-PAGE, x * 48000, about, sequence calculation
-
?
-
x * 52000, recombinant enzyme, SDS-PAGE, x * 48000, about, sequence calculation
-
?
Aspergillus fumigatus CBS 101355
-
x * 52000, recombinant enzyme, SDS-PAGE, x * 48000, about, sequence calculation
-
?
Aspergillus fumigatus FGSC A1100
-
x * 52000, recombinant enzyme, SDS-PAGE, x * 48000, about, sequence calculation
-
?
x * 27470, sequence calculation. x * 45000, recombinant tagged enzyme, SDS-PAGE
?
-
x * 27470, sequence calculation. x * 45000, recombinant tagged enzyme, SDS-PAGE
-
?
x * 27300, calculated, x * 30500 and x * 32500, SDS-PAGE of recombinant protein
?
x * 27300, about, sequence calculation, x * 30300, recombinant His6-tagged enzyme, x * 32500, recombinant OmpA-His6-tagged enzyme
?
Bacillus amyloliquefaciens BLB369
-
x * 27300, about, sequence calculation, x * 30300, recombinant His6-tagged enzyme, x * 32500, recombinant OmpA-His6-tagged enzyme
-
?
x * 28000, recombinant enzyme, SDS-PAGE, x * 96000, recombinant CotA-BglS chimeric mutant enzyme, SDS-PAGE
?
-
x * 28000, recombinant enzyme, SDS-PAGE, x * 96000, recombinant CotA-BglS chimeric mutant enzyme, SDS-PAGE
-
?
x * 26900, about, sequence calculation, x * 24000, recombinant enzyme, SDS-PAGE
?
-
x * 26900, about, sequence calculation, x * 24000, recombinant enzyme, SDS-PAGE
-
?
x * 45170, calculated, x * 60000-80000, SDS-PAGE of recombinant enzyme, x * 48000, SDS-PAGE after Endo H treatment
?
x * 239000, about, sequence calculation, x * 25000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 239000, about, sequence calculation, x * 25000, recombinant His-tagged enzyme, SDS-PAGE
-
?
KM079629
x * 45133, sequence calculation, x * 41694, recombinant enzyme without signal peptide, SDS-PAGE
monomer
-
1 * 27000, recombinant mature circular enzyme variant LicA-C1 without intein sequences, SDS-PAGE
monomer
-
1 * 30000, isozyme EG1, SDS-PAGE, 1 * 50000, isozyme EG2, SDS-PAGE
monomer
-
1 * 30000, isozyme EG1, SDS-PAGE, 1 * 50000, isozyme EG2, SDS-PAGE
-
additional information
-
the Thr-Pro box has a positive effect while the dockerin domain has a negative impact on the properties of LicMB. The N-terminal residues 10-25 and C-terminal residues 1-9 of LicMB-CD are necessary to retain high thermostability, while the N-terminal residues 1-7 and C-terminal residues 1-3 are not necessary to maintain enzymatic activity
additional information
-
the Thr-Pro box has a positive effect while the dockerin domain has a negative impact on the properties of LicMB. The N-terminal residues 10-25 and C-terminal residues 1-9 of LicMB-CD are necessary to retain high thermostability, while the N-terminal residues 1-7 and C-terminal residues 1-3 are not necessary to maintain enzymatic activity
-
additional information
-
four protein bands of approximately 40, 32, 25 and 18 kDa are resolved from pJ2
additional information
-
four protein bands of approximately 40, 32, 25 and 18 kDa are resolved from pJ2
-
additional information
-
molecular structure modeling and analysis
additional information
domain organization, lack of a carbohydrate binding module
additional information
the enzyme has an endo-1,3-1,4-beta-glucanase domain
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
no glycoprotein
proteolytic modification
glycoprotein
the enzyme has four potential N-glycosylation sites (N96, N201, N205, and N379) that are highly conserved among GH7 endoglucanases from other Aspergillus species
glycoprotein
-
the enzyme has four potential N-glycosylation sites (N96, N201, N205, and N379) that are highly conserved among GH7 endoglucanases from other Aspergillus species
-
glycoprotein
-
the enzyme has four potential N-glycosylation sites (N96, N201, N205, and N379) that are highly conserved among GH7 endoglucanases from other Aspergillus species
-
glycoprotein
Aspergillus fumigatus CBS 101355
-
the enzyme has four potential N-glycosylation sites (N96, N201, N205, and N379) that are highly conserved among GH7 endoglucanases from other Aspergillus species
-
glycoprotein
Aspergillus fumigatus FGSC A1100
-
the enzyme has four potential N-glycosylation sites (N96, N201, N205, and N379) that are highly conserved among GH7 endoglucanases from other Aspergillus species
-
glycoprotein
-
enzyme I contains 0.7% carbohydrate of which three residues are probably N-acetylglucosamine, enzyme II contains 3.6% carbohydrate
glycoprotein
the enzyme contains two possible N-glycosylation sites at 72 (NKT) and 275 (NPT), respectively
glycoprotein
-
the enzyme contains two possible N-glycosylation sites at 72 (NKT) and 275 (NPT), respectively
-
no glycoprotein
five potential N-glycosylation site Asn-Xaa-Thr/Ser-Zaa, where Zaa is not Pro, are found. Endo H treatment decreases molecular mass from 60000-80000 to 48000, SDS-PAGE
no glycoprotein
no N-glycosylation sites present in the protein, Endo H treatment does not result in a protein band shift
proteolytic modification
presence of an N-terminal signal peptide at residues 1-9
proteolytic modification
-
a N-terminal signal peptide of 29 amino residues is cleaved from the enzyme secreted from Orpinomyces whereas 21 amino acid residues of the signal peptide are removed when the enzyme is produced by E. coli
proteolytic modification
sequence contains a signal peptide of 31 amino acids
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.5 A resolution, native enzyme, 1.6 A resolution, enzyme-inhibitor Glc-beta-1,3-isofagomine-complex, hanging drop vapor diffusion method for the enzyme, sitting drop vapor diffusion method for the complex
-
crystal structure to 1.95 A resolution. The enzyme folds into a classic GH16 beta-jellyroll architecture which consists of two beta-sheets atop each other, with the substrate-binding cleft lying on the concave side of the inner beta-sheet. Two BisTris propane molecules are in the positive and negative substrate binding sites
purified recombinant catalytic domain, sitting drop vapour diffusion method, mixing of 0.002 ml of 30 mg/ml protein in 25 mM Tris pH 7.5, 150 mM NaCl, and 0.002 ml reservori solution containing 0.04 M citric acid, 0.06 M Bis-Tris propane, pH 6.4, 18% w/v PEG 3350, 25°C, 7 days, optimized method, X-ray diffraction structure determination and analysis at 1.95 A resolution, molecular replacement method
molecular modeling of structures of wild-type and mutant K142N/Q203L/N214D does not reveal obvious differences in structure
molecular modeling of structure. Residues T2, S5,Y7, N14, S44, N78, S143, Y144, T146, D161, Q163, W209 and K213 are implicated in the contact between two monomers
enzyme-substrate complex, experiments by car-Parinello molecular dynamics simulations combined with force field molecular dynamics QM/MM CPMD, substrate 4-methylumbelliferyl tetrasaccharide
-
H(A16-M) in complex with beta-glucan tetrasaccharide, resolution range from 34.5 A to 1.64 A, hanging-drop vapour diffusion, room temperature
-
homology modeling of structure. The enzyme is primarily composed of a beta-sheet, with two juxtaposed curved antiparallel beta-sheets consisting of seven strands. It forms a single compact globular domain, creating a deep cavity as a carbohydrate-binding channel for beta-glucan. The carbohydrate-binding region is a type B domain
-
homology modeling of structure. Amino acid residues expected to form hydrogen bond with beta-glucan, nucleophile Glu134, the acid/base catalyst Glu138, Tyr152 and water mediate hydrogen bonds with Asn55, Gln148, Asn150, Glu160, and Asn211, are found in the active site cleft
the crystal structure of the enzyme is used for structure modelling, PDB ID 3O5S
molecular dynamic simulation and and optimization of residue sites in the calcium region to increase the thermostability
-
apo-form and substrate complex structures of mutant V18Y/W203Y, to 1.53 A resolution
mutant E85I, at 2.2 A resolution, by hanging-drop vapour-diffusion method at room temperature. The mutant crystallizes in space group P3121 with one molecule in the asymmetric unit, Ca2+ ion-binding site is maintained
mutant F40I, to 1.7 A resolution. Overall globular structures in the wild-type and mutant F40I enzymes do not differ
mutant W203F of truncated beta-glucanase catalytic domain, residues 1-243, to 1.4 A resolution. Residue W203 is stacked with the glucose product of cellotriose. Two extra calcium ions and a Tris molecule bind to the mutant structure. A Tris molecule, bound to the catalytic residues of E56 and E60, is found at the position normally taken by substrate binding at the -1 subsite. A second Ca2+ ion is found near the residues F152 and E154 on the protein's surface, and a third one near the active site residue D202
purified recombinant mutant V18Y/W203Y alone and in complex with product cellotetraose , from 0.1 M TrisHCl, pH 7.5, 0.3 M calcium acetate, and 29% PEG 5000 MME for the free mutant, and 0.15 M Tris, pH 8.5, 0.4 M calcium acetate and 33% PEG 5000 MME plus soaking in mother liquor with 5 mM cellotetraose for 1 h for the complexed mutant, X-ray diffraction structure determination and analysis at 1.53 A resolution, molecular replacement method
truncated form of enzyme containing the catalytic domain from amino acid 1-258, seleno-methionine labeled protein
-
purified wild-type PtLic16A and inactive mutant E113A in ligand-free form and in complex with the ligands cellobiose, cellotetraose and glucotriose, X-ray diffraction structure determination and analysis at 1.80-2.25 A resolution. Native PtLic16A crystals belong to the space group C2221 and contain four polypeptide chains in an asymmetric unit. The E113A mutant crystals belong to a different space group of C2 and have two protein molecules in an asymmetric unit. The third E113A crystal belongs to space group P21, with four molecules in an asymmetric unit
hanging drop vapor diffusion method, using 7.5% (v/v) 2-methyl-2,4-pentanediol, 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, and 0.1 M Tris (base)/Bicine, pH 8.5
the structure of Gluc5_26A adopts a stable trimeric quaternary structure also observable in solution. The N-terminal region protrudes into the active site of an adjacent monomer. The N-terminus governs the substrate specificity of Gluc5_26A. Its deletion opens the enzyme cleft at the -3 subsite and turns the enzyme into an endo-beta(1,4)-glucanase
purified recombinant His-tagged wild-type and mutant enzymes, hanging drop vapour diffusion method, mixing of 0.002 ml of 10 mg/ml protein with 0.002 ml reservoir solution containing 24% PEG 3350 and 100 mM sodium citrate, pH 5.2, 4°C, crystals of enzyme mutant E269S in complex with laminarin oligosaccharides are obtained from 0.002 ml of 13.3 mg/ml protein and 5 mM of purified hexasaccharides,with 0.001 ml of reservoir solution containing 100 mM sodium malonate, imidazole, and boric acid (MIB-buffer), pH 4.0, and 19% of PEG 1500 in hanging drops at 20°C. Single crystals of mutant E269S in complex with MLG trisaccharides are obtained from mixing 0.002 ml 11.7 mg/ml of protein, 0.04% w/v of MLG degradation products with 0.001 ml of reservoir solution containing 100 mM MIB buffer, pH 4.0, 17% of PEG 1500, and 10% of glycerol in hanging drops at 12°C, X-ray diffraction structure determination and analysis at 1.13-1.45 A resolution, molecular replacement method
purified wild-type PtLic16A and inactive mutant E113A in ligand-free form and in complex with the ligands cellobiose, cellotetraose and glucotriose, X-ray diffraction structure determination and analysis at 1.80-2.25 A resolution. Native PtLic16A crystals belong to the space group C2221 and contain four polypeptide chains in an asymmetric unit. The E113A mutant crystals belong to a different space group of C2 and have two protein molecules in an asymmetric unit. The third E113A crystal belongs to space group P21, with four molecules in an asymmetric unit
-
purified wild-type PtLic16A and inactive mutant E113A in ligand-free form and in complex with the ligands cellobiose, cellotetraose and glucotriose, X-ray diffraction structure determination and analysis at 1.80-2.25 A resolution. Native PtLic16A crystals belong to the space group C2221 and contain four polypeptide chains in an asymmetric unit. The E113A mutant crystals belong to a different space group of C2 and have two protein molecules in an asymmetric unit. The third E113A crystal belongs to space group P21, with four molecules in an asymmetric unit
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K142N/Q203L/N214D
E134A
E134A/E138A
-
no enzymic activity, but reaction occurs in presence of sodium azide, E138 is the general acid-base catalyst
N207D
mutant displays better thermotolerance than the wild type but also reduced activity
K48A
-
123% of wild-type activity, thermostability and halostability are enhanced. Catalytic efficiency of mutants is enhanced as a result of the increase in substrate affinity. The half-lives of the mutant increases up to about 7fold at 60-70°C
K48L
-
137% of wild-type activity, thermostability and halostability are enhanced. Catalytic efficiency of mutants is enhanced as a result of the increase in substrate affinity. The half-lives of the mutant increases up to about 7fold at 60-70°C
K48A
Bacillus sp. (in: Bacteria) KCCM 90078
-
123% of wild-type activity, thermostability and halostability are enhanced. Catalytic efficiency of mutants is enhanced as a result of the increase in substrate affinity. The half-lives of the mutant increases up to about 7fold at 60-70°C
-
K48L
Bacillus sp. (in: Bacteria) KCCM 90078
-
137% of wild-type activity, thermostability and halostability are enhanced. Catalytic efficiency of mutants is enhanced as a result of the increase in substrate affinity. The half-lives of the mutant increases up to about 7fold at 60-70°C
-
K48A
mutation enhances catalytic efficiency, thermostability and halostability
K48L
mutation enhances catalytic efficiency, thermostability and halostability
M44V/N53H
M44V/N53H
E46P/S43E/H205P/S40E
-
64% increase in specific activity, 20°C increase in optimal enzymatic temperature and a 13.8 °C rise in protein melting temperature compared to wild-type
K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
mutant with increased catalytic activity and thermostability
N31C/T187C
-
the mutations significantly enhance the protein thermostability
N31C/T187C/P102C/N125C
P102C/N125C
-
the mutations significantly enhance the protein thermostability
E46P/S43E/H205P/S40E
-
64% increase in specific activity, 20°C increase in optimal enzymatic temperature and a 13.8 °C rise in protein melting temperature compared to wild-type
-
N31C/T187C
-
the mutations significantly enhance the protein thermostability
-
N31C/T187C/P102C/N125C
P102C/N125C
-
the mutations significantly enhance the protein thermostability
-
D202L
shows a 1.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
D202N
exhibits a 1.8fold increase in catalytic efficiency (kcat/KM) compared to the wild-type
D206M
shows a 1.1fold increase in catalytic efficiency (kcat/KM) compared to the wild-type
D206N
exhibits a 1.5fold increase in catalytic efficiency (kcat/KM) compared to the wild-type
D206R
exhibits the highest relative activity at 50°C over 10 min, shows a 1.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
D58E
-
dramatic decrease in kcat, substrate affinity similar to wild type
D58N
-
dramatic decrease in kcat, substrate affinity similar to wild type
E11L
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity, more than 2fold increase in KM-value, significant decrease in catalytic efficiency
E47I
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 2fold increase in KM-value
E56D
-
dramatic decrease in kcat, substrate affinity similar to wild type
E60D
-
dramatic decrease in kcat, substrate affinity similar to wild type
F205L
shows a 3.8fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
F40I
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity, significant decrease in catalytic efficiency
G201S
shows a 1.5fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
G207N
shows a fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
K200F
is the most heat-sensitive enzyme, retains 72% of activity at 45°C for 10 min, shows a 1.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
K200M
shows a 1.1fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
K64A
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure
K64M
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 2fold increase in KM-value
L62G
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure
M27D/M39R
M27R/M39D
M39F
N139A
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 2fold increase in KM-value, significant decrease in catalytic efficiency
N208G
shows a fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
N44L
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure
N44Q
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 2fold increase in KM-value
R137M
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity, more than 2fold increase in KM-value, significant decrease in catalytic efficiency
R137Q
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity, more than 2fold increase in KM-value, significant decrease in catalytic efficiency
R209M
shows a 1.1fold increase, in catalytic efficiency (kcat/KM) compared to the wild-type
S71F
S84D
T204F
shows a 2.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
V18Y
V18Y/W203Y
V61F
W141F
-
5-7-fold increase in KM-value for lichenan compared to wild type, decrease in kcat-value, no significant change in thermal stability
W141H
-
5-7-fold increase in KM-value for lichenan compared to wild type, decrease in kcat-value, no significant change in thermal stability
W148F
-
decrease in kcat-value, no significant change in thermal stability
W165F
-
after incubation at pH 3.0, 1 h, 3-7-fold higher activity than wild type
W186F
-
increase in kcat-value, no significant change in thermal stability
W203F
W203R
W203Y
W54F
-
decrease in kcat-value, no significant change in thermal stability
W54Y
-
decrease in kcat-value, no significant change in thermal stability
Y42L
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity
C263S
-
random mutagenesis, the mutant shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme
D221G2
-
random mutagenesis, the mutant shows unaltered properties compared to the wild-type enzyme
D56G
-
random mutagenesis, the mutant shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme
D56G/D221G/C263S
-
random mutagenesis, mutant PtLic16AM2 shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme. Mutation D221G alone does not lead to altered enzyme properties
E113A
-
inactive mutant. In the structure of E113A/1,3-1,4-beta-glucotriose complex, the sugar bound to the -1 subsite adopts an intermediate-like (alpha-anomeric) configuration
W108A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W108F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W108Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E113A
inactive mutant. In the structure of E113A/1,3-1,4-beta-glucotriose complex, the sugar bound to the -1 subsite adopts an intermediate-like (alpha-anomeric) configuration
W108A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W108F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W108Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E113A
-
inactive mutant. In the structure of E113A/1,3-1,4-beta-glucotriose complex, the sugar bound to the -1 subsite adopts an intermediate-like (alpha-anomeric) configuration
-
W108A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
W108F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
W108Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
W253A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
C17R/Q87T/D152G/Y307H/V330A/N344D
E149D/V370E
the mutant shows 59.9% activity at pH 5.5 and 50°C compared to the wild type enzyme
K12R/F30L/N114D/N252D/T348S/N380S
the mutant shows 62.1% activity at pH 5.5 and 50°C compared to the wild type enzyme
N197D/M322V
N4S
the mutant shows 75.3% activity at pH 5.5 and 50°C compared to the wild type enzyme
S11R/T210S
the mutant shows 231.3% activity at pH 5.5 and 50°C compared to the wild type enzyme
Y389F/ K395R
the mutant shows 81% activity at pH 5.5 and 50°C compared to the wild type enzyme
E269S
additional information
K142N/Q203L/N214D
mutant isolated by error-prone PCR, 48.6 increase in catalytic activity compared to wild-type. The optimal pH of the mutated enzyme is 5.0, which is lower than the parent enzyme, but thermal stability is almost the same
K142N/Q203L/N214D
mutation leads to increased activity and decreased optimal pH, while the same thermostability is maintained
K142N/Q203L/N214D
-
mutant isolated by error-prone PCR, 48.6 increase in catalytic activity compared to wild-type. The optimal pH of the mutated enzyme is 5.0, which is lower than the parent enzyme, but thermal stability is almost the same
-
K142N/Q203L/N214D
-
mutation leads to increased activity and decreased optimal pH, while the same thermostability is maintained
-
E134A
-
catalyzes condensation reaction with alpha-fluorido-substrates
E134A
-
mutant devoid of hydrolase activity but efficiently catalyzing transglycosylation
M44V/N53H
mutant displays best ability to tolerate an acid environment and improved thermal stability
M44V/N53H
-
mutant displays best ability to tolerate an acid environment and improved thermal stability
-
N31C/T187C/P102C/N125C
-
introduction of disulfide pairs N31C-T187C and P102C-N125C, 48.3% increase in half-life value at 60°C and a 4.1°C rise in melting temperature, catalytic properties are similar to wild-type with a decrease in optimal pH
N31C/T187C/P102C/N125C
-
the mutant with wild type activity shows a 48.3% increase in half-life value at 60°C and a 4.1°C rise in melting temperature compared to the wild type enzyme
N31C/T187C/P102C/N125C
-
introduction of disulfide pairs N31C-T187C and P102C-N125C, 48.3% increase in half-life value at 60°C and a 4.1°C rise in melting temperature, catalytic properties are similar to wild-type with a decrease in optimal pH
-
N31C/T187C/P102C/N125C
-
the mutant with wild type activity shows a 48.3% increase in half-life value at 60°C and a 4.1°C rise in melting temperature compared to the wild type enzyme
-
M39F
site-directed mutagenesis, 7% reduced activity compared to wild-type
S84D
site-directed mutagenesis, 19% reduced activity compared to wild-type
V18Y
104% of wild-type activity. Increase in thermostability by 2 degrees
V18Y
site-directed mutagenesis, 4% reduced activity compared to wild-type
V18Y/W203Y
site-directed mutagenesis, 34% increased activity compared to wild-type
V61F
site-directed mutagenesis, 79% reduced activity compared to wild-type
W203F
-
increase in kcat-value, no significant change in thermal stability
W203F
exhibits a 2.4fold increase in catalytic efficiency (kcat/KM) compared to the wild-type
W203F
mutant of truncated beta-glucanase catalytic domain, residues 1-243. mutant has increased hydrolytic activity. Residue W203 is stacked with the glucose product of cellotriose. Two extra calcium ions and a Tris molecule bind to the mutant structure. A Tris molecule, bound to the catalytic residues of E56 and E60, is found at the position normally taken by substrate binding at the -1 subsite. A second Ca2+ ion is found near the residues F152 and E154 on the protein's surface, and a third one near the active site residue D202
W203F
site-directed mutagenesis, 13% reduced activity compared to wild-type
W203F
-
site-directed mutagenesis, truncated and mutated 1,31,4-beta-D-glucanase, no activity with laminarin
W203R
-
5-7-fold increase in KM-value for lichenan compared to wild type, decrease in kcat-value, after incubation at pH 3.0, 1 h, 3-7-fold higher activity than wild type, no significant change in thermal stability
W203R
exhibits a 207fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
W203Y
site-directed mutagenesis, 30% increased activity compared to wild-type
C17R/Q87T/D152G/Y307H/V330A/N344D
2.1fold increase in specific activity
C17R/Q87T/D152G/Y307H/V330A/N344D
the mutant shows 200.8% activity at pH 5.5 and 50°C compared to the wild type enzyme
N197D/M322V
the mutant shows 144.7% activity at pH 5.5 and 50°C compared to the wild type enzyme
E269S
site-directed mutagenesis, nucleophile replacement, inactive mutant
E269S
-
site-directed mutagenesis, nucleophile replacement, inactive mutant
-
additional information
-
construction of diverse enzyme truncation mutants for domain functional analysis, overview
additional information
-
generation of transgenic Nicotiana tabacum plants expressing LicB from Clostridium thermocellum, no altered phenotype, overview. Expression of bacterial beta-1,3-1,4-glucanase gene exerts no significant influence on tobacco plant metabolism, while the expression of bacterial beta-1,3-glucanase affects plant metabolism only at early stages of growth and development. By contrast, the expression of bacterial beta-1,4-glucanase has a significant effect on transgenic tobacco plant metabolism
additional information
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
additional information
-
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
additional information
-
construction of hybrid genes encoding circularly permutated lichenase variants with integrated small peptides, i.e. NC-L-53, NC-L-99, NC-L-53-99, and NC-L-140, method overview. Generation of a thermostable lichenase gene variant encoding only the enzyme's catalytic domain LicBM3. Thermostabilities of the mutant constructs, overview
additional information
end-to-end fusion, circular permutation, domain insertion
additional information
end-to-end fusion, circular permutation, domain insertion
additional information
-
end-to-end fusion, circular permutation, domain insertion
-
additional information
-
construction of diverse enzyme truncation mutants for domain functional analysis, overview
-
additional information
-
construction of hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase. Hybrid enzyme H2 consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens. Hybrid enzyme H1 exhibits increased thermostability especially in an acidic environment compared to both parental enzymes. Hybrid enzyme H2 is more thermolabile than the naturally occuring beta-glucanases
additional information
-
hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, expression in Escherichia coli
additional information
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
additional information
-
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
additional information
-
modifying five (out of 12) epsilon-amino groups in lysine residues with nitrous acid improves thermostablility and enzymatic activity of the enzyme, optimizing the condition of chemical modification, overview. Compared to the wild-type enzyme, the optimally-modified enzyme has higher specific activity and T50 value, which are 3370 U/mg and 70°C, respectively. Its half-life values at 50 and 60°C are extended and reach 58.5 and 49.5 min, respectively
additional information
-
covalent linkage between the N- and C-termini of a polypeptide chain to create circular variants of the enzyme by an intein-driven protein splicing approach, method, overview. Two circular variants, LicAC1 and LicA-C2, which have connecting loops of 20 and 14 amino acids, respectively, show catalytic activities that are approximately two and three times higher, respectively, compared to that of the linear LicA, LicA-L1. Also the thermal stability of the circular variants is significantly increased compared to the linear form. The circular proteins contain a thrombin recognition site and can be linearized by cleavage with thrombin
additional information
-
the truncated gene product, devoid of cellulose-binding domain, shows 60% of activity and binds to avicel
additional information
construction of a chimeric bifunctional laccase/beta-1,3-1,4-glucanase mutant enzyme by insertion fusion of the bglS and cotA genes, protein CotA, UniProt ID P07788, the approximation of the two catalytic domains in the chimeric enzyme, and the formation of an inter-domain interface increase catalytic activities,molecular dynamics simulations, overview. The laccase efficiency with substrate 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonic acid) is higher in the chimera, while the glucanase activity with lichenan shows a Kcat/KM value increased by 26%, a lower Km anf kcat. The beta-1,3-1,4-glucanase hydrolyzes plant cell wall beta-glucans, and the copper-dependent oxidase laccase catalyzes the oxidation of aromatic compounds with simultaneous reduction of oxygen to water. The mutant chimeric enzyme shows synergistic sugar release from milled sugarcane bagasse
additional information
-
construction of a chimeric bifunctional laccase/beta-1,3-1,4-glucanase mutant enzyme by insertion fusion of the bglS and cotA genes, protein CotA, UniProt ID P07788, the approximation of the two catalytic domains in the chimeric enzyme, and the formation of an inter-domain interface increase catalytic activities,molecular dynamics simulations, overview. The laccase efficiency with substrate 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonic acid) is higher in the chimera, while the glucanase activity with lichenan shows a Kcat/KM value increased by 26%, a lower Km anf kcat. The beta-1,3-1,4-glucanase hydrolyzes plant cell wall beta-glucans, and the copper-dependent oxidase laccase catalyzes the oxidation of aromatic compounds with simultaneous reduction of oxygen to water. The mutant chimeric enzyme shows synergistic sugar release from milled sugarcane bagasse
additional information
end-to-end fusion by cyclization with SpyTag/SpyCatcher, and oligomerization by Foldon
additional information
end-to-end fusion by cyclization with SpyTag/SpyCatcher, and oligomerization by Foldon
additional information
end-to-end fusion by cyclization with SpyTag/SpyCatcher, and oligomerization by Foldon
additional information
end-to-end fusion by cyclization with SpyTag/SpyCatcher, and oligomerization by Foldon
additional information
-
end-to-end fusion by cyclization with SpyTag/SpyCatcher, and oligomerization by Foldon
-
additional information
-
construction of a chimeric bifunctional laccase/beta-1,3-1,4-glucanase mutant enzyme by insertion fusion of the bglS and cotA genes, protein CotA, UniProt ID P07788, the approximation of the two catalytic domains in the chimeric enzyme, and the formation of an inter-domain interface increase catalytic activities,molecular dynamics simulations, overview. The laccase efficiency with substrate 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonic acid) is higher in the chimera, while the glucanase activity with lichenan shows a Kcat/KM value increased by 26%, a lower Km anf kcat. The beta-1,3-1,4-glucanase hydrolyzes plant cell wall beta-glucans, and the copper-dependent oxidase laccase catalyzes the oxidation of aromatic compounds with simultaneous reduction of oxygen to water. The mutant chimeric enzyme shows synergistic sugar release from milled sugarcane bagasse
-
additional information
-
the truncated gene product, devoid of cellulose-binding domain, shows 60% of activity and binds to avicel
-
additional information
rational design of disulfide bonds in the enzyme by site-directed mutagenesis
additional information
-
rational design of disulfide bonds in the enzyme by site-directed mutagenesis
-
additional information
-
truncated form of enzyme containing the catalytic domain from amino acid 1-258, higher thermal stability and enzymatic activity than wild type protein, crystal structure
additional information
construction of mutants based on catalytic domain, residues 1-243, with higher thermostability and specific activity
additional information
-
engineering of dual-functional hybrid glucanases from a truncated and mutated 1,3-1,4-beta-D-glucanase gene TFsW203F from Fibrobacter succinogenes, and a 1,3-beta-D-glucanase gene TmLam from hyperthermophilic Thermotoga maritima used as target enzymes, by ligating substrate-binding domains (TmB1 and TmB2) and the catalytic domain (TmLamCD) of TmLam to the N- or C-terminus of TFsW203F to create four hybrid enzymes, TmB1-TFsW203F, TFsW203F-TmB2, TmB1-TFsW203F-TmB2 and TFsW203F-TmLamCD, creation of desirable hybrid enzymes with economic benefits for industrial applications. Improved thermal tolerance of the hybrid enzyme TFsW203FTmLamCD, fluorescence and circular dichroism spectrometric analyses, overview. Kinetic properties of parental TFsW203F and mutant hybrid glucanases
additional information
kinetic and thermostability analysis of the mutant enzymes, overview
additional information
end-to-end fusion, site-directed mutagenesis
additional information
-
end-to-end fusion, site-directed mutagenesis
-
additional information
-
protein-engineered, thermostable (1,3-1,4)-beta-glucanase: the codons for hybrid H(A12-M)DELTAY13 are modified to match those of the gene encoding barley (1,3-1,4)-beta-glucanase isoenzyme EII
additional information
-
screening of the random mutant library, mutations D56G, D221G, and C263S have only minor effects on specific activity and pH stability
additional information
-
construction of hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase. Hybrid enzyme H2 consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens. Hybrid enzyme H1 exhibits increased thermostability especially in an acidic environment compared to both parental enzymes. Hybrid enzyme H2 is more thermolabile than the naturally occuring beta-glucanases
additional information
-
hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, expression in Escherichia coli
additional information
truncated mutants, which comprise 360, 286, and 215 amino acid residues instead of the 409 residues of the wild type, show complete loss of enzymatic activity
additional information
-
UV irradiation leads to mutants TC2 and TC5 with increased activity against barley beta-glucan during growth on solka floc
additional information
deletion of the N-terminal sequence up to residue Ser38. The mutant is devoid of the helix-turn motif interacting with residues of the substrate-binding cleft at the level of subsite -3. The mutation uncovers the enzyme cleft at the -3 subsite and turns the enzyme into an endo-beta(1,4)-glucanase
additional information
-
deletion of the N-terminal sequence up to residue Ser38. The mutant is devoid of the helix-turn motif interacting with residues of the substrate-binding cleft at the level of subsite -3. The mutation uncovers the enzyme cleft at the -3 subsite and turns the enzyme into an endo-beta(1,4)-glucanase
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2
1 h, wild-type 5% residual activity, mutant T113S 40% residual activity, mutant M44V/N53H 50% residual activity, mutant M44V/N53H 80% residual activity
738548
3
-
retains approximately 80% of original activity after treatment at pH 3.0 for 12 h
677749
3 - 10
3 - 11
purified recombinant His-tagged enzyme, 50°C, 30 min, completely stable
729409
3 - 8
completely stable up to pH 6.0, 40% activity remaining at pH 7.0, inactivation at pH 8.0
752108
3.5 - 12
the enzyme is acid-, alkali- and salt-tolerant, the purified recombinant His-tagged enzyme retains more than 80% activity after incubation for 4 h
729476
3.5 - 7
3.5 - 8
purified recombinant enzyme, 30 min, over 80% activity remaining
750809
3.5 - 8.5
-
the enzyme remains stable between pH 3.5 and 8.5 after 30 min incubation
744957
3.5 - 9
4 - 10
4 - 6
-
the recombinant enzyme is stable between pH 4.0 and 6.0, having 85% of the original activity
677749
4 - 8
Thermomonospora sp.
-
-
678492
4 - 9
4.1
5 - 7.5
purified native enzyme, retains 90% of its activity at 60°C for 30 min
729865
5.5 - 7.5
-
the enzyme retains about 60% activity at pH 5.5 and 90% at pH 7.5 after 10 min of incubation
746205
5.6 - 6
6 - 9
8
-
retains approximately 80% of original activity after treatment at pH 8.0 for 12 h
677749
3.5 - 7
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase, stable
171537
3.5 - 7
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase, stable
171537
4 - 10
-
purified isozymes EG1 and EG2, retaining over 90% activity after 48 h, after 72 h isozyme EG1 loses 30% and isozyme EG2 15% activity
730844
4 - 9
-
purified native enzyme TaGlu34 exhibits excellent stability at pH 4.0-9.0, retaining more than 80% of its maximal activity
750242
4.1
-
65°C, 1 h, hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, 85%-95% of the initial activity is retained
171544
4.1
-
65°C, 1 h, hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, 85%-95% of the initial activity is retained
171544
5.6 - 6
-
hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens, stable
171537
5.6 - 6
-
hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens, stable
171537
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
20 - 40
-
the remaining activity decreased to 20% at 20-40°C and is completely destroyed at 50-70°C
22
-
11 days, complete inactivation of wild-type, 70% residual activity of mutant D70V
25 - 40
purified recombinant enzyme, pH 6.0, 70 min, completely stable
30 - 60
30 - 90
-
temperature effects on mutant W203F and on W203F mutant bifunctional hybrid enzymes, the latter is more resistant to heat treatment than the parental TFsW203F, overview
40
40 - 50
-
purified isozymes EG1 and EG2, retaining over 90% activity after 1 h
40 - 55
45
50
50 - 60
-
sharp decrease in activity up to 60°C, but very stable below 50°C
50 - 70
55
60
60 - 70
65
70
75
80
80 - 90
purified recombinant enzyme, 70% and 40% activity remaining after 2 h at 80°C and 90°C, respectively, half-lives of the enzyme are 3.4 h and 1.4 h at 80°C and 90°C, respectively
85
90
additional information
100
purified native enzyme, pH 5.5, 40% activity remaining after 30 min
100
-
even when subjected to 100°C for 3 h, beta-glucanase activity does not show significant reduction
30 - 60
completely stable up to 50°C for 1 h and loss of 10% activity after 48 h at 50°C, 50% activity remaing at 55°C after 30 min and inactivation after 5 h at 55°C, rapid inactivation at 60°C
30 - 60
-
99.1, 87.8, 56.6, and 34.2% residual activity after 30 min preincubation at 30, 40, 50, and 60°C, respectively
30 - 60
-
104.5, 101.2, 67.9, and 21.2% residual activity after 30 min preincubation at 30, 40, 50, and 60°C, respectively
30 - 60
-
102, 91.2, 60.7, and 4.3% residual activity after 30 min preincubation at 30, 40, 50, and 60°C, respectively
30 - 60
-
98, 74.3, 2.4, and 0% residual activity after 30 min preincubation at 30, 40, 50, and 60°C, respectively
40
-
purified native enzyme, 75% activity remaining after 120 min
40 - 55
-
the enzyme remains stable between 40 and 55°C after 30 min incubation
45
the wild-type maintains more than 85% of the original activity for 10 min
50
purified recombinant His-tagged enzyme, pH 6.0, 30 min, completely stable
50
purified recombinant His-tagged enzyme retaining more than 70% activity at up to 50°C for 2 h
50
-
purified native enzyme, 60% activity remaining after 120 min
50 - 70
-
after incubation at 50, 60, and 70°C for 30 min, the residual activity is 95, 60, and 0%, respectively
50 - 70
-
after 2 h incubation at 50°C and 60°C, the residual activity remaines 100% and 50%, respectively, while the enzymatic activity is abolished after 3 min incubation at 70°C
50 - 70
-
the purified native enzyme shows half-lives of 209, 130 and 69 min at 50, 60 and 70°C, respectively
55
purified recombinant His-tagged enzyme, half-life is about 50 min, 10% activity remaining after 2 h
60
purified recombinant enzyme, retains more than 90% activity after 2 h
60
2 h, more than 85% residual activity, both wild-type and mutant K142N/Q203L/N214D
60
-
purified isozymes EG1 and EG2, half-lives are 55 min and 5 h, respectively
60
-
pH 5.0-6.0, 10 min, stable. pH 6, in presence of 10 mM CaCl2 and serum albumin, stable for 120 min
60
half-life of wild-type 46.2 min, of mutant K48A 346 min, of mutant K48L 138 min, respectively
60
-
the melting temperature is 50.8°C. The half-life of the enzyme at 60°C is 59 min. The enzyme retains more than 60% of its activity at up to 75°C and is inactivated at 80°C after 10 min of incubation
60
-
4 min, 50% inactivation, wild-type, 11 min, 50% inactivation, mutant D70V
60
purified recombinant His-tagged enzyme, inactivation within 10 min, in presence of 5 mM CaCl2 the enzyme retains over 80% activity after 2 h
60
after 30 min and 1 h at 60°C, the enzyme retains about 60% and 35% of activity, respectively
60
purified native enzyme, no loss in activity at pH 5.5 for 30 min, half-life is 225 min
60 - 70
-
purified recombinant enzyme, the wild-type enzymes activity decline rapidly above 60°C, while the optimally-modified enzyme is more stable and shows activity up to 70°C
65
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase is stable for more than 1 h at pH 5.5. The 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase. Hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens irreversible thermoinactivated within 20-25 min
65
-
the linear enzyme form loses 50% activity within 3 min, whereas the two circular variants have 6fold (LicA-C1) and 16fold (LicA-C2) increased half-life time of inactivation
65
purified recombinant His-tagged enzyme, pH 6.0, 30 min, loss of 50% activity
65
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase is stable for more than 1 h at pH 5.5. The 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase. Hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens irreversible thermoinactivated within 20-25 min
65
purified recombinant His-tagged enzyme, in presence of 5 mM CaCl2 the enzyme retains 40% activity after 10 min, and 20% after 20 min, inactivation after 1 h
70
-
purified recombinant enzyme, pH 7.0, 40% activity remaining after 6 h
70
purified recombinant enzyme, retains more 75% activity after 10 min
70
-
pH 6.0, 1 h, hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase exhibit 90% of the initial activity, the parental enzymes retain 5% or less of the initial activity
70
-
purified isozymes EG1 and EG2, half-lives are 10 min and 52 min, respectively
70
purified recombinant His-tagged enzyme, pH 6.0, 30 min, inactivation
70
half-life of wild-type 4.5 min, of mutant K48A 30.5 min, of mutant K48L 15.1 min, respectively
70
-
pH 6.0, 1 h, hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase exhibit 90% of the initial activity, the parental enzymes retain 5% or less of the initial activity
70
purified recombinant enzyme, completely stable for 8 h, and loss of 20% activity after 22 h
75
-
purified recombinant wild-type enzyme, 10 min, 51% remaining activity in absence of Ca2+, 86% in presence of 1 mM Ca2+
80
-
purified recombinant wild-type enzyme, 5 min, 54% remaining activity in absence of Ca2+, 73% in presence of 1 mM Ca2+
80
-
purified recombinant enzyme, pH 7.0, no activity remaining after 1 h
80
purified recombinant enzyme, retains more 44% activity after 10 min
80
purified recombinant enzyme, retains 54% activity at 80°C after incubation for 60 min
80
4 min, complete loss of activtiy for wild-type, 10 min, 60% residual activity for mutant T113S
80
purified native enzyme, pH 5.5, half-life is 53 min, 80% activity remaining after 30 min
85
purified native enzyme, pH 5.5, half-life is 27 min, inactivation after 120 min
90
-
the residual activity of mHG at 90°C for 10 min is 83.45% of its maximum activity
90
purified native enzyme, pH 5.5, 60% activity remaining after 30 min
additional information
-
Ca2+ stabilizes the enzyme at higher temperatures, thermal stability of recombinant wild-type enzyme and mutants in presence and absence of Ca2+, overview
additional information
-
particularly thermostable in presence of Ca2+
additional information
-
Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation
additional information
-
addition of 1 mM EDTA causes the linear enzyme to denature at 59.8°C, which is lower compared to the melting temperature of 62.6°C in the presence of calcium. At 1 mM EDTA, the circular enzyme variant LicA-C1 shows a melting temperature of 62.8°C, at 1 mM CaCl2 the melting temperature is 66.4°C
additional information
-
particularly thermostable in presence of Ca2+
additional information
-
particularly thermostable in presence of Ca2+
additional information
-
thermal inactivation follow first-order kinetics, overview
additional information
-
particularly thermostable in presence of Ca2+
additional information
-
Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation
additional information
-
particularly thermostable in presence of Ca2+
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation
enzyme is rather unstable, stability increases from pH 4 to pH 7 and decreases from 25°C to 35°C, o-phenanthroline lowers stability of enzyme
-
in strong acid solution (HCl), beta-glucanase loses activity under conditions of pH 2.0, 1.0, and 0 indicating no tolerance to HCl
-
the enzyme is able to conserve its activity after a drastic treatment with 500 mM NaOH, and the only way to stop enzyme activity is treatment with 8 M urea
the purified recombinant His-tagged enzyme retains over 90% activity in 4 M NaCl at 25°C for 24 h
Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation
-
Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM sodium phosphate, pH 7.8, 300 mM sodium chloride, stable for several weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3.1fold to homogeneity by ammonium sulfate fractionation, dialysis and anion exchange chromatography, followed by hydrophobic interaction chromatography
affinity chromatography of epoxy-activated sepharose 6B and ultrafiltration technique
-
by ammonium sulfate precipitation and two steps of ion-exchange chromatographies. Purified 122.5fold with an apparent homogeneity and a recovery yield of 8.9%
-
DEAE Sephadex A50 column chromatography and Sephacryl S-200 gel filtration
Thermomonospora sp.
-
GSTrap FF column chromatography and HiTrap Benzamidine FF column chromatography
Hi-Trap Q column chromatography and CHT-II column chromatography
immobilized metal ion affinity chromatography, gel filtration, anion exchange chromatography
-
mutants purified on Ni-NTA affinity column, more than 95% purity
native enzyme 37fold from strain YC-9 by ammonium sulfate precipitation, anion exchange chromatography, and gel filtration, recombinant enzyme from Escherichia coli strain BL21 (DE3) cell culture supernatant by ammonium sulfate precipitation, anion exchange chromatography, and gel filtration
native enzyme 6.8fold by ammonium sulfate fractionation and two different steps of anion exchange chromatography, to homogeneity
native enzyme by 16fold ammonium sulfate fractionation, combined cation and anion exchange chromatography, and another anion exchange chromatography
-
native extracellular enzyme 0.63fold from cell-free culture supernatant by heat treatment at 50°C for 10 min, anion exchange chromatography, lyophilization, and gel filtration to homogeneity
-
native extracellular enzyme 14.24fold from culture supernatant by ultrafiltration and gel filtration to homogeneity
-
native extracellular enzyme from cell culture supernatant 7.3fold to homogeneity by ammonium sulfate fractionation, and anion exchange and hydrophobic interaction chromatography
-
native extracellular isozymes EG1 and EG2 0.24fold and 11.6fold, respectively, from cell-free culture supernatant by dialysis and concentration with PEG 400, followed by anion exchange chromatography and gel filtration, both isozymes to homogeneity
-
parental enzymes and hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase
parental enzymes, hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
Q-Sepharose FF column twice, Ni-NTA affinity column for the Escherichia coli protein, Q-Sepharose FF column for the Pichia pastoris protein
-
recombinant enzyme from Escherichia coli
recombinant enzyme from Escherichia coli strain C43(DE3), the signal peptide is cleaved
KM079629
recombinant GST-tagged EGL1 from Escherichia coli by glutathione affinity chromatography, the tag is cleaved off by thrombin, followed by benzamidine resin chromatography
recombinant GST-tagged EGL2 from Escherichia coli by glutathione affinity chromatography, the tag is cleaved off by thrombin, followed by benzamidine resin chromatography
recombinant His-tagged enzyme 2.5fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography to homogeneity
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by dialysis, ultrafiltration, and nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
recombinant His-tagged isolated catalytic domain of the enzyme from Escherichia coli strain BL21trxB(DE3) by nickel affinity chromatography and dialysis, tag cleavage by factor Xa digestion, and removal of the tag by another step of nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, tag cleavage and again nickel affinity chromatography, recombinant extracellular wild-type and mutants V18Y, W203Y, and V18Y/W203Y enzymes from Pichia pastoris cell culture supernatant by dialysis and anion exchange chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme from Escherichia coli by nickel affinity chromatography and ultrafiltration
recombinant N-terminally His-tagged linear and circular enzymes from Escherichia coli strains BL21(DE3) or JM109(DE3) by nickel affinity chromatography
-
secreted recombinant OmpA-His6-tagged enzyme from cell culture supernatant by nickel affinity chromatography
the cloned protein from the recombinant strain BL21/pET21a-RuCelA is purified using Ni-NTA resin
wild type and mutant enzymes W101F, W101Y, E103D, E103Q, D105N, D105K, E107D, E107Q, and E107H
-
parental enzymes and hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase
-
parental enzymes and hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase
-
parental enzymes, hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
-
parental enzymes, hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminally truncated (10 kDa), overexpression in Escherichia coli BL21 (DE3) and Pichia pastoris X-33, mutants with increased catalytic efficiency and thermotolerance
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DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis. Recombinant expression of the enzyme fused to the Trx-tag/His-tag/S-tag sequences in Escherichia coli strain BL21 (DE3), the enzyme is located in the cell lysate and the cell culture supernatant
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Pichia pastoris
expression in Pichia pastoris and Escherichia coli, recombinant enzmye expressed in Pichia pastoris shows higher specific activity
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), heterologous expression of extracellular wild-type and mutant enzymes in Pichia pastoris
expression of the His-tagged isolated catalytic domain of the enzyme, residues 31-251, in Escherichia coli strain BL21trxB(DE3) with an extra linker AGAGA at its N-terminus
expression of the N-terminally His-tagged enzyme with or without inteins, constructs for linear and circular enzymes, in Escherichia coli strains BL21(DE3) or JM109(DE3). The inteins are spliced out
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expression of wild-type enzyme and mutant circular enzyme constructs in Escherichia coli strain XL1-Blue
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gene AFUA_6G01800 or Af-egl7, DNA and amino acid sequnce determination and analysis, sequence comparisons, quantitative RT-PCR exoression analysis, recombinant expression in Escherichia coli strain Rosetta (DE3) pLysS in inclusion bodies, subcloning in Escherichia coli strain DH10beta
gene beg1, recombinant expression in Saccharomyces cerevisiae, the enzyme is secreted
gene bg1, recombinant expression in Escherichia coli and in Pichia pastoris
gene bg1314, DNA and amino acid sequence determination and analysis, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21
gene bga1, recombinant expression in Escherichia coli, the enzyme is secreted
Bacillus sp. N137
gene bgc, recombinant expression in Bacillus subtilis and in Bacillus megaterium
gene bgi, recombinant expression in Escherichia coli, the enzyme is secreted
gene bgl, recombinant expression in Escherichia coli, the enzyme is secreted
gene bgl5-1, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
gene bgl5-1, recombinant expression in Escherichia coli, the enzyme is secreted
gene bglA13, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli
gene bglA16, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli
gene bglA51, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli
gene bglBB, recombinant expression in Escherichia coli, the enzyme is secreted
gene bglM2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli
gene bglS, expression of mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme in Escherichia coli
gene bglS, recombinant expression in Escherichia coli, in Saccharomyces cerevisiae, in plants, and in mammalian cells, the enzyme is secreted
gene bglS, recombinant expression in Saccharomyces cerevisiae
gene bp_cel9A, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21
gene FSU_0226, recombinant expression in Escherichia coli and in Pichia pastoris
gene gcs2, recombinant expression in Escherichia coli, the enzyme is secreted
gene glu369, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of the extracellular enzyme in Escherichia coli TOP10 cells using vector pKJD4 also encoding the OmpA signal sequence for Escherichia coli periplasmic localization, periplasmic secretion of the recombinant OmpA-His6-tagged enzyme
gene lic16A, recombinant expression in Escherichia coli
gene LicB, expression of mature enzyme and isolated catalytic domain, as well as of the enzyme truncation mutants in Escherichia coli strain BL21
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gene licB, recombinant expression in Escherichia coli and in Pichia pastoris
gene mt-lic, genomic library screening, DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, recombinant expression in Escherichia coli strain C43(DE3)
KM079629
gene NFEg16A, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) as intracellular soluble protein
gene OsEGL1, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, functional expression od GST-tagged EGL1 in Escherichia coli
gene OsEGL2, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, functional expression of GST-tagged EGL2 in Escherichia coli
gene plicA, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, subcloning in Escherichia coli strain DH5alpha, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene PtLic16A, DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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gene RmLic16A, DNA and amino acid sequence determination and analysis, sequence comparisons
gene SU40-glu, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene US8_01508, recombinant expression in Escherichia coli, the enzyme is secreted
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gene Zobellia_2431, DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens, expression in Escherichia coli
hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, expression in Escherichia coli
hybrid from Bacillus macerans and Bacillus amyloliquefaciens, H(A16-M)
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into pET3a vector and expressed in Escherichia coli strain BL21(DE3)pLysS
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plasmid carrying the truncated 1,3-1,4-beta-D-glucanase gene in the pET26b(+) vector, transformed into Escherichia coli XL1-Blue. Overexpression of the truncated form and mutants in Escherichia coli BL21 (DE3) cells
recombinant expression and secretion from Bacillus subtilis strain WB800 using vector pP43JM2
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recombinant expression in Escherichia coli
recombinant expression in Escherichia coli and in Pichia pastoris
recombinant expression in Escherichia coli, and in Mus musculus, and in Sus scrofa parotid gland
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-beta-glucanase during germination
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wild-type and mutants cloned into vector pET26b(+) and expressed in Escherichia coli BL21 (DE3)
gene bgi, recombinant expression in Escherichia coli, the enzyme is secreted
gene bgi, recombinant expression in Escherichia coli, the enzyme is secreted
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens, expression in Escherichia coli
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hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens, expression in Escherichia coli
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hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, expression in Escherichia coli
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hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
substrate sugarcane exploded bagasse (SEB), induces Af-egl7 by 2500fold
the expression of endo-(1,3;1,4)-beta-glucanase is upregulated in response to wounding, methyl jasmonate, abscisic acid and ethephon in rice seedlings
the expression of endo-(1,3;1,4)-beta-glucanase is upregulated in response to wounding, methyl jasmonate, abscisic acid and ethephon in rice seedlings. The increase in the leaf elongation rate of rice seedlings treated under mechanical wounding is concomitant with an increase in OsEGL1 expression levels in seedling leaves, overview
substrate sugarcane exploded bagasse (SEB), induces Af-egl7 by 2500fold
substrate sugarcane exploded bagasse (SEB), induces Af-egl7 by 2500fold
Aspergillus fumigatus CBS 101355
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substrate sugarcane exploded bagasse (SEB), induces Af-egl7 by 2500fold
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substrate sugarcane exploded bagasse (SEB), induces Af-egl7 by 2500fold
Aspergillus fumigatus FGSC A1100
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substrate sugarcane exploded bagasse (SEB), induces Af-egl7 by 2500fold
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from inclusion bodies by denaturing and dialysis against Tris 10 mM, TCEP 0.1 mM, 0.05 mM EDTA, and 0.06% v/v N-lauroylsarcosine, pH 8.0, and protein refolding in 50 mM Tris, 12.5 mM cyclodextrin, and 1 mM EDTA, pH 7.5 by dialysis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
biofuel production
RuCelA can produce xylo-oligosaccharides and cell-oligosaccharides in the continuous saccharification of pretreated rice straw, which can be further degraded into fermentable sugars. Therefor, the bifunctional RuCelA distinguishes itself as an ideal candidate for industrial application
brewing
degradation
food industry
industry
nutrition
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the enzyme is able to reduce both the viscosity of the brewer mash and the filtration time, indicating its potential value for the brewing industry
synthesis
additional information
agriculture
1,3-1,4-beta-D-glucanase are widely used as a feed additive to help non-ruminant animals digest plant fibers, with potential in increasing nutrition turnover rate and reducing sanitary problems
agriculture
overexpression of barley (1->3,1->4)-beta-glucanase isoenzyme EII under the control of a promoter of barley D-Hordein gene Hor3-1 in barley cultivar Golden Promise. The T2 generation of transgenic lines shows increased activity of glucanase in grains. Total beta-glucan content is reduced by more than 95.73% in transgenic grains compared with the wild-type control. Overexpression leads to an increase in 1000-grain weight, which might be due to elevated amounts of starch in the grain
agriculture
enzyme shows the ability to inhibit the growth of phytopathogenic fungus Alternaria alternata
analysis
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the enzyme is used for oligosaccharide profiling of mixed-linkage glucan, beta-1,3-1,4-glucan, a characteristic hemicellulose in primary cell walls of grasses, that adsorps onto microcrystalline cellulose in a slow, irreversible, and temperature-dependent manner. The binding of the oligomer is reduced if the cellulose samples are first treated with certain cell wall polysaccharides, such as xyloglucan and glucuronoarabinoxylan
analysis
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assay procedure for the measurement of beta-glucanase and lichenase in crude enzyme extracts. Substrate 4,6-O-benzylidene-2-chloro-4-nitrophenyl-beta-3'-cellotriosyl-beta-glucopyranoside is a more generally applicable reagent. Standard curves allow the assay absorbance response to be directly converted to beta-glucanase/lichenase activity on barley beta-glucan. Manual and automated assay formats aloow the analysis of beta-glucanase in malt flour and lichenase enzyme extracts and the assays are repeatable
brewing
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the enzyme is a candidate for the production of beta-gluco-oligosaccharides and in brewing industry
brewing
Paenibacillus barengoltzii CAU904
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the enzyme is a candidate for the production of beta-gluco-oligosaccharides and in brewing industry
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degradation
hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilizedon commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed
degradation
the saccharification of untreated reed and rice straw powders by commercial enzymes (Celluclast 1.5 L and Novozym 188) is increased by 10.4 and 4.8%, respectively, by the addition of BGlc8H. In the presence of Ca2+ and BGlc8H, the saccharification of the pretreated reed and rice straw powders by the commercial enzymes is increased by 18.5 and 11.7%, respectively
degradation
fermentation capacity of recombinant Bacillus subtilis expressing mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P reaches 242.02 U ml/h. The addition of the mutant protein in Congress mashing significantly reduces the filtration time and viscosity of mash by 29.7% and 12.3%, respectively
degradation
Acetivibrio thermocellus DSM 1237
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hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilizedon commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed
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degradation
Bacillus tequilensis CGX 5-2
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fermentation capacity of recombinant Bacillus subtilis expressing mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P reaches 242.02 U ml/h. The addition of the mutant protein in Congress mashing significantly reduces the filtration time and viscosity of mash by 29.7% and 12.3%, respectively
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food industry
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the enzyme is a good candidate in the malting and brewing industry reducing the filtration time and viscosity of mash from barley grains, overview
food industry
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the enzyme is considered as a candidate for application particularly in the animal feed industry
food industry
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the secretively produced beta-1,3-1,4-glucanase shows excellent thermostability up to 80°C and a wide pH range from pH 4 to pH 11 and has a potential in the food and animal feed applications
food industry
the thermostable enzyme can be useful in mashing at 72°C of brewing processes
food industry
-
enzyme can promote mashing with a reduced filtration time (14.0%) and viscosity (3.4%)
food industry
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exogenous 1,3-1,4-beta-glucanases but not 1,4-beta-glucanases (EC 3.2.1.4) are obligatory enzymes to improve the nutritive value of barley-based diets for broilers. Enzyme is completely resistant to proteolytic inactivation after a 30 min incubation with pancreatic proteases
food industry
the addition of mutant K20S/N31c/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P in congress mashing decreases the filtration time and viscosity by 21.3 and 9.6 %, respectively
food industry
the enzyme is used for production and processing of alcoholic beverages
food industry
the enzyme is used for production of oligomers as prebiotics
food industry
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the thermostable enzyme can be useful in mashing at 72°C of brewing processes
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food industry
Acetivibrio thermocellus DSM 1237
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the secretively produced beta-1,3-1,4-glucanase shows excellent thermostability up to 80°C and a wide pH range from pH 4 to pH 11 and has a potential in the food and animal feed applications
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food industry
Paenibacillus barengoltzii CAU904
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enzyme can promote mashing with a reduced filtration time (14.0%) and viscosity (3.4%)
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food industry
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the enzyme is considered as a candidate for application particularly in the animal feed industry
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food industry
Bacillus subtilis NCIB 8565
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the enzyme is used for production and processing of alcoholic beverages
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food industry
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the enzyme is used for production of oligomers as prebiotics
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food industry
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the enzyme is a good candidate in the malting and brewing industry reducing the filtration time and viscosity of mash from barley grains, overview
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industry
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properties make the enzyme highly suitable for industrial applications
industry
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properties make the enzyme highly suitable for industrial applications
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synthesis
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the unusually resistance against inactivation by heat, ethanol or ionic detergents makes the enzyme highly suitable for industrial application in the mashing process of beer brewing
synthesis
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
synthesis
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
synthesis
over-expression in Pichia pastoris, with a yield of about 1000 U/ml in a 3.7 l fermentor
synthesis
upon expression in Pichia pastoirs as active extracellular beta-1,3-1,4-glucanase, the recombinant protein is secreted predominantly into the medium and comprises up to 85% of the total extracellular proteins and reaches a protein concentration of 9.1 g/l with an activity of 55,300 U/ml in 5-l fermentor culture
synthesis
analysis of fermentation conditions for beta-1,3-1,4-glucanase production under solid-state fermentation. Under the optimized fermentation conditions, viz. oatmeal as sole carbon source, 5% (w/w) peptone as sole nitrogen source, initial moisture of 80% (w/w), initial culture pH of 5.0, incubation temperature of 50°C and incubation time of 6 days, the highest beta-1,3-1,4-glucanase activity of 20025 U/g dry substrate is achieved. The addition of the purified beta-1,3-1,4-glucanase in mash obviously reduces its filtration time (24.6%) and viscosity (2.61%)
synthesis
expression of mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P in Bacillus subtilis to maximal extracellular activity of 4840.4 U/ml
synthesis
immobilization of enzyme on porous silica using glutaraldehyde. Enzyme activity decreases sharply at high concentrations of glutaraldehyde. Immobilized protein is stable over a wide range of pH and can be stored long term at 4°C. After 10 cycles, the enzyme retains 42% of its initial catalytic activity
synthesis
the enzyme can be used in the production of anti-hypercholesterolemic agents
synthesis
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analysis of fermentation conditions for beta-1,3-1,4-glucanase production under solid-state fermentation. Under the optimized fermentation conditions, viz. oatmeal as sole carbon source, 5% (w/w) peptone as sole nitrogen source, initial moisture of 80% (w/w), initial culture pH of 5.0, incubation temperature of 50°C and incubation time of 6 days, the highest beta-1,3-1,4-glucanase activity of 20025 U/g dry substrate is achieved. The addition of the purified beta-1,3-1,4-glucanase in mash obviously reduces its filtration time (24.6%) and viscosity (2.61%)
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synthesis
Niallia circulans ATCC 21367
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the enzyme can be used in the production of anti-hypercholesterolemic agents
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synthesis
Bacillus tequilensis CGX 5-2
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expression of mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P in Bacillus subtilis to maximal extracellular activity of 4840.4 U/ml
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additional information
the alkaline beta-1,3-1,4-glucanase may have potential in industrial applications, such as detergent, paper and pulp industries
additional information
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the alkaline beta-1,3-1,4-glucanase may have potential in industrial applications, such as detergent, paper and pulp industries
additional information
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
Bacillus sp. N137
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
additional information
upon addition to a commercial cellulase cocktail, Af-EGL7 significantly improves sugarcane exploded bagasse (SEB) saccharification, which suggests that enzyme Af-EGL7 has great potential to hydrolyze complex biomass. Af-EGL7 is a promising candidate to enhance enzyme cocktails used in biorefineries such as consolidated bioprocessing
additional information
-
upon addition to a commercial cellulase cocktail, Af-EGL7 significantly improves sugarcane exploded bagasse (SEB) saccharification, which suggests that enzyme Af-EGL7 has great potential to hydrolyze complex biomass. Af-EGL7 is a promising candidate to enhance enzyme cocktails used in biorefineries such as consolidated bioprocessing
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
Acetivibrio thermocellus DSM 1237
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
Acetivibrio thermocellus NBRC 103400
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
Aspergillus fumigatus CBS 101355
-
upon addition to a commercial cellulase cocktail, Af-EGL7 significantly improves sugarcane exploded bagasse (SEB) saccharification, which suggests that enzyme Af-EGL7 has great potential to hydrolyze complex biomass. Af-EGL7 is a promising candidate to enhance enzyme cocktails used in biorefineries such as consolidated bioprocessing
-
additional information
Bacillus subtilis NCIB 8565
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
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additional information
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upon addition to a commercial cellulase cocktail, Af-EGL7 significantly improves sugarcane exploded bagasse (SEB) saccharification, which suggests that enzyme Af-EGL7 has great potential to hydrolyze complex biomass. Af-EGL7 is a promising candidate to enhance enzyme cocktails used in biorefineries such as consolidated bioprocessing
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additional information
Niallia circulans ATCC 21367
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
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additional information
Rhodothermus marinus ITI378
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
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additional information
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
-
additional information
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
Acetivibrio thermocellus VPI 7372
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
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additional information
Bacillus pumilus US570
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
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additional information
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
Aspergillus fumigatus FGSC A1100
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upon addition to a commercial cellulase cocktail, Af-EGL7 significantly improves sugarcane exploded bagasse (SEB) saccharification, which suggests that enzyme Af-EGL7 has great potential to hydrolyze complex biomass. Af-EGL7 is a promising candidate to enhance enzyme cocktails used in biorefineries such as consolidated bioprocessing
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
-
additional information
-
upon addition to a commercial cellulase cocktail, Af-EGL7 significantly improves sugarcane exploded bagasse (SEB) saccharification, which suggests that enzyme Af-EGL7 has great potential to hydrolyze complex biomass. Af-EGL7 is a promising candidate to enhance enzyme cocktails used in biorefineries such as consolidated bioprocessing
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
-
additional information
Acetivibrio thermocellus NCIMB 10682
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
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additional information
Acetivibrio thermocellus NRRL B-4536
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
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additional information
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the alkaline beta-1,3-1,4-glucanase may have potential in industrial applications, such as detergent, paper and pulp industries
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Release 2023.1 (January 2023)
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