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Information on EC 3.2.1.73 - licheninase and Organism(s) Acetivibrio thermocellus and UniProt Accession A3DBX3
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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: Acetivibrio thermocellus
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
-
-
-
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1,3-1,4-beta-D-glucan 4-glucanohydrolase
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-
-
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1,3-1,4-beta-D-glucan glucanohydrolase
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-
-
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1,3;1,4-beta-glucan 4-glucanohydrolase
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-
-
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1,3;1,4-beta-glucan endohydrolase
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-
-
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beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase
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-
-
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beta-1,3-1,4-glucanase
endo-beta-1,3-1,4 glucanase
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-
-
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laminarinase
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-
-
-
LicB
Lichenase
Mixed linkage beta-glucanase
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-
-
-
Lichenase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
beta-1,3-1,4-glucanase catalyzes strict endo-hydrolysis of the beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in the mixed-linked beta-glucans via a double-displacement mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
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SYSTEMATIC NAME
IUBMB Comments
(1->3)-(1->4)-beta-D-glucan 4-glucanohydrolase
Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.
CAS REGISTRY NUMBER
COMMENTARY
37288-51-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
?
additional information
?
-
-
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
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-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
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-
?
additional information
?
-
-
no activity against beta-1,4- or beta-1,3 homopolymers of gluco- or manno-configured polysaccharides
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-
?
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
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-
?
additional information
?
-
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
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-
?
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
?
-
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
?
-
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
?
additional information
?
-
-
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
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
?
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
Ca2+ stabilizes the enzyme at higher temperatures
additional information
-
no effects by 10 mM of Na+, K+, Ca2+, and Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
poor inhibition at 10 mM by Co2+ and EDTA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.3
Glcbeta3Glcbeta-methylumbelliferone
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pH 7.0, 37°C, 50 mM sodium phosphate buffer
additional information
additional information
KM value for native enzyme, substrate beta-D-glucan, is 2.7 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1.2 mg/ml
-
additional information
additional information
-
KM value for native enzyme, substrate beta-D-glucan, is 2.7 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1.2 mg/ml
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additional information
additional information
-
1.65 mg/ml with beta-1,3-1,4-glucan, at pH 6.0, 70°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 51 ml/mg/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1014 ml/mg/min
-
additional information
additional information
-
kcat/KM value for native enzyme, substrate beta-D-glucan, is 51 ml/mg/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1014 ml/mg/min
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
80
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 80
55 - 90
-
55°C: about 50% of maximal activity, 90°C: about 30% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
beta-1,3-1,4-glucanases from various microorganisms and plants belong to glycoside hydrolase families 16 and 17, respectively
additional information
-
in silico analysis and structure homology modelling of the enzyme's catalytic domain, LicBM3, secondary structure
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
x * 28000, about, recombinant catalytic domain, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure to 1.95 A resolution. The enzyme folds into a classic GH16 beta-jellyroll architecture which consists of two beta-sheets atop each other, with the substrate-binding cleft lying on the concave side of the inner beta-sheet. Two BisTris propane molecules are in the positive and negative substrate binding sites
purified recombinant catalytic domain, sitting drop vapour diffusion method, mixing of 0.002 ml of 30 mg/ml protein in 25 mM Tris pH 7.5, 150 mM NaCl, and 0.002 ml reservori solution containing 0.04 M citric acid, 0.06 M Bis-Tris propane, pH 6.4, 18% w/v PEG 3350, 25°C, 7 days, optimized method, X-ray diffraction structure determination and analysis at 1.95 A resolution, molecular replacement method
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of diverse enzyme truncation mutants for domain functional analysis, overview
additional information
-
generation of transgenic Nicotiana tabacum plants expressing LicB from Clostridium thermocellum, no altered phenotype, overview. Expression of bacterial beta-1,3-1,4-glucanase gene exerts no significant influence on tobacco plant metabolism, while the expression of bacterial beta-1,3-glucanase affects plant metabolism only at early stages of growth and development. By contrast, the expression of bacterial beta-1,4-glucanase has a significant effect on transgenic tobacco plant metabolism
additional information
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
additional information
-
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
additional information
-
construction of hybrid genes encoding circularly permutated lichenase variants with integrated small peptides, i.e. NC-L-53, NC-L-99, NC-L-53-99, and NC-L-140, method overview. Generation of a thermostable lichenase gene variant encoding only the enzyme's catalytic domain LicBM3. Thermostabilities of the mutant constructs, overview
additional information
end-to-end fusion, circular permutation, domain insertion
additional information
end-to-end fusion, circular permutation, domain insertion
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
purified recombinant enzyme, pH 7.0, 40% activity remaining after 6 h
75
-
purified recombinant wild-type enzyme, 10 min, 51% remaining activity in absence of Ca2+, 86% in presence of 1 mM Ca2+
80
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
80
-
purified recombinant wild-type enzyme, 5 min, 54% remaining activity in absence of Ca2+, 73% in presence of 1 mM Ca2+
80
-
purified recombinant enzyme, pH 7.0, no activity remaining after 1 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged isolated catalytic domain of the enzyme from Escherichia coli strain BL21trxB(DE3) by nickel affinity chromatography and dialysis, tag cleavage by factor Xa digestion, and removal of the tag by another step of nickel affinity chromatography
immobilized metal ion affinity chromatography, gel filtration, anion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris and Escherichia coli, recombinant enzmye expressed in Pichia pastoris shows higher specific activity
expression of the His-tagged isolated catalytic domain of the enzyme, residues 31-251, in Escherichia coli strain BL21trxB(DE3) with an extra linker AGAGA at its N-terminus
gene licB, recombinant expression in Escherichia coli and in Pichia pastoris
expression in Escherichia coli
expression of wild-type enzyme and mutant circular enzyme constructs in Escherichia coli strain XL1-Blue
-
gene bglS, recombinant expression in Escherichia coli, in Saccharomyces cerevisiae, in plants, and in mammalian cells, the enzyme is secreted
gene LicB, expression of mature enzyme and isolated catalytic domain, as well as of the enzyme truncation mutants in Escherichia coli strain BL21
-
recombinant expression and secretion from Bacillus subtilis strain WB800 using vector pP43JM2
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilizedon commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed
food industry
synthesis
additional information
food industry
-
the secretively produced beta-1,3-1,4-glucanase shows excellent thermostability up to 80°C and a wide pH range from pH 4 to pH 11 and has a potential in the food and animal feed applications
food industry
-
exogenous 1,3-1,4-beta-glucanases but not 1,4-beta-glucanases (EC 3.2.1.4) are obligatory enzymes to improve the nutritive value of barley-based diets for broilers. Enzyme is completely resistant to proteolytic inactivation after a 30 min incubation with pancreatic proteases
synthesis
-
the unusually resistance against inactivation by heat, ethanol or ionic detergents makes the enzyme highly suitable for industrial application in the mashing process of beer brewing
synthesis
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schimming, S.; Schwarz, W.H.; Staudenbauer, W.L.
Properties of a thermoactive beta-1,3-1,4-glucanase (lichenase) from Clostridium thermocellum expressed in Escherichia coli
Biochem. Biophys. Res. Commun.
177
447-452
1991
Acetivibrio thermocellus
Taylor, E.J.; Goyal, A.; Guerreiro, C.I.; Prates, J.A.; Money, V.A.; Ferry, N.; Morland, C.; Planas, A.; Macdonald, J.A.; Stick, R.V.; Gilbert, H.J.; Fontes, C.M.; Davies, G.J.
How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides: structure and activity of a Clostridium thermocellum lichenase, CtLic26A
J. Biol. Chem.
280
32761-32767
2005
Acetivibrio thermocellus
Chichester, J.A.; Musiychuk, K.; de la Rosa, P.; Horsey, A.; Stevenson, N.; Ugulava, N.; Rabindran, S.; Palmer, G.A.; Mett, V.; Yusibov, V.
Immunogenicity of a subunit vaccine against Bacillus anthracis
Vaccine
25
3111-3114
2007
Acetivibrio thermocellus
Niu, D.; Zhou, X.X.; Yuan, T.Y.; Lin, Z.W.; Ruan, H.; Li, W.F.
Effect of the C-terminal domains and terminal residues of catalytic domain on enzymatic activity and thermostability of lichenase from Clostridium thermocellum
Biotechnol. Lett.
32
963-967
2010
Acetivibrio thermocellus, Acetivibrio thermocellus ZJL4
Abdeev, R.M.; Abdeeva, I.A.; Bruskin, S.S.; Musiychuk, K.A.; Goldenkova-Pavlova, I.V.; Piruzian, E.S.
Bacterial thermostable beta-glucanases as a tool for plant functional genomics
Gene
436
81-89
2009
Acetivibrio thermocellus
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
Zhang, L.; Zhao, P.; Chen, C.C.; Huang, C.H.; Ko, T.P.; Zheng, Y.; Guo, R.T.
Preliminary X-ray diffraction analysis of a thermophilic beta-1,3-1,4-glucanase from Clostridium thermocellum
Acta Crystallogr. Sect. F
70
946-948
2014
Acetivibrio thermocellus (A3DBX3), Acetivibrio thermocellus, Acetivibrio thermocellus DSM 1237 (A3DBX3)
Luo, Z.; Gao, Q.; Li, X.; Bao, J.
Cloning of LicB from Clostridium thermocellum and its efficient secretive expression of thermostable beta-1,3-1,4-glucanase
Appl. Biochem. Biotechnol.
173
562-570
2014
Acetivibrio thermocellus, Acetivibrio thermocellus DSM 1237
Tyurin, A.; Sadovskaya, N.; Nikiforova, K.; Mustafaev, O.; Komakhin, R.; Fadeev, V.; Goldenkova-Pavlova, I.
Clostridium thermocellum thermostable lichenase with circular permutations and modifications in the N-terminal region retains its activity and thermostability
Biochim. Biophys. Acta
1854
10-19
2015
Acetivibrio thermocellus
Jia, L.; Budinova, G.; Takasugi, Y.; Noda, S.; Tanaka, T.; Ichinose, H.; Goto, M.; Kamiya, N.
Synergistic degradation of arabinoxylan by free and immobilized xylanases and arabinofuranosidase
Biochem. Eng. J.
114
268-275
2016
Acetivibrio thermocellus (P10478), Acetivibrio thermocellus DSM 1237 (P10478)
-
Chen, C.C.; Huang, J.W.; Zhao, P.; Ko, T.P.; Huang, C.H.; Chan, H.C.; Huang, Z.; Liu, W.; Cheng, Y.S.; Liu, J.R.; Guo, R.T.
Structural analyses and yeast production of the beta-1,3-1,4-glucanase catalytic module encoded by the licB gene of Clostridium thermocellum
Enzyme Microb. Technol.
71
1-7
2015
Acetivibrio thermocellus (A3DBX3), Acetivibrio thermocellus, Acetivibrio thermocellus DSM 1237 (A3DBX3)
Fernandes, V.; Costa, M.; Ribeiro, T.; Serrano, L.; Cardoso, V.; Santos, H.; Lordelo, M.; Ferreira, L.; Fontes, C.
1,3-1,4-beta-Glucanases and not 1,4-beta-glucanases improve the nutritive value of barley-based diets for broilers
Anim. Feed Sci. Technol.
211
153-163
2016
Acetivibrio thermocellus
-
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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