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Information on EC 3.2.1.73 - licheninase and Organism(s) Bacillus amyloliquefaciens and UniProt Accession P07980
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3.2.1.73 licheninaseIUBMB Comments
Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.
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Word Map
- 3.2.1.73
- cellulases
-
cellulolytic
- trichoderma
- knee
- reesei
- cellobiohydrolase
- exoglucanase
- thermocellum
- avicel
-
carboxymethyl
-
lignocellulosic
-
cellulosic
-
arthroscopic
-
saccharification
- beta-glucosidase
- carboxymethylcellulose
-
cellulose-binding
- straw
-
microcrystalline
-
glutenins
- cellulosome
- bagasse
- cellotriose
- lichenan
- xyloglucans
- cellulomonas
- cellotetraose
- xylanases
-
3.2.1.4
-
hemicellulases
- cmcase
-
patellar
- endo-beta-1,4-glucanase
-
patellofemoral
- succinogenes
- endoxylanase
-
dockerins
- humicola
-
fpase
- fibrobacter
-
cellulose-degrading
-
lysholm
-
lignocellulolytic
- mannanase
- cellodextrins
- meniscal
- cellobiase
- thermobifida
-
xylanolytic
- brewing
- synthesis
- endocellulase
- agriculture
- biofuel production
- degradation
- food industry
- analysis
- industry
- nutrition
The taxonomic range for the selected organisms is: Bacillus amyloliquefaciens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
endoglucanase, plica, glu-1, glu-3, endo-beta-glucanase, 1,3-1,4-beta-glucanase, 1,3-1,4-beta-d-glucanase, bglc8h, af-egl7, xyniii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(1->3,1->4)-beta-glucanase isoenzyme EII
-
-
-
-
1,3-1,4-beta-D-glucan 4-glucanohydrolase
-
-
-
-
1,3-1,4-beta-D-glucan glucanohydrolase
-
-
-
-
1,3;1,4-beta-glucan 4-glucanohydrolase
-
-
-
-
1,3;1,4-beta-glucan endohydrolase
-
-
-
-
beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase
-
-
-
-
endo-beta-1,3-1,4 glucanase
-
-
-
-
laminarinase
-
-
-
-
Lichenase
Mixed linkage beta-glucanase
-
-
-
-
Lichenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
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.
CAS REGISTRY NUMBER
COMMENTARY
37288-51-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
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
-
-
?
additional information
?
-
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
?
additional information
?
-
-
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
antifungal enzyme activity assay
-
-
?
additional information
?
-
antifungal enzyme activity assay
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3,4)-epoxybutyl beta-D-cellobioside
-
identification of Glu105 at the active site
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
KM value for native enzyme, substrate beta-D-glucan, is 1.5 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1.2 mg/ml
-
additional information
additional information
-
KM value for native enzyme, substrate beta-D-glucan, is 1.5 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1.2 mg/ml
-
additional information
additional information
-
7.9 mg/ml for recombinant wild-type enzyme, 7.2 mg/ml for recombinant optimally-modified enzyme, with AZO blue beta-glucan at pH 6.5, 40°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
109
AZO blue beta-glucan
-
recombinant wild-type enzyme, pH 6.5, 40°C
-
267
AZO blue beta-glucan
-
recombinant optimally-modified enzyme, pH 6.5, 40°C
-
20.3
Beta-D-glucan
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, pH 6.0, 70°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Kcat/KM value for native enzyme, substrate beta-D-glucan, is 369 mg/ml/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1014 mg/ml/min
-
additional information
additional information
-
Kcat/KM value for native enzyme, substrate beta-D-glucan, is 369 mg/ml/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1014 mg/ml/min
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.4
-
hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
1746
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate lichenan, pH 6.0, 70°C
2434
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, pH 6.0, 70°C
2717
-
recombinant wild-type enzyme, pH 6.5, 40°C, substrate AZO blue beta-glucan
3370
-
recombinant optimally-modified enzyme, pH 6.5, 40°C, substrate AZO blue beta-glucan
3722
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8
-
activity range, wild-type and optimally-modified enzymes, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 65
-
activity range, wild-type and optimally-modified enzymes, overview
40 - 60
-
40°C: about 60% of maximal activity, 60°C: about 20% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the GH16 endo-beta-1,3-1,4-glucanases family
physiological function
endo-beta-1,3-1,4-glucanases are glycoside hydrolases involved in the enzymatic depolymerization of 1,3-1,4-beta-glucans and show antifungal activity against some fungi. Bacillus amyloliquefaciens BLB369 has a high antagonistic activity against phytopathogenic fungi. The purified recombinant enzyme has the ability to inhibit the growth of the phytopathogenic fungus Alternaria alternata
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 27300, calculated, x * 30500 and x * 32500, SDS-PAGE of recombinant protein
?
x * 27300, about, sequence calculation, x * 30300, recombinant His6-tagged enzyme, x * 32500, recombinant OmpA-His6-tagged enzyme
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase. Hybrid enzyme H2 consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens. Hybrid enzyme H1 exhibits increased thermostability especially in an acidic environment compared to both parental enzymes. Hybrid enzyme H2 is more thermolabile than the naturally occuring beta-glucanases
additional information
-
hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, expression in Escherichia coli
additional information
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
additional information
-
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
additional information
-
modifying five (out of 12) epsilon-amino groups in lysine residues with nitrous acid improves thermostablility and enzymatic activity of the enzyme, optimizing the condition of chemical modification, overview. Compared to the wild-type enzyme, the optimally-modified enzyme has higher specific activity and T50 value, which are 3370 U/mg and 70°C, respectively. Its half-life values at 50 and 60°C are extended and reach 58.5 and 49.5 min, respectively
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 7
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase, stable
171537
4.1
5.6 - 6
-
hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens, stable
171537
4.1
-
65°C, 1 h, hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, 85%-95% of the initial activity is retained
171544
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 70
-
purified recombinant enzyme, the wild-type enzymes activity decline rapidly above 60°C, while the optimally-modified enzyme is more stable and shows activity up to 70°C
65
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
additional information
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
additional information
-
particularly thermostable in presence of Ca2+
additional information
-
Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
secreted recombinant OmpA-His6-tagged enzyme from cell culture supernatant by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene bgl, recombinant expression in Escherichia coli, the enzyme is secreted
gene glu369, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of the extracellular enzyme in Escherichia coli TOP10 cells using vector pKJD4 also encoding the OmpA signal sequence for Escherichia coli periplasmic localization, periplasmic secretion of the recombinant OmpA-His6-tagged enzyme
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
-
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
enzyme shows the ability to inhibit the growth of phytopathogenic fungus Alternaria alternata
synthesis
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
additional information
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Borriss, R.; Zemek, J.
beta-1,3-1,4-Glucanase in sporenbildenden Mikroorganismen. III. Substratspezifitt und Wirkungsweise einiger Bacillus-beta-Glucan Hydrolasen
Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg. , Abt. II
135
696-703
1980
Bacillus amyloliquefaciens, Niallia circulans, Brevibacillus laterosporus, Bacillus pumilus, Paenibacillus polymyxa
Borriss, R.; Zemek, J.
beta-1,3-1,4-Glucanase in sporenbildenden Mikroorganismen. IV. Eigenschaften einiger Bacillus-beta-Glucan-Hydrolasen
Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg. , Abt. II
136
63-69
1981
Bacillus amyloliquefaciens, Niallia circulans, Bacillus subtilis, Brevibacillus laterosporus, Paenibacillus macerans, Bacillus pumilus, Paenibacillus polymyxa
Borriss, R.; Olsen, O.; Thomsen, K.K.; von Wettstein, D.
Hybrid Bacillus endo-(1-3,1-4)-beta-glucanases: construction of recombinant genes and molecular properties of the gene products
Carlsberg Res. Commun.
54
41-54
1989
Bacillus amyloliquefaciens, Paenibacillus macerans
Olsen, O.; Borrisss, R.; Simon, O.; Thomsen, K.K.
Hybrid Bacillus (1-3,1-4)-beta-glucanases: engineering thermostable enzymes by construction of hybrid genes
Mol. Gen. Genet.
225
177-185
1991
Bacillus amyloliquefaciens, Bacillus subtilis, Paenibacillus macerans
Hoj, P.B.; Condron, R.; Traeger, J.C.; McAuliffe, J.C.; Stone, B.A.
Identification of glutamic acid 105 at the active site of Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan 4-glucanohydrolase using epoxide-based inhibitors
J. Biol. Chem.
267
25059-25066
1992
Bacillus amyloliquefaciens
Sun, J.; Wang, H.; Lv, W.; Ma, C.; Lou, Z.; Dai, Y.
Construction and characterization of a fusion beta-1,3-1,4-glucanase to improve hydrolytic activity and thermostability
Biotechnol. Lett.
33
2193-2199
2011
Acetivibrio thermocellus (Q84C00), Acetivibrio thermocellus, Bacillus amyloliquefaciens (Q84F88), Bacillus amyloliquefaciens
Niu, C.; Zhu, L.; Wang, J.; Li, Q.
Simultaneous enhanced catalytic activity and thermostability of a 1,3-1,4-beta-glucanase from Bacillus amyloliqueformis by chemical modification of lysine residues
Biotechnol. Lett.
36
2453-2460
2014
Bacillus amyloliquefaciens
Zalila-Kolsi, I.; Sellami, S.; Tounsi, S.; Jamoussi, K.
Heterologous expression and periplasmic secretion of an antifungal Bacillus amyloliquefaciens BLB369 endo-beta-1,3-1,4-glucanase in Escherichia coli
J. Phytopathol.
166
28-33
2018
Bacillus amyloliquefaciens (A0A1C8L3J5), Bacillus amyloliquefaciens (A0A3G1ZIV1), Bacillus amyloliquefaciens BLB369 (A0A3G1ZIV1)
-
Goldenkova-Pavlova, I.V.; Tyurin, A.A.; Mustafaev, O.N.
The features that distinguish lichenases from other polysaccharide-hydrolyzing enzymes and the relevance of lichenases for biotechnological applications
Appl. Microbiol. Biotechnol.
102
3951-3965
2018
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens (P07980), Bacillus altitudinis, Paenibacillus barcinonensis (A0A097QQT4), Bacillus pumilus (A0A0F6QU36), Paenibacillus barengoltzii (A0A0K1P4J7), Bacillus velezensis (A0A0M4NIK2), Acetivibrio thermocellus (A3DBX3), Acetivibrio thermocellus (Q84C00), Bacillus subtilis (A8CGP1), Bacillus subtilis (G0YW23), Bacillus subtilis (P04957), Bacillus subtilis (Q45691), Paenibacillus polymyxa (A9Z0X6), Ruminococcus albus (E9SCT3), Bacillus sp. SJ-10 (I1W007), Bacillus tequilensis (K0A689), Fibrobacter succinogenes (P17989), Niallia circulans (P19254), Bacillus licheniformis (P27051), Brevibacillus brevis (P37073), Rhodothermus marinus (P45798), Bacillus sp. N137 (Q45648), Bacillus sp. A3 (Q6YAT3), Paenibacillus macerans (Q846Q0), Bacillus subtilis MA139 (A8CGP1), Bacillus tequilensis CGX5-1 (K0A689), Acetivibrio thermocellus DSM 1237 (A3DBX3), Bacillus subtilis 168 (P04957), Ruminococcus albus 8 (E9SCT3), Acetivibrio thermocellus NBRC 103400 (A3DBX3), Brevibacillus brevis ALK36 (P37073), Bacillus velezensis S2 (A0A0M4NIK2), Bacillus altitudinis YC-9, Bacillus subtilis NCIB 8565 (Q45691), Paenibacillus polymyxa CP7 (A9Z0X6), Niallia circulans ATCC 21367 (P19254), Rhodothermus marinus ITI378 (P45798), Bacillus amyloliquefaciens ATCC 23350, Bacillus amyloliquefaciens ATCC 15841 (P07980), Acetivibrio thermocellus ATCC 27405 (A3DBX3), Fibrobacter succinogenes S85 (P17989), Acetivibrio thermocellus VPI 7372 (A3DBX3), Bacillus pumilus US570 (A0A0F6QU36), Bacillus subtilis SU40 (G0YW23), Paenibacillus barcinonensis BP-23 (A0A097QQT4), Acetivibrio thermocellus F7 (Q84C00), Acetivibrio thermocellus NCIMB 10682 (A3DBX3), Acetivibrio thermocellus NRRL B-4536 (A3DBX3)
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