Information on EC 3.2.1.73 - licheninase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
3.2.1.73
-
RECOMMENDED NAME
GeneOntology No.
licheninase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
show the reaction diagram
-
-
-
-
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
show the reaction diagram
mechanism, kinetic model
-
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
show the reaction diagram
allosteric activation mechanism, feedback inhibition
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(1,3)(1,4)-beta-D-glucan-4-glucanohydrolase
-
-
(1->3,1->4)-beta-glucanase isoenzyme EII
-
-
-
-
1,3-1,4-beta-D-glucan 4-glucanohydrolase
-
-
-
-
1,3-1,4-beta-D-glucan 4-glucanohydrolase
-
-
1,3-1,4-beta-D-glucan 4-glucanohydrolase
Bacillus subtilis A3
-
-
-
1,3-1,4-beta-D-glucan 4-glucanohydrolase
-
-
1,3-1,4-beta-D-glucan glucanohydrolase
-
-
-
-
1,3-1,4-beta-D-glucan-4-glucano hydrolase
-
-
1,3-1,4-beta-D-glucan-4-glucano hydrolase
Bacillus subtilis GN156
-
-
-
1,3-1,4-beta-D-glucanase
-
-
1,3-1,4-beta-D-glucanase
Bacillus subtilis A3
-
-
-
1,3-1,4-beta-D-glucanase
-
-
1,3-1,4-beta-D-glucanase
Clostridium thermocellum ZJL4
-
-
-
1,3-1,4-beta-D-glucanase
-
-
1,3-1,4-beta-glucanase
-
-
1,3-1,4-beta-glucanase
-
-
1,3-1,4-beta-glucanase
-
-
1,3-1,4-beta-glucanase
-
-
1,3;1,4-beta-glucan 4-glucanohydrolase
-
-
-
-
1,3;1,4-beta-glucan endohydrolase
-
-
-
-
beta-(1,3-1,4)-glucanase
-
-
beta-(1,3-1,4)-glucanase
Aspergillus niger A-25
-
-
-
beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase
-
-
-
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
Bacillus licheniformis EGW039, Bacillus licheniformis EGW039(CGMCC
-
-
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
Bacillus subtilis GN156
-
-
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
-
-
beta-1-3, 1-4 glucan 4-glucanohydrolase
Thermomonospora sp.
-
-
beta-glucanase
-
-
beta-glucanase
-
-
beta-glucanase
Hypocrea koningii ZJU-T
-
-
-
beta-glucanase
-
-
beta-glucanase
-
-
bifunctional xylanase/endoglucanase
E2DQY5
RuCelA, a bifunctional xylanase/endoglucanase, EC 3.2.1.8 and EC 3.2.1.73
endo-(1,3;1,4)-beta-glucanase
Q8S9P4
-
endo-(1,3;1,4)-beta-glucanase
Q5UAW3
-
Endo-beta-1,3-1,4 glucanase
-
-
-
-
endo-beta-1,3-1,4-glucanase
-
-
Endoglucanase
E2DQY5
-
Fsbeta-glucanase
-
-
GHF16 TFsbeta-glucanase
-
-
GHF17 barley 1,3-1,4-beta-D-glucanase
-
-
GluIII
Aspergillus niger A-25
-
-
-
H(A16-M)
-
-
laminarinase
-
-
-
-
Lic16A
E0XN39
-
Lichenase
-
-
-
-
Lichenase
Bacillus subtilis A3
-
-
-
Lichenase
Clostridium thermocellum ZJL4
-
-
-
Lichenase
-
-
Lichenase
-
the multifunctional enzyme domain GH44 possesses cellulase, xylanase, and lichenase activities
Lichenase
Paenibacillus polymyxa GS01
-
the multifunctional enzyme domain GH44 possesses cellulase, xylanase, and lichenase activities
-
Lichenase
-
-
LicMB
Clostridium thermocellum ZJL4
-
-
-
mHG
Bacillus subtilis A3
-
-
-
Mixed linkage beta-glucanase
-
-
-
-
RuCelA
E2DQY5
gene name
TF-glucanase
P17989
-
XynIII
-
bifunctional xylanase showing also beta-(1,3-1,4)-glucanase activity
XynIII
Aspergillus niger A-25
-
bifunctional xylanase showing also beta-(1,3-1,4)-glucanase activity
-
CAS REGISTRY NUMBER
COMMENTARY
37288-51-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain A-25
-
-
Manually annotated by BRENDA team
Aspergillus niger A-25
strain A-25
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
strain EGW039 (CGMCC 0635)
-
-
Manually annotated by BRENDA team
strain EGW039(CGMCC 0635)
-
-
Manually annotated by BRENDA team
Bacillus licheniformis EGW039
strain EGW039 (CGMCC 0635)
-
-
Manually annotated by BRENDA team
Bacillus licheniformis EGW039(CGMCC
strain EGW039(CGMCC 0635)
-
-
Manually annotated by BRENDA team
hybrid from B. macerans and B. amyloliquefaciens
-
-
Manually annotated by BRENDA team
IMET B 376
-
-
Manually annotated by BRENDA team
strain A3
-
-
Manually annotated by BRENDA team
strain GN156
-
-
Manually annotated by BRENDA team
Bacillus subtilis A3
strain A3
-
-
Manually annotated by BRENDA team
Bacillus subtilis A8-8
-
-
-
Manually annotated by BRENDA team
Bacillus subtilis GN156
strain GN156
-
-
Manually annotated by BRENDA team
Bispora sp.
-
UniProt
Manually annotated by BRENDA team
strain ZJL4, gene LicB
-
-
Manually annotated by BRENDA team
Clostridium thermocellum ZJL4
strain ZJL4, gene LicB
-
-
Manually annotated by BRENDA team
isoenzyme I and II
-
-
Manually annotated by BRENDA team
strain ZJU-T
-
-
Manually annotated by BRENDA team
Hypocrea koningii ZJU-T
strain ZJU-T
-
-
Manually annotated by BRENDA team
var. miniatus
-
-
Manually annotated by BRENDA team
Orpinomyces sp.
strain PC-2
-
-
Manually annotated by BRENDA team
L. cv. Kirara 397
-
-
Manually annotated by BRENDA team
OsEGL2; cv. Yukihikari, gene OsEGL2
UniProt
Manually annotated by BRENDA team
OsEGL1; cv. Yukihikari, gene OsEGL1
UniProt
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes W101F, W101Y, E103D, E103Q, D105N, D105K, E107D, E107Q, and E107H
-
-
Manually annotated by BRENDA team
strain GS01
-
-
Manually annotated by BRENDA team
Paenibacillus polymyxa GS01
strain GS01
-
-
Manually annotated by BRENDA team
variant microsporus
-
-
Manually annotated by BRENDA team
cultivar Musketeer
Uniprot
Manually annotated by BRENDA team
Thermomonospora sp.
-
-
-
Manually annotated by BRENDA team
strain MSB8
-
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1-3,1-4)-beta-D-glucan + H2O
?
show the reaction diagram
-
i.e. barley (1-3,1-4)-beta-glucan
-
-
?
1,3-1,4-beta-D-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
1,3-1,4-beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
-
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
show the reaction diagram
-
-
-
-
-
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucopyranoside + H2O
4-methylumbelliferone + 3-O-beta-cellobiosyl-beta-D-glucopyranoside
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
4-methylumbelliferone + 3-O-beta-cellobiosyl-beta-D-glucose
show the reaction diagram
-
-
-
-
?
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-
show the reaction diagram
-
-
-
-
-
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-
show the reaction diagram
-
-
-
-
-
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-
show the reaction diagram
-
-
-
-
-
4-methylumbelliferyl cellobiose + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl laminaribiose + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-(1,3)-beta-D-glucooligosaccharides + H2O
4-methylumbelliferol + beta-D-oligosaccharides
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-Gal-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
?
show the reaction diagram
-
Gal substrate has a 1.3fold higher kcat/KM-value than Glc substrate
-
-
r
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc + H2O
4-methylumbelliferone + beta-D-Glc-(1-3)-beta-D-Glc
show the reaction diagram
-
-
-
-
-
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
show the reaction diagram
-
-
-
-
-
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
?
show the reaction diagram
-
Gal substrate has a 1.3fold higher kcat/KM-value than Glc substrate
-
-
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
show the reaction diagram
-
-
-
-
-
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
show the reaction diagram
-
-
-
-
-
4-nitrophenyl beta-D-cellobioside + H2O
?
show the reaction diagram
-
1% of the activity with carboxymethyl-cellulose
-
-
?
4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-2-deoxy-beta-D-erythro-pentopyranoside + H2O
?
show the reaction diagram
-
2-deoxy analog is better substrate than corresponding 2-hydroxy substrate
-
-
?
4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-arabinopyranoside + H2O
?
show the reaction diagram
-
2-deoxy analog is better substrate than corresponding 2-hydroxy substrate
-
-
?
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-
show the reaction diagram
-
-
-
-
-
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-
show the reaction diagram
-
-
-
-
-
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-glucopyranoside
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
show the reaction diagram
-
-
-
-
-
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-xylopyranoside
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Xyl + F-
show the reaction diagram
-
-
-
-
-
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-
show the reaction diagram
-
-
-
-
-
alpha-laminaribiosyl fluoride + 4-nitrophenyl-beta-D-glucopyranoside
4-nitrophenyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
show the reaction diagram
-
-
-
-
-
alpha-laminaribiosyl fluoride + 4-nitrophenyl-beta-D-xylopyranoside
4-nitrophenyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Xyl + F-
show the reaction diagram
-
-
-
-
-
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-
show the reaction diagram
-
-
-
-
-
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-
show the reaction diagram
-
-
-
-
-
arabinoxylan + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis A8-8
-
50% of the activity with carboxymethyl-cellulose
-
-
?
barley beta-D-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
P17989
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
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
?
show the reaction diagram
Hypocrea koningii ZJU-T
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Bacillus licheniformis EGW039(CGMCC
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Bacillus licheniformis EGW039
-
-
-
-
?
barley beta-glucan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose + ?
show the reaction diagram
-
-
-
-
?
beta-(1-3),(1-4)-D-glucan + H2O
beta-D-glucose + ?
show the reaction diagram
-
-
-
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
-
from Hordeum vulgare, from Hordeum vulgare, best substrate
-
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
E0XN39
source of substrate: barley
-
-
?
beta-1,3/1,4-glucan + H2O
?
show the reaction diagram
Q5UAW3
best substrate is 1,3/1,4-beta-glucan from Hordeum vulgare, and almost equally active from Avena sativa
-
-
?
beta-D-glucan + H2O
?
show the reaction diagram
-
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
-
-
?
beta-D-glucan + H2O
?
show the reaction diagram
Q84F88
source of substrate: oat
-
-
?
beta-D-glucan + H2O
?
show the reaction diagram
Q84C00
source of substrate: oat
-
-
?
beta-D-glucan + H2O
?
show the reaction diagram
Bispora sp.
D2DRB6
source: barley, best substrate
hydrolysis products from barley beta-glucan are 6.8 micromol/ml glucose and 16.3 micromol/ml cellobiose
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
Bispora sp.
D2DRB6
9.8% of the activity with beta-D-glucan
-
-
?
carboxymethyl-cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethyl-cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethyl-cellulose + H2O
?
show the reaction diagram
-
a negligible amount of hydrolysis of carboxymethyl-cellulose is observed
-
-
?
carboxymethyl-cellulose + H2O
?
show the reaction diagram
Hypocrea koningii ZJU-T
-
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
E2DQY5
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
18% of the activity with beta-1,3-1,4-glucan from Hordeum vulgare
-
-
?
cellulose + H2O
?
show the reaction diagram
-
7% of the activity with beta-1,3-1,4-glucan from Hordeum vulgare
-
-
?
cellulose + H2O
?
show the reaction diagram
E2DQY5
filter paper
main products are cellobiose and cellotriose
-
?
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
show the reaction diagram
-
-
-
-
?
Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-3)Glcbeta(1-4)Glcbeta(1-4)Glc-OMe + H2O
?
show the reaction diagram
-
-
-
-
?
Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-3)Glc + H2O
?
show the reaction diagram
-
-
-
-
?
Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta-O-4-methylumbeliferone + H2O
?
show the reaction diagram
-
-
-
-
?
Glcbeta3Glcbeta-methylumbelliferone + H2O
?
show the reaction diagram
-
-
-
-
?
hydroxyethylcellulose + H2O
?
show the reaction diagram
E2DQY5
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
Q1EMA6
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis A8-8
-
70% of the activity with carboxymethyl-cellulose
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
-
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Q84F88
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Q84C00
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
85% of the activity with beta-1,3-1,4-glucan from Hordeum vulgare
-
-
?
lichenan + H2O
?
show the reaction diagram
Q5UAW3
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
?
show the reaction diagram
-, Q8S9P4
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
?
show the reaction diagram
-
500% of the activity with carboxymethyl-cellulose
-
-
?
lichenan + H2O
?
show the reaction diagram
E0XN39
68.8% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
show the reaction diagram
Bispora sp.
D2DRB6
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
?
show the reaction diagram
Paenibacillus polymyxa GS01
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus licheniformis EGW039(CGMCC
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus subtilis A8-8
-
500% of the activity with carboxymethyl-cellulose
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus licheniformis EGW039
-
-
-
-
?
lichenan + H2O
D-glucose + ?
show the reaction diagram
Thermomonospora sp.
-
-
-
-
?
lichenan + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
reducing sugar + ?
show the reaction diagram
Hypocrea koningii, Hypocrea koningii ZJU-T
-
-
-
-
?
lichenan + H2O
reducing sugar + ?
show the reaction diagram
Bacillus subtilis A3
-
-
-
-
?
lichenin + H2O
?
show the reaction diagram
-
-
-
-
?
lichenin + H2O
?
show the reaction diagram
-
-
-
-
?
lichenin + H2O
?
show the reaction diagram
Aspergillus niger A-25
-
-
-
-
?
xylan + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis A8-8
-
500% of the activity with carboxymethyl-cellulose
-
-
?
xylan + H2O
xylose + ?
show the reaction diagram
Thermomonospora sp.
-
-
-
-
?
barley beta-glucan + H2O
beta-glucan oligosaccharides
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
additional information
-
-
-
pentose, triose, tetarose and a high molecular weight polysaccharide with 1,3 linkage, pentose, triose, tetrose and a high molecular weight polysaccharide with 1,3 linkage
-
?
barley beta-glucan + H2O
additional information
-
Bacillus subtilis GN156
-
-
pentose, triose, tetarose and a high molecular weight polysaccharide with 1,3 linkage, pentose, triose, tetrose and a high molecular weight polysaccharide with 1,3 linkage
-
?
beta-1,3/1,4-glucan + H2O
?
show the reaction diagram
-, Q8S9P4
best substrate is 1,3/1,4-beta-glucan from Hordeum vulgare, and almost equally active from Avena sativa
-
-
?
beta-D-glucan + H2O
additional information
-
-
-
-
-
?
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
-
Orpinomyces sp.
-
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
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from oat
oligosaccharides are formed as the major products, no glucose
?
beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethyl beta-glucan + H2O
additional information
-
-
carboxymethyl beta-glucan from barley
trisaccharide, 53%, tetrasaccharide, 25%
?
lichenan + H2O
lichenan oligosaccharides
show the reaction diagram
-
-
-
-
?
lichenin + H2O
additional information
-
-
-
-
-
?
lichenin + H2O
additional information
-
-
-
-
-
?
lichenin + H2O
additional information
-
-
-
-
-
?
lichenin + H2O
additional information
-
-
-
-
-
?
lichenin + H2O
additional information
-
-
-
-
-
?
lichenin + H2O
additional information
-
-
-
-
-
?
lichenin + H2O
additional information
-
Orpinomyces sp.
-
-
main products are triose and tetraose
?
lichenin + H2O
additional information
-
-
lichenin from Cetralia islandica and from Usnea barbata
-
-
?
lichenin + H2O
?
show the reaction diagram
Clostridium thermocellum ZJL4
-
-
-
-
?
additional information
?
-
-
no hydrolysis of carboxymethylpachyman
-
-
-
additional information
?
-
-
no hydrolysis of carboxymethylpachyman, no hydrolysis of starch, no hydrolysis of xylan
-
-
-
additional information
?
-
Orpinomyces sp.
-
no hydrolysis of xylan
-
-
-
additional information
?
-
-
no hydrolysis of laminarin
-
-
-
additional information
?
-
-
no hydrolysis of laminarin
-
-
-
additional information
?
-
-
no hydrolysis of laminarin
-
-
-
additional information
?
-
Orpinomyces sp.
-
no hydrolysis of laminarin
-
-
-
additional information
?
-
-
no hydrolysis of laminaran
-
-
-
additional information
?
-
-
no hydrolysis of carboxymethylcellulose
-
-
-
additional information
?
-
-
no hydrolysis of carboxymethylcellulose
-
-
-
additional information
?
-
-
no hydrolysis of carboxymethylcellulose
-
-
-
additional information
?
-
-
no hydrolysis of carboxymethylcellulose
-
-
-
additional information
?
-
Orpinomyces sp.
-
no hydrolysis of carboxymethylcellulose
-
-
-
additional information
?
-
-
no hydrolysis of pustulan
-
-
-
additional information
?
-
Orpinomyces sp.
-
no hydrolysis of pustulan
-
-
-
additional information
?
-
-
no activity against beta-1,4- or beta-1,3 homopolymers of gluco- or manno-configured polysaccharides
-
-
-
additional information
?
-
-
activity against 1% carboxymethylcellulose is not observed
-
-
-
additional information
?
-
-
carboxymethylcellulose and arabinoxylan are no substrates
-
-
-
additional information
?
-
-
carboxymethylcellulose and starch are no substrates
-
-
-
additional information
?
-
-
carboxymethylcellulose, arabinoxylan, laminarin, and starch are no substrates
-
-
-
additional information
?
-
-
does not display any activity on crystalline cellulose or laminarin
-
-
-
additional information
?
-
-
does not hydrolyze carboxymethyl-cellulose or avicel cellulose
-
-
-
additional information
?
-
-
no activity on cellulose
-
-
-
additional information
?
-
Thermomonospora sp.
-
no activity towards avicel, laminarin, gum arabic, p-nitrophenyl glucoside, and p-nitrophenyl xylopyranoside
-
-
-
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
?
-
-
the purified enzyme fraction shows no activity on laminarin and xylan
-
-
-
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
?
-
-
does not hydrolyze laminaripentaose and cellopentaose
-
-
-
additional information
?
-
-
no activity against carboxymethylcellulose, xylan, laminarin, dextrin
-
-
-
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
?
-
-
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
?
-
Q5UAW3
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
?
-
-, Q8S9P4
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
?
-
Q84F88
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
-
additional information
?
-
Q84C00
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
-
additional information
?
-
-
no substrate: cellobiose
-
-
-
additional information
?
-
Bispora sp.
D2DRB6
poor substrates: laminarin, oat spelt xylan. No substrate: avicel
-
-
-
additional information
?
-
E0XN39
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
?
-
E2DQY5
no activitiy using beta-1,3-glucan, laminarin, or Avicel as substrates
-
-
-
additional information
?
-
Aspergillus niger A-25
-
does not hydrolyze carboxymethyl-cellulose or avicel cellulose
-
-
-
additional information
?
-
Hypocrea koningii ZJU-T
-
the purified enzyme fraction shows no activity on laminarin and xylan
-
-
-
additional information
?
-
Bacillus licheniformis EGW039(CGMCC
-
no activity on cellulose
-
-
-
additional information
?
-
Clostridium thermocellum ZJL4
-
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
?
-
Bacillus subtilis A8-8
-
no substrate: cellobiose
-
-
-
additional information
?
-
Bacillus licheniformis EGW039
-
activity against 1% carboxymethylcellulose is not observed
-
-
-
additional information
?
-
Bacillus subtilis GN156
-
no activity against carboxymethylcellulose, xylan, laminarin, dextrin
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
-
from Hordeum vulgare
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
Clostridium thermocellum, Clostridium thermocellum ZJL4
-
lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
necessary for the activity of the enzyme
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
Co2+
-
activates at 10 mM
Co2+
-
9% activation at 1 mM
Co2+
-
5 mM, 160% of initial activity
Co2+
E2DQY5
10 mM, activity increased to 154%
Cu2+
-
0.3% residual activity at 12 mM
Cu2+
-
110.11% activity at 1 mM
Cu2+
E2DQY5
10 mM, activity decreased to 86%
Fe2+
-
activates at 10 mM
Fe2+
-
20.8% increase of activity at 1 mM
Fe3+
-
89.6% residual activity at 12 mM
K+
-
115.73% activity at 1 mM
Li+
-
103.25% activity at 1 mM
Mg2+
-
95.2% residual activity at 12 mM
Mg2+
-
5.3% increase of activity at 1 mM
Mg2+
E2DQY5
10 mM, activity decreased to 85%
Mn2+
-
activates at 10 mM
Mn2+
-
62.3% residual activity at 12 mM
Ni2+
-
19% activation at 1 mM
Zn2+
-
65% residual activity at 12 mM
Mn2+
-
5 mM, 152% of initial activity
additional information
-
shows no sensitivity to Ca2+ and Al3+
additional information
-
Ca2+ stabilizes the enzyme at higher temperatures
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(3,4)-epoxybutyl beta-D-cellobioside
-
identification of Glu105 at the active site
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
-
2,4,6-Trinitrobenzenesulfonic acid
Thermomonospora sp.
-
-
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
2-mercaptoethanol
-
10 mM, 28% inhibition
2-mercaptoethanol
-
inhibits activity at a concentration of 5%
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
4-methylumbelliferyl-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-(1-3)-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
-
-
5,5'-dithiobis 2-nitrobenzoic acid
Thermomonospora sp.
-
-
-
Ag+
-
inhibits the enzyme activity at 4 mM by 56.9%
Ag+
Bispora sp.
D2DRB6
strong inhibition
Ba2+
-
8% inhibition at 1 mM
beta-mercaptoethanol
-
inhibits the enzyme activity at 4 mM by 82.7%
Ca2+
-
78.65% residual activity at 1 mM
Ca2+
-
90.98% residual activity at 1 mM
Ca2+
-
partially inhibited
Ca2+
-
inhibits the enzyme activity at 4 mM by 55.5%
Ca2+
-
noncompetitive
CaCl2
-
10 mM, 33% inhibition
Co2+
-
82.19% residual activity at 1 mM
Cu2+
-
91.01% residual activity at 0.5 mM
Cu2+
-
44% residual activity at 1 mM
Cu2+
-
partially inhibited
Cu2+
-
completely inhibits the enzyme activity at 4 mM
Cu2+
-
14% inhibition at 1 mM
dithiothreitol
-
1 mM, 21% inhibition
DTT
-
inhibits the enzyme activity at 4 mM by 82.3%
EDTA
-
10 mM, 18% inhibition
EDTA
-
47.3% residual activity at 60 mM
EDTA
-
79.64% residual activity at 1 mM
EDTA
-
inhibits the enzyme activity at 4 mM by 43.4%
EDTA
Bispora sp.
D2DRB6
strong inhibition
EDTA
-
12% inhibition at 1 mM
epoxyalkyl cellobiosides
-
irreversible active-site directed inactivation, stereospecific requirements for inhibition
-
Fe2+
-
84.27% residual activity at 1 mM
-
Fe2+
-
slightly inhibited
-
Fe2+
-
inhibits the enzyme activity at 4 mM by 14.9%
-
Fe3+
-
93.26% residual activity at 1 mM
-
Fe3+
-
inhibits the enzyme activity at 4 mM by 13.5%
-
Fe3+
-
5 mM, 58% of initial activity
-
Glc-beta-1,3-isofagomine
-
-
glucono-delta-lactone
-
-
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
completely inhibits the enzyme activity at 4 mM
Hg2+
Bispora sp.
D2DRB6
strong inhibition
imidazole
-
competitive
K+
-
95.61% residual activity at 1 mM
Li+
-
66.29% residual activity at 0.5 mM
Mg2+
-
78.65% residual activity at 0.5 mM
Mg2+
-
slightly inhibited
Mg2+
-
inhibits the enzyme activity at 4 mM by 52.9%
Mg2+
-
8% inhibition at 1 mM
Mn2+
-
77.53% residual activity at 1 mM
Mn2+
-
37.29% residual activity at 1 mM
Mn2+
-
partially inhibited
Mn2+
-
completely inhibits the enzyme activity at 4 mM
Na+
-
inhibits the enzyme activity at 4 mM by 47.3%; inhibits the enzyme activity at 4 mM by 80.3%
Ni2+
-
inhibits the enzyme activity at 4 mM by 11.5%
o-phthaldehyde
Thermomonospora sp.
-
-
Pb2+
-
97.75% residual activity at 0.5 mM
Pb2+
-
79.29% residual activity at 1 mM
SDS
-
100 mM, 28% inhibition
SDS
-
inhibits activity at a concentration of 5%
SDS
-
inhibits the enzyme activity at 4 mM by 88.2%
Sodium dodecyl sulfate
Bispora sp.
D2DRB6
strong inhibition
Sr2+
-
inhibits the enzyme activity at 4 mM by 49%
Urea
-
14.5% residual activity at 7 mM
Zn2+
-
69.66% residual activity at 0.5 mM
Zn2+
-
88.66% residual activity at 1 mM
Zn2+
-
partially inhibited
Zn2+
-
inhibits the enzyme activity at 4 mM by 11.6%
Zn2+
-
8% inhibition at 1 mM
Mn2+
-
67% inhibition at 1 mM
additional information
-
no inhibition up to a concentration of 10% SDS-PAGE
-
additional information
-
resistent to trypsin protease digestion
-
additional information
-
no significant effects are found for Ca2+, Mg2+, glycerol, D-sorbitol, boric acid, and EDTA
-
additional information
-
not inhibited by Li+; not inhibited by Li+, not significantly by Fe2+
-
additional information
-
substrate inhibition for 4-methylumbelliferyl laminaribiose, but not for 4-methylumbelliferyl cellobiose
-
additional information
-
no inhibition by Ca2+ and Fe2+ at 1 mM
-
additional information
-
not inhibitory: EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Avicel
-
mutants show higher levels of activity compared to wild type
-
beet pulp
-
mutants show higher levels of activity compared to wild type
-
beta-mercaptoethanol
-
0.1%
N-bromosuccinimide
-
-
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
-
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 50C for 4 days
-
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.7
-
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
0.7
-
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
0.37
-
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
-
pH 6.9, 30C
0.5
-
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
-
pH 7.2, 30C
0.6
-
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
-
pH 7.8, 30C
0.058
-
4-methylumbelliferyl cellobiose
-
-
0.19
-
4-methylumbelliferyl laminaribiose
-
-
1
-
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
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, 30C
1.36
-
beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35C
0.34
-
beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35C
5.3
-
Glcbeta3Glcbeta-methylumbelliferone
-
pH 7.0, 37C, 50 mM sodium phosphate buffer
2.29
-
Laminarin
-
Y123F, mg/ml
3.82
-
Laminarin
-
E131Q, mg/ml
3.9
-
Laminarin
-
Y123A, mg/ml
4.05
-
Laminarin
-
Y24W, mg/ml
4.42
-
Laminarin
-
E63Q, mg/ml
5.41
-
Laminarin
-
H99D, mg/ml
5.61
-
Laminarin
-
S90A, mg/ml
5.76
-
Laminarin
-
A98W, mg/ml
5.88
-
Laminarin
-
Y24A, mg/ml
6.1
-
Laminarin
-
W192A, mg/ml
6.18
-
Laminarin
-
R65A, mg/ml
6.73
-
Laminarin
-
wild type, mg/ml
7.19
-
Laminarin
-
W184Y, mg/ml
9.1
-
Laminarin
-
E63D, mg/ml
9.46
-
Laminarin
-
Y24F, mg/ml
11.1
-
Laminarin
-
H99R, mg/ml
14.7
-
Laminarin
-
N26A, mg/ml
0.13
-
lichenan
-
Y123A, mg/ml
0.14
-
lichenan
-
Y24W, mg/ml
0.16
-
lichenan
-
Y123F, mg/ml
0.26
-
lichenan
-
H99D, mg/ml
0.33
-
lichenan
-
S90A, mg/ml
0.45
-
lichenan
-
wild type, mg/ml
0.61
-
lichenan
-
A98W, mg/ml
0.68
-
lichenan
-
W184Y, mg/ml
0.89
-
lichenan
-
H99R, mg/ml
0.98
-
lichenan
-
pH 6.0, 40C, mutant D58N
1.04
-
lichenan
-
pH 6.0, 40C, mutant E60D
1.47
-
lichenan
-
E63Q, mg/ml
1.69
-
lichenan
-
pH 6.0, 40C, mutant E56D
1.91
-
lichenan
-
pH 6.0, 40C, wild type
1.95
-
lichenan
-
R65A, mg/ml
2.1
-
lichenan
-
pH 6.0, 40C, mutant D58E
2.19
-
lichenan
-
Y24F, mg/ml
2.37
-
lichenan
-
E131Q, mg/ml
2.5
-
lichenan
-
wild type
2.83
-
lichenan
-
expressed in Pichia pastoris
2.89
-
lichenan
-
expressed in Escherichia coli
3.1
-
lichenan
-
pH 6.0, 40C, mutant G63A
3.13
-
lichenan
-
W192A, mg/ml
3.85
-
lichenan
-
Y24A, mg/ml
4.7
-
lichenan
-
N26A, mg/ml
4.8
5
lichenan
-
E63D, mg/ml
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, 30C
additional information
-
Barley beta-glucan
-
1.53 mg/ml; 4.36 mg/ml with substrate barley beta-glucan
0.15
-
beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35C
additional information
-
Carboxymethylcellulose
E2DQY5
Km-value: 2.71 g/l at 50C, pH5.0
-
10.3
-
lichenan
-
pH 6.0, 40C, mutant M39F
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
Orpinomyces sp.
-
-
-
additional information
-
additional information
-
wild-type and mutant enzymes
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
Q84F88
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
Q84C00
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.25
-
1,3-1,4-beta-D-glucan
-
wild-type, expressed in Escherichia coli, pH 5.0, 50C
-
2.44
-
1,3-1,4-beta-D-glucan
-
mutant V18Y, expressed in Escherichia coli, pH 5.0, 50C
-
3.29
-
1,3-1,4-beta-D-glucan
-
mutant V18Y/W203Y, expressed in Escherichia coli, pH 5.0, 50C
-
3.67
-
1,3-1,4-beta-D-glucan
-
mutant W203Y, expressed in Escherichia coli, pH 5.0, 50C
-
1.35
-
4-methylumbelliferyl cellobiose
-
-
0.327
-
4-methylumbelliferyl laminaribiose
-
-
0.074
-
Barley beta-glucan
-
-
0.091
-
Barley beta-glucan
-
-
8.4
-
Barley beta-glucan
-
-
81.6
-
Barley beta-glucan
-
calculated as D-glucose units released from beta-glucan
13.5
-
beta-1,3-1,4-glucan
-
pH 4.0, 75C, substrate from Hordeum vulgare
0.04
-
beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35C
0.91
-
beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35C
1.35
-
beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35C
2.3
-
Beta-D-glucan
Q84C00
native enzyme, pH 6.0, 70C
9.2
-
Beta-D-glucan
Q84F88
native enzyme, pH 6.0, 50C
20.3
-
Beta-D-glucan
Q84F88
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, pH 6.0, 70C
20.3
-
Beta-D-glucan
Q84C00
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, pH 6.0, 70C
5.3
-
Carboxymethylcellulose
-
pH 4.0, 75C, substrate from Hordeum vulgare
-
0.0039
-
Laminarin
-
E63Q
0.0097
-
Laminarin
-
E63D
0.021
-
Laminarin
-
W192A; Y123A
0.045
-
Laminarin
-
N26A
0.056
-
Laminarin
-
S90A
0.07
-
Laminarin
-
Y24A
0.09
-
Laminarin
-
R65A
0.095
-
Laminarin
-
W184Y
0.1711
-
Laminarin
-
Y24F
0.178
-
Laminarin
-
H99R
0.198
-
Laminarin
-
H99D
0.217
-
Laminarin
-
E131Q
0.263
-
Laminarin
-
wild type
0.375
-
Laminarin
-
A98W
0.5
-
Laminarin
-
Y24W
0.65
-
Laminarin
-
Y123F
0.047
-
lichenan
-
E131Q
0.2
-
lichenan
-
mutant enzyme E107D
0.55
-
lichenan
-
mutant enzyme E103D
0.7
-
lichenan
-
mutant enzyme E107H
1.7
-
lichenan
-
mutant enzyme W101Y
2.9
-
lichenan
-
mutant enzyme W101F
3.1
-
lichenan
-
mutant enzyme D105N
3.71
-
lichenan
-
calculated as D-glucose units released from lichenan
5.8
-
lichenan
-
mutant E11L, 45C, pH 5.0
8.08
-
lichenan
-
E63Q
27
-
lichenan
-
E63D
40.4
-
lichenan
-
Y123A
40.5
-
lichenan
-
W192A
44
-
lichenan
-
mutant W203R, calculated as D-glucose units released from lichenan
109
-
lichenan
-
mutant Q70I, calculated as D-glucose units released from lichenan
112.6
-
lichenan
-
E63D
131
-
lichenan
-
mutant F40I, 45C, pH not specified in the publication
147.1
-
lichenan
-
H99R
154
-
lichenan
-
mutant R137Q, 40C, pH not specified in the publication
163.8
-
lichenan
-
W184Y
166.4
-
lichenan
-
calculated as D-glucose units released from lichenan
244
-
lichenan
-
mutant Q70A, calculated as D-glucose units released from lichenan
262
-
lichenan
-
N26A
276
-
lichenan
-
H99D
302.4
-
lichenan
-
E131Q
322
-
lichenan
-
mutant Y42L, 45C, pH not specified in the publication
324
-
lichenan
-
S90A
325
-
lichenan
-
Y24A
349
-
lichenan
-
mutant R137M, 40C, pH not specified in the publication
371
-
lichenan
-
mutant Q70N, calculated as D-glucose units released from lichenan
401
-
lichenan
-
mutant L62G, 45C, pH not specified in the publication
481
-
lichenan
-
Y24F
504
-
lichenan
-
mutant N72Q, calculated as D-glucose units released from lichenan
608
-
lichenan
-
mutant G207-, calculated as D-glucose units released from lichenan
627
-
lichenan
-
Y123F
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, 45C, pH not specified in the publication
785
-
lichenan
-
mutant E85I, calculated as D-glucose units released from lichenan
787
-
lichenan
-
Y24W
811
-
lichenan
-
R65A
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
908
-
lichenan
-
A98W
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, 45C, pH not specified in the publication
1020
-
lichenan
-
wild-type enzyme
1037
-
lichenan
-
mutant R209M, calculated as D-glucose units released from lichenan
1141
-
lichenan
-
mutant K200F, calculated as D-glucose units released from lichenan
1191
-
lichenan
-
wild type
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, 50C, pH not specified in the publication
1833
-
lichenan
-
mutant K64M, 50C, 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, 55C, 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
3026
-
lichenan
-
mutant N44Q, 55C, pH not specified in the publication
3641
-
lichenan
-
mutant Q81I, calculated as D-glucose units released from lichenan
3911
-
lichenan
-
wild-type, 50C, pH 5.0
3920
-
lichenan
-
truncated enzyme, calculated as D-glucose units released from lichenan
5476
-
lichenan
-
mutant W203F, calculated as D-glucose units released from lichenan
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
Q84F88
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
0
additional information
-
additional information
Q84C00
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
0
additional information
-
additional information
-
kcat/KM-value for wild-type, substrate lichenan, 1358 ml/mg/s
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.5
-
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
0.9
-
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
6
-
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
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, 30C
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, 30C
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
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.197
-
-
concentrated crude extract, at 50C, pH 5
1.01
-
-
recombinant enzyme at 37C
1.57
-
-
pH 6.0, 40C, mutant D58E
2.43
-
-
pH 6.0, 40C, mutant D58N
2.57
-
-
pH 6.0, 40C, mutant E60D
5.75
-
-
pH 6.0, 40C, mutant E56D
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
11.6
-
-
mutant E11L, 45C, pH 5.0
12.6
-
-
after 55.53fold purification, at 50C, pH 5
14.5
-
-
37C, pH 5.0
15
19
-
pH 6.0, mutant W105H
15
25
-
mutant N139A, 45C, pH not specified in the publication
18.89
-
Thermomonospora sp.
-
enzyme from culture filtrate, using xylan as a substrate, at 50C, pH 7.0
25
-
Thermomonospora sp.
-
enzyme from culture filtrate, using lichenan as a substrate, at 50C, pH 7.0
29
-
-
pH 6.0, mutant W54F
29
-
-
purified native enzyme, substrate is Hordeum vulgare beta-1,3-1,4-glucan
37
-
-
pH 6.0, mutant W54Y
43
46
-
mutant N44L, 55C, pH not specified in the publication
50.9
-
-
crude culture supernatant
54.3
-
E2DQY5
carboxymethylcellulose as substrate, pH 5.0, 50C
58.6
-
E2DQY5
hydroxyethylcellulose as substrate, pH 5.0, 50C
60
61
-
mutant N44Q, 55C, pH not specified in the publication
69
-
-
pH 6.0, mutant W141H
70
-
-
pH 6.0, mutant W203R
70
-
-
mutant W203R
192
-
Q84C00
native enzyme, substrate lichenan, pH 6.0, 70C
234
-
-
mutant enzyme D317A, at 50C
236
-
-
mutant Q70I
240
-
-
mutant enzyme D220A, at 50C
241
-
-
mutant enzyme E323A, at 50C
245
-
-
mutant enzyme E242A, at 50C
258
-
-
mutant enzyme D106A, at 50C
262
-
-
mutant F40I, 45C, pH not specified in the publication
266
-
-
mutant enzyme D258A, at 50C
271
-
-
mutant enzyme E262A, at 50C
273
-
-
mutant enzyme D100A, at 50C
274
-
-
mutant enzyme D195A, at 50C
275
-
Q84C00
native enzyme, substrate beta-D-glucan, pH 6.0, 70C
283.8
-
-
recombinant enzyme from crude extract, using barley beta-glucan as a substrate
296
-
-
mutant enzyme D196A, at 50C
308
-
-
mutant R137Q, 40C, pH not specified in the publication
387
-
-
-
419
-
-
pH 6.0, mutant W141F
480
-
-
pH 6.0, mutant W148F
502
-
-
pH 6.0, 40C, mutant G63A
527
-
-
mutant Q70A
545
-
-
pH 6.0, 40C, mutant M39F
555.1
-
-
purified enzyme
598.6
-
Thermomonospora sp.
-
after 31.6fold purification, using xylan as a substrate, at 50C, pH 7.0
644
-
-
mutant Y42L, 45C, pH not specified in the publication
699
-
-
mutant R137M, 40C, pH not specified in the publication
748
-
-
mutant enzyme D314A, at 50C
754
-
-
wild type enzyme, at 50C
792.2
-
Thermomonospora sp.
-
after 31.6fold purification, using lichenan as a substrate, at 50C, pH 7.0
802
-
-
mutant Q70N
803
-
-
mutant L62G, 45C, pH not specified in the publication
851
-
Q84F88
native enzyme, substrate lichenan, pH 6.0, 50C
916
-
-
pH 6.0, mutant W112F
969
-
-
mutant G207-
1089
-
-
mutant N72Q
1106
-
Q84F88
native enzyme, substrate beta-D-glucan, pH 6.0, 50C
1114
-
-
mutant D206R
1280
-
-
recombinant enzyme, using barley beta-glucan as a substrate, at 50C and pH 6.0
1329
-
-
-
1335
-
-
recombinant enzyme, using lichenan as a substrate, at 50C and pH 6.0
1377
-
-
mutant F205L
1381
-
-
mutant Q70D
1385
-
-
mutant Q70E
1388
-
-
pH 6.0, 40C, wild type
1406
-
-
mutant D202L
1452
-
-
mutant K200M
1501
-
-
mutant N208G
1572
-
-
pH 6.0, mutant W165H
1621
-
-
pH 6.0, mutant W105F
1652
-
-
mutant R209M
1699
-
-
mutant E85I
1746
-
Q84F88
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate lichenan, pH 6.0, 70C
1746
-
Q84C00
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate lichenan, pH 6.0, 70C
1755
-
-
pH 6.0, mutant W198F
1774
-
-
mutant N72A
1791
-
-
pH 6.0, mutant W165F
1817
-
-
mutant K200F
1906
-
-
recombinant enzyme, using lichenan as a substrate
1986
-
-
mutant E47I, 45C, pH not specified in the publication
2034
-
-
mutant T204F
2065
-
-
pH 6.0, wild type
2065
-
-
wild type, sodium citrate buffer, pH 6.0, 50C, 10 min
2065
-
-
wild-type
2155
-
-
mutant G201S
2434
-
Q84F88
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, pH 6.0, 70C
2434
-
Q84C00
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, pH 6.0, 70C
2479
-
-
recombinant enzyme after 8.74fold purification, using barley beta-glucan as a substrate
2740
-
Bispora sp.
D2DRB6
substrate lichenan, pH 5.0, 60C
2941
-
-
pH 6.0, mutant W186F
2962
-
-
mutant D206N
3076
-
-
mutant E85D
3104
-
-
mutant Q70R
3115
-
-
mutant G207N
3282
-
-
mutant D206M
3581
-
-
mutant K64A, 50C, pH not specified in the publication
3659
-
Orpinomyces sp.
-
-
3671
-
-
mutant K64M, 50C, pH not specified in the publication
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
4040
-
Bispora sp.
D2DRB6
substrtae beta-D-glucan, pH 5.0, 60C
4081
-
-
mutant D202N
5694
-
-
wild-type, expressed in Escherichia coli, pH 5.0, 50C
5758
-
-
mutant Q81N
6242
-
-
122.5fold purified enzyme
6520
-
-
mutant V18Y, expressed in Escherichia coli, pH 5.0, 50C
7833
-
-
wild-type, 50C, pH 5.0
7873
-
-
mutant Q81I
7980
-
-
expressed in Escherichia coli, sodium citrate buffer, pH 6.0, 50C, 10 min
8208
-
E0XN39
substrate lichenan, pH 7.0, 70C
8478
-
-
truncated enzyme
8726
-
-
pH 6.0, mutant W203F
8726
-
-
mutant W203F
9263
-
-
mutant W203Y, expressed in Escherichia coli, pH 5.0, 50C
9967
-
-
mutant V18Y/W203Y, expressed in Escherichia coli, pH 5.0, 50C
10800
-
-
expressed in Pichia pastoris X-33, sodium citrate buffer, pH 6.0, 50C, 10 min
11940
-
E0XN39
substrate barley beta-glucan, pH 7.0, 70C
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.5
-
Bispora sp.
D2DRB6
three activity peaks at pH 1.5, 3.5, and 5.0. At pH 1.5, 61% of the activity at pH 5.0
3.5
-
Bispora sp.
D2DRB6
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
-
-
two optima at pH 4 and 6.5
4
-
-
two optima at pH 4.0 and 6.3
4
-
-
two optima at pH 4 and 6.5
4.5
-
-
-
4.5
-
-
wild type, mutant H300P
5
-
Bispora sp.
D2DRB6
three activity peaks at pH 1.5, 3.5, and 5.0. Maximum activity at pH 5.0
5
-
-
wild-type and mutant E11L
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
5.6
-
-
recombinant enzyme
5.8
6.2
Orpinomyces sp.
-
-
6
7
-
recombinant proteins
6
-
-
recombinant enzyme
6.3
-
-
two optima at pH 4.0 and 6.3
6.5
-
-
two optima at pH 4 and 6.5
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
7
-
Thermomonospora sp.
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
5.5
-
79% and 73% of the maximum activity, respectively, at pH 3.5 and pH 4.5
3
6
-
pH 3.0: about 50% of maximal activity, pH 6.0: about 40% of maximal activity
5
12.5
-
half-maximal activity at pH 5.0 and at pH 12.5
5.2
8
-
50% of maximal activity at pH 5.2 and pH 8.0
5.4
7
Orpinomyces sp.
-
about 80% of maximal activity at pH 5.4 and at pH 7.0
5.5
6
-
mutant enzyme E107H
5.5
7
-
more than 80% of maximal activity at pH 5.5 and pH 7.0
5.9
6.5
-
more than 80% of maximal activity at pH 5.9 and pH 6.5
5.9
8.5
-
more than 80% of maximal activity at pH 5.9 and pH 8.5
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
9
-
with 50% of the activity remaining at pH 9
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
recombinant enzyme
40
-
-
mutants R137M and R137Q
45
-
Orpinomyces sp.
-
-
45
-
-
recombinant enzyme
45
-
-
mutants E11L, F40I, Y42L, E47I, L62G, and N139A
50
-
-
lichenin or oat beta-D-glucan as substrate
50
-
Thermomonospora sp.
-
-
50
-
-
wild-type, mutants K64A and K64M
55
-
-
mutants N44L and N44Q
60
-
Bispora sp.
D2DRB6
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-8
60
Q1EMA6
-
20
70
-
30 min with about 50% of activity remaining at 50C; the remaining activity decreased to 20% at 20-40C and is completely destroyed at 50-70C
30
60
-
30C, about 30% of maximal activity with oat beta-D-glucan, about 45% of maximal activity with lichenin, 60C: about 20% of maximal activity with lichenin and oat beta-D-glucan as substrate
37
65
-
more than 80% of maximal activity at 37C and at 65C
40
55
-
about 60% of maximal activity at 40C and at 55C
40
60
-
40C: about 60% of maximal activity, 60C: about 20% of maximal activity
40
65
-
40C: about 60% of maximal activity, 65C: about 50% of maximal activity
40
65
-
about 40% of maximal activity at 40C and at 65C
40
65
-
40C: about 80% of maximal activity, 65C: about 60% of maximal activity
40
80
-
40C: about 40% of maximal activity, 80C: about 30% of maximal activity
45
65
-
45C: about 80% of maximal activity, 65C: about 90% of maximal activity
45
90
-
at temperatures of 60C and 85C, the enzyme activity is 85% and 80% of maximal activity, respectively
55
75
-
more than 80% of maximal activity at 55C and at 75C
55
90
-
55C: about 50% of maximal activity, 90C: about 30% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
-
-
isoelectric focusing
3.6
-
-
isoelectricfocusing
4.2
-
-
isoelectric focusing
4.27
-
Thermomonospora sp.
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
isoenzyme II is synthesized exclusively in the aleurone layer, isoenzyme III is detected in scutellum and aleurone layer
Manually annotated by BRENDA team
Orpinomyces sp.
-
recombinant enzyme expressed in E. coli
Manually annotated by BRENDA team
Bacillus subtilis GN156
-
-
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
second leaf, enzyme protein increases upon incubation in the dark and disappears upon illumination or feeding with sucrose
Manually annotated by BRENDA team
Q5UAW3
gene OsEGL1 is expressed in seedling, and young and adult plant roots
Manually annotated by BRENDA team
-
isoenzyme I is synthesized predominantly in the scutellum, isoenzyme III is detected in scutellum and aleurone layer
Manually annotated by BRENDA team
-
transfer from antural light/dark cycle into darkness induces eisozyme EI
Manually annotated by BRENDA team
additional information
-
the optimum temperature for the fungal growth is 28C, the fungus does not grow above 42C
Manually annotated by BRENDA team
additional information
E2DQY5
isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Orpinomyces sp.
-
recombinant enzyme expressed in Escherichia coli
-
Manually annotated by BRENDA team
Bacillus subtilis GN156
-
-
-
-
Manually annotated by BRENDA team
Orpinomyces sp.
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
25000
-
-
SDS-PAGE
25300
-
-
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
27700
-
-
enzyme I, ultracentrifugation
27900
-
-
SDS-PAGE
28000
-
-
recombinant enzyme with a six-His tag at the N terminus, SDS-PAGE
29000
-
-
SDS-PAGE
31690
-
-
mass spectrometry
32000
-
-
gel filtration
33730
-
-
mass spectrometry
33800
-
-
enzyme II, ultracentrifugation
34000
-
-
SDS-PAGE
34600
-
-
gel filtration
36500
-
-
SDS-PAGE
37200
-
-
gel filtration
52000
-
-
gel filtration
55000
-
-
SDS-PAGE
60000
-
-
SDS-PAGE
60600
-
E2DQY5
calculated mass
63000
-
-
SDS-PAGE
64120
-
Thermomonospora sp.
-
gel filtration
64240
-
Thermomonospora sp.
-
calculated from amino acid sequence
64500
-
Thermomonospora sp.
-
SDS-PAGE
66730
-
Thermomonospora sp.
-
MALDI-TOF mass spectrometry
90000
-
-
SDS-PAGE, J2 is composed of three protein subunits of 40, 32 and 18 kDa
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 27500, enzyme inactivated by epoxyalkyl beta-D-oligoglucosides
?
-
x * 24000, SDS-PAGE
?
-
x * 30000, SDS-PAGE
?
-
x * 26000, SDS-PAGE
?
Orpinomyces sp.
-
x * 27000, recombinant enzyme, SDS-PAGE; x * 27929, calculation from nucleotide sequence
?
-
x * 32085, calculation from nucleotide sequence
?
-
x * 30000, SDS-PAGE
?
-
x * 29000, SDS-PAGE
?
-
x * 35000, recombinant enzyme, SDS-PAGE
?
-
x * 33500, SDS-PAGE, recombinant enzyme with His-tag
?
Bispora sp.
D2DRB6
x * 45170, calculated, x * 60000-80000, SDS-PAGE of recombinant enzyme, x * 48000, SDS-PAGE after Endo H treatment
?
E0XN39
x * 38500, SDS-PAGE, x * 31923, calculated
?
-
x * 55000, SDS-PAGE
?
Bacillus subtilis A8-8
-
x * 55000, SDS-PAGE
-
dimer
-
2 * 26000, SDS-PAGE
monomer
-
1 * 35200, SDS-PAGE
monomer
-
1 * 28000, enzyme II, SDS-PAGE; 1 * 28000, enzyme I, SDS-PAGE
monomer
-
1 * 31000, SDS-PAGE
monomer
-
1 * 38600, SDS-PAGE
additional information
-
four protein bands of approximately 40, 32, 25 and 18 kDa are resolved from pJ2
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
Bacillus subtilis GN156
-
four protein bands of approximately 40, 32, 25 and 18 kDa are resolved from pJ2
-
additional information
Clostridium thermocellum ZJL4
-
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
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no glycoprotein
Bispora sp.
D2DRB6
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
proteolytic modification
Bispora sp.
D2DRB6
presence of an N-terminal signal peptide at residues 1-9
glycoprotein
-
expressed in Pichia pastoris
glycoprotein
-
enzyme I contains 0.7% carbohydrate of which three residues are probably N-acetylglucosamine, enzyme II contains 3.6% carbohydrate
proteolytic modification
Orpinomyces sp.
-
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
no glycoprotein
E0XN39
no N-glycosylation sites present in the protein, Endo H treatment does not result in a protein band shift
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
hybrid enzyme
-
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
-
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
-
truncated form of enzyme containing the catalytic domain from amino acid 1-258, seleno-methionine labeled protein
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1
8
Bispora sp.
D2DRB6
37C, 1 h, more than 85% of maximum activity
2.5
9
-
4C or 20C, stable for 20 h
3
-
-
retains approximately 80% of original activity after treatment at pH 3.0 for 12 h
3.4
9.8
Orpinomyces sp.
-
4C, stable for at least 24 h
3.5
7
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase, stable
3.6
10.6
-
-
4
5
-
25C, 72-96 h, stable
4
6
-
the recombinant enzyme is stable between pH 4.0 and 6.0, having 85% of the original activity
4
7
-
increase in stability from pH 4 to pH 7
4
8
Thermomonospora sp.
-
-
4
-
-
optimum condition for the beta-glucanase stability
4.1
-
-
65C, 1 h, 95% loss of activity; 65C, 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
4.1
-
-
65C, 1 h, complete inactivation; 65C, 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
4.8
6.4
-
stable
5
6
-
60C, 10 min, stable
5
7
-
10 min, stable
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
6
9
-
with 50% of the activity remaining at pH 9
6
9
-
stable within
6
-
-
no enzyme activity is detected at pH higher than 6
8
-
-
retains approximately 80% of original activity after treatment at pH 8.0 for 12 h
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-4
-
Q1EMA6
GLU-3 retains 14%-35% activity at -4C
20
40
-
the remaining activity decreased to 20% at 20-40C and is completely destroyed at 50-70C
20
50
-
30 min with about 50% of activity remaining at 50C
22
-
-
11 days, complete inactivation of wild-type, 70% residual activity of mutant D70V
25
35
-
decrease in stability from 25C to 35C
30
60
-
99.1, 87.8, 56.6, and 34.2% residual activity after 30 min preincubation at 30, 40, 50, and 60C, respectively
30
60
-
104.5, 101.2, 67.9, and 21.2% residual activity after 30 min preincubation at 30, 40, 50, and 60C, respectively
30
60
-
102, 91.2, 60.7, and 4.3% residual activity after 30 min preincubation at 30, 40, 50, and 60C, respectively
30
60
-
98, 74.3, 2.4, and 0% residual activity after 30 min preincubation at 30, 40, 50, and 60C, respectively
40
-
-
pH 5.5, 10 min, stable
40
-
Orpinomyces sp.
-
recombinant enzyme, pH 6.0, 24 h, stable
40
-
-
10 min, stable
44.5
-
-
15 min, 50% of activity, mutant G44R
45
-
Orpinomyces sp.
-
recombinant enzyme, pH 6.0, 24 h, 28% loss of activity
45
-
-
the wild-type maintains more than 85% of the original activity for 10 min
46
-
-
15 min, 50% of activity, mutant K23R
46.1
-
-
15 min, 50% of activity, mutant A79P
46.2
-
-
15 min, 50% of activity, mutant F85Y
47.5
-
-
15 min, 50% of activity, wild type
47.9
-
-
15 min, 50% of activity, mutant M298K, mutant T17D
48.2
-
-
15 min, 50% of activity, mutant N290H
50
60
-
sharp decrease in activity up to 60C, but very stable below 50C
50
70
-
after incubation at 50, 60, and 70C for 30 min, the residual activity is 95, 60, and 0%, respectively
50
70
-
after 2 h incubation at 50C and 60C, the residual activity remaines 100% and 50%, respectively, while the enzymatic activity is abolished after 3 min incubation at 70C
50
-
Orpinomyces sp.
-
recombinant enzyme, pH 6.0, 24 h, 41% loss of activity
50
-
-
10 min, about 25% loss of activity
50
-
-
unstable above
50
-
E0XN39
30 min, more than 90% of maximum activity
51.2
-
-
15 min, 50% of activity, mutant H300P
52
-
-
10 min, 50% inactivation, wild-type
55
-
Orpinomyces sp.
-
recombinant enzyme, pH 6.0, 24 h, 70% loss of activity
60
-
-
10 min, 50% loss of activity, crude enzyme extract
60
-
-
15 min, pH 6.5, stable
60
-
-
pH 5.5, 10 min, complete loss of activity
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
-
-
10 min, about 35% loss of activity
60
-
-
10 min, complete inactivation
60
-
-
4 min, 50% inactivation, wild-type, 11 min, 50% inactivation, mutant D70V
60
-
Bispora sp.
D2DRB6
stable for at least 1 h
64
-
Q1EMA6
GLU-3 is irreversibly denatured above 64C
65
-
-
half-life: 25 min; 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
-
-
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
-
-
for 30 min
65
-
-
purified native enzyme, half-life is over 68 days
66
-
-
10 min, 50% inactivation, mutant D70V
70
-
-
1 h, 15% loss of activity
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
-
Bispora sp.
D2DRB6
5 min, 48% residual activity, 60 min, 30% residual activity
70
-
-
purified native enzyme, half-life is 125 h
70
-
E0XN39
30 min, 65% of maximum activity
75
-
-
1 h, 25% loss of activity
75
-
-
purified recombinant wild-type enzyme, 10 min, 51% remaining activity in absence of Ca2+, 86% in presence of 1 mM Ca2+
75
-
-
purified native enzyme, half-life is 22 h
80
-
Thermomonospora sp.
-
half-life of 5 min at 80C
80
-
-
optimum condition for the beta-glucanase stability
80
-
-
purified recombinant wild-type enzyme, 5 min, 54% remaining activity in absence of Ca2+, 73% in presence of 1 mM Ca2+
80
-
-
purified native enzyme, half-life is 1 h
85
-
-
purified native enzyme, half-life is about 5 min
90
-
-
80% activity after 10 min
90
-
-
the residual activity of mHG at 90C for 10 min is 83.45% of its maximum activity
90
-
-
purified native enzyme, half-life is 80 s
100
-
-
even when subjected to 100C for 3 h, beta-glucanase activity does not show significant reduction
additional information
-
-
particularly thermostable in presence of Ca2+
additional information
-
-
Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation
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
-
-
thermal inactivation follow first-order kinetics, overview
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation
-
particularly thermostable in presence of Ca2+
-
stable to repeated freeze-thaw cycles
-
enzyme is highly resistant to both pepsin and trypsin
Bispora sp.
D2DRB6
Ca2+ stabilizes the enzyme at higher temperatures
-
in strong acid solution (HCl), beta-glucanase loses activity under conditions of pH 2.0, 1.0, and 0 indicating no tolerance to HCl
-
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 25C to 35C, o-phenanthroline lowers stability of enzyme
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ethanol
-
stable up to concentrations up to 10% w/v
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-15C, stable for 12 months
-
4C, 50 mM sodium phosphate, pH 7.8, 300 mM sodium chloride, stable for several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DEAE-Sepharose CL-6B column chromatography
-
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
-
Ni-NTA His Bind resin column chromatography
-
affinity chromatography of epoxy-activated sepharose 6B and ultrafiltration technique
-
Ni-NTA agarose column chromatography
-
immobilized metal ion affinity chromatography, gel filtration, anion exchange chromatography
-
mutants purified on Ni-NTA affinity column, more than 95% purity
-
on Ni-NTA affinity column
-
Q-Sepharose FF column twice, Ni-NTA affinity column for the Escherichia coli protein, Q-Sepharose FF column for the Pichia pastoris protein
-
Sephadex G-100 gel filtration
-
native enzyme by 16fold ammonium sulfate fractionation, combined cation and anion exchange chromatography, and another anion exchange chromatography
-
recombinant enzyme
Orpinomyces sp.
-
recombinant GST-tagged EGL2 from Escherichia coli by glutathione affinity chromatography, the tag is cleaved off by thrombin, followed by benzamidine resin chromatography
Q8S9P4
recombinant GST-tagged EGL1 from Escherichia coli by glutathione affinity chromatography, the tag is cleaved off by thrombin, followed by benzamidine resin chromatography
Q5UAW3
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%
-
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
-
wild type and mutant enzymes W101F, W101Y, E103D, E103Q, D105N, D105K, E107D, E107Q, and E107H
-
SP-Sepharose column chromatography and Sephacryl S-100 gel filtration
-
GSTrap FF column chromatography and HiTrap Benzamidine FF column chromatography
Q1EMA6
by gel filtration and ultrafiltration
-
DEAE Sephadex A50 column chromatography and Sephacryl S-200 gel filtration
Thermomonospora sp.
-
the cloned protein from the recombinant strain BL21/pET21a-RuCelA is purified using Ni-NTA resin
E2DQY5
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
Q84F88
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
-
expressed in Escherichia coli strain BL21 (DE3)
-
expressed in Pichia pastoris strain GS115
-
hybrid from Bacillus macerans and Bacillus amyloliquefaciens
-
hybrid from Bacillus macerans and Bacillus amyloliquefaciens, H(A16-M)
-
expression as GST-fusion protein
-
expression in Pichia pastoris
Bispora sp.
D2DRB6
expression in Escherichia coli
-
expressed in Nicotiana benthamina as fusion protein
-
expression in Escherichia coli
Q84C00
gene LicB, expression of mature enzyme and isolated catalytic domain, as well as of the enzyme truncation mutants in Escherichia coli strain BL21
-
overexpression in Escherichia coli XL1-blue and BL21 with His-tag
-
recombinant expression in transgenic Nicotiana tabacum plants
-
C-terminally truncated (10 kDa), overexpression in Escherichia coli BL21 (DE3) and Pichia pastoris X-33, mutants with increased catalytic efficiency and thermotolerance
-
expressed in Lactobacillus reuteri strain Pg4
-
expression in Escherichia coli
-
expression in Escherichia coli and Pichia pastoris
-
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
-
wild-type and mutants cloned into vector pET26b(+) and expressed in Escherichia coli BL21 (DE3)
-
expression in Escherichia coli
-
expression in Escherichia coli, isolation and characterization of the gene
-
transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-beta-glucanase during germination
-
expression in Escherichia coli
Orpinomyces sp.
-
gene OsEGL2, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, functional expression of GST-tagged EGL2 in Escherichia coli
Q8S9P4
gene OsEGL1, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, functional expression od GST-tagged EGL1 in Escherichia coli
Q5UAW3
expression in Pichia pastoris
E0XN39
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
-
expressed in Escherichia coli
Q1EMA6
into pET3a vector and expressed in Escherichia coli strain BL21(DE3)pLysS
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21/pET21a
E2DQY5
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
Q8S9P4
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
Q5UAW3
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E134A
-
inactive mutant, analysis of substrate binding
E134A
-
mutant devoid of hydrolase activity but efficiently catalyzing transglycosylation
E134A
-
catalyzes condensation reaction with alpha-fluorido-substrates
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
A98W
-
active-site variant
E105Q/E109Q
-
catalytically impaired
E131Q
-
active-site variant
E63D
-
active-site variant
E63Q
-
active-site variant
N26A
-
active-site variant
R65A
-
active-site variant
S90A
-
active-site variant
W184Y
-
active-site variant
W192A
-
active-site variant
Y123A
-
active-site variant
Y123F
-
active-site variant
Y24A
-
active-site variant
Y24F
-
active-site variant
233Stop
-
28.4% of wild-type activity
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 50C over 10 min, shows a 1.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
D58A
-
no enzymatic activity
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
E56A
-
no enzymatic activity
E56D
-
dramatic decrease in kcat, substrate affinity similar to wild type
E56Q
-
no enzymatic activity
E60A
-
no enzymatic activity
E60D
-
dramatic decrease in kcat, substrate affinity similar to wild type
E60Q
-
no enzymatic activity
E85D
-
has 5fold lower kcat/Km ratios than the wild-type
E85I
-
has 5fold lower kcat/Km ratios than the 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
G63A
-
decrease in thermostability
K200F
-
is the most heat-sensitive enzyme, retains 72% of activity at 45C 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
-
0.1% of wild-type activity
M27R/M39D
-
0.2% of wild-type activity
M39F
-
5-fold increase in km value
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
N72A
-
has 11fold lower kcat/Km ratios than the wild-type
N72Q
-
has 17fold lower kcat/Km ratios than the wild-type
Q70A
-
has 299fold lower kcat/Km ratios than the wild-type
Q70D
-
has 62fold lower kcat/Km ratios than the wild-type
Q70E
-
has 106fold lower kcat/Km ratios than the wild-type
Q70I
-
has 499fold lower kcat/Km ratios than the wild-type
Q70N
-
has 63fold lower kcat/Km ratios than the wild-type
Q70R
-
has 35fold lower kcat/Km ratios than the wild-type
Q81I
-
has 2fold lower kcat/Km ratios than the wild-type
Q81N
-
has 2.5fold lower kcat/Km ratios than the wild-type
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
-
loss of activity
S84D
-
80.9% of wild-type activity
T204F
-
shows a 2.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
V18Y
-
104% of wild-type activity. Increase in thermostability by 2 degrees
V18Y/W203Y
-
134.3% of wild-type activity
V61F
-
20.9% of wild-type activity
W105F
-
significant decrease in thermostability
W105H
-
significant decrease in thermostability
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
W165H
-
significant decrease in thermostability
W186F
-
increase in kcat-value, no significant change in thermal stability
W198F
-
significant decrease in thermostability
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
-
87.6% of wild-type activity
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
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
-
130.2% of wild-type activity
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
A79P
-
decrease in thermal stability
F85Y
-
decrease in thermal stability
G44R
-
decrease in thermal stability
H300P
-
increase in thermal stability
K23R
-
decrease in thermal stability
N290H
-
slight increase in thermal stability
D70V
-
thermostable mutant, similar katalytic efficiency as wild type
D105K
-
activity is reduced to less than 1%
D105N
-
activity is reduced to less than 1%
E103D
-
activity is reduced to less than 1%
E103Q
-
activity is reduced to less than 1%
E107D
-
activity is reduced to less than 1%
E107H
-
activity is reduced to less than 1%
W101F
-
activity is reduced to less than 1%
W101Y
-
activity is reduced to less than 1%
D100A
-
36% relative activity compared to the wild type enzyme
D106A
-
34% relative activity compared to the wild type enzyme
D195A
-
36% relative activity compared to the wild type enzyme
D220A
-
32% relative activity compared to the wild type enzyme
D258A
-
35% relative activity compared to the wild type enzyme
D314A
-
99% relative activity compared to the wild type enzyme
D317A
-
31% relative activity compared to the wild type enzyme
E196A
-
39% relative activity compared to the wild type enzyme
E222A
-
no activity
E242A
-
32% relative activity compared to the wild type enzyme
E262A
-
36% relative activity compared to the wild type enzyme
E323A
-
32% relative activity compared to the wild type enzyme
E91A
-
no activity
D195A
Paenibacillus polymyxa GS01
-
36% relative activity compared to the wild type enzyme
-
D258A
Paenibacillus polymyxa GS01
-
35% relative activity compared to the wild type enzyme
-
D314A
Paenibacillus polymyxa GS01
-
99% relative activity compared to the wild type enzyme
-
E222A
Paenibacillus polymyxa GS01
-
no activity
-
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
Q84F88
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 80C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
H99D
-
active-site variant
additional information
-
subsite +1 mutants, kinetic analysis
Y24W
-
active-site variant
additional information
-
the truncated gene product, devoid of cellulose-binding domain, shows 60% of activity and binds to avicel
additional information
Bacillus subtilis A8-8
-
the truncated gene product, devoid of cellulose-binding domain, shows 60% of activity and binds to avicel
-
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
Q84C00
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 80C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
additional information
Clostridium thermocellum ZJL4
-
construction of diverse enzyme truncation mutants for domain functional analysis, overview
-
M39F
-
92.8% of wild-type activity
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
M298K
-
thermal stabiltiy similar to wild type
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
E107Q
-
activity is reduced to less than 1%
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
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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
E323A
Paenibacillus polymyxa GS01
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32% relative activity compared to the wild type enzyme
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additional information
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UV irradiation leads to mutants TC2 and TC5 with increased activity against barley beta-glucan during growth on solka floc
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
Q84F88
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 80C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
synthesis
Bispora sp.
D2DRB6
over-expression in Pichia pastoris, with a yield of about 1000 U/ml in a 3.7 l fermentor
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
Q84C00
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 80C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
industry
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properties make the enzyme highly suitable for industrial applications
synthesis
E0XN39
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
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
biofuel production
E2DQY5
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