3.2.1.73: licheninase
This is an abbreviated version!
For detailed information about licheninase, go to the full flat file.
Word Map on EC 3.2.1.73
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3.2.1.73
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cellulases
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cellulolytic
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trichoderma
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knee
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reesei
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cellobiohydrolase
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exoglucanase
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thermocellum
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avicel
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carboxymethyl
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lignocellulosic
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cellulosic
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arthroscopic
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saccharification
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beta-glucosidase
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carboxymethylcellulose
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cellulose-binding
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straw
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microcrystalline
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glutenins
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cellulosome
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bagasse
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cellotriose
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lichenan
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xyloglucans
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cellulomonas
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cellotetraose
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xylanases
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3.2.1.4
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hemicellulases
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cmcase
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patellar
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endo-beta-1,4-glucanase
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patellofemoral
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succinogenes
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endoxylanase
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dockerins
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humicola
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fpase
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fibrobacter
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cellulose-degrading
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lysholm
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lignocellulolytic
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mannanase
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cellodextrins
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meniscal
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cellobiase
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thermobifida
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xylanolytic
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brewing
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synthesis
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endocellulase
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agriculture
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biofuel production
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degradation
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food industry
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analysis
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industry
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nutrition
- 3.2.1.73
- cellulases
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cellulolytic
- trichoderma
- knee
- reesei
- cellobiohydrolase
- exoglucanase
- thermocellum
- avicel
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carboxymethyl
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lignocellulosic
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cellulosic
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arthroscopic
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saccharification
- beta-glucosidase
- carboxymethylcellulose
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cellulose-binding
- straw
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microcrystalline
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glutenins
- cellulosome
- bagasse
- cellotriose
- lichenan
- xyloglucans
- cellulomonas
- cellotetraose
- xylanases
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3.2.1.4
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hemicellulases
- cmcase
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patellar
- endo-beta-1,4-glucanase
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patellofemoral
- succinogenes
- endoxylanase
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dockerins
- humicola
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fpase
- fibrobacter
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cellulose-degrading
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lysholm
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lignocellulolytic
- mannanase
- cellodextrins
- meniscal
- cellobiase
- thermobifida
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xylanolytic
- brewing
- synthesis
- endocellulase
- agriculture
- biofuel production
- degradation
- food industry
- analysis
- industry
- nutrition
Reaction
Synonyms
(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 glucanohydrolase, 1,3-1,4-beta-D-glucan-4-glucano hydrolase, 1,3-1,4-beta-D-glucanase, 1,3-1,4-beta-glucanase, 1,3;1,4-beta-glucan 4-glucanohydrolase, 1,3;1,4-beta-glucan endohydrolase, Af-EGL7, Afu6g01800, Beg1, beta-(1,3-1,4)-glucanase, beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase, beta-1,3-1,4 glucanase, beta-1,3-1,4-D-glucanase, beta-1,3-1,4-glucanase, beta-1,3;1,4-glucanase, beta-1-3, 1-4 glucan 4-glucanohydrolase, beta-glucanase, BG1, Bg1314, Bga1, bgc, bgi, Bgl, bgl5-1, BglA, BglA13, BglA16, BglA51, BglBB, bglBC1, BGlc8H, BglM2, BglS, BglT, BglTO, Bglu16A, bifunctional xylanase/endoglucanase, BLB369, BLB369 endo-beta-1,3-1,4-glucanase, Blc8H, BP_Cel9A, Cel5F, CP7 beta-1,3-1,4-glucanase, CtGlu16A, Cthe_0211, CtLic16A, CtLic26A, E-LICHN, EG1, EGL, EII, endo-(1,3)(1,4)-beta-glucanase, endo-(1,3;1,4)-beta-glucanase, endo-beta-1,3-1,4 glucanase, endo-beta-1,3-1,4-glucanase, endo-beta-1,3;1,4-glucan-D-glycosyl hydrolase, endo-beta-glucanase, endoglucanase, endotype beta-1,3-1,4-glucanase, Fisuc_2961, Fsbeta-glucanase, FSU_0226, Gcs2, GH7 endo-1,4-beta-glucanase, GHF16 TFsbeta-glucanase, GHF17 barley 1,3-1,4-beta-D-glucanase, Glc16A, GLU-1, GLU-3, glu369, Gluc5_26A, GluIII, GluUS570, glycoside hydrolase family 9 endoglucanase, GyrA, H(A16-M), lam1, LamA, laminarinase, Lic16A, Lic8H, LicA, LicB, Lichenase, lichenase-2, LicKM, licM, LicMB, LicS, McLic1, mHG, Mixed linkage beta-glucanase, More, NFEg16A, PbBglu16A, PlicA, PtLic16A, Ra0505, RuCelA, TaGlu34, TC2, TC5, TF-glu, TF-glucanase, theme C glycoside hydrolase family 9 endo-beta-glucanase, TM1752, US8_01508, XynIII, XynZ, ZgLamA
ECTree
3.2.1.73 licheninaseAdvanced search results
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results (Application
Application on EC 3.2.1.73 - licheninase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
agriculture
analysis
biofuel production
RuCelA can produce xylo-oligosaccharides and cell-oligosaccharides in the continuous saccharification of pretreated rice straw, which can be further degraded into fermentable sugars. Therefor, the bifunctional RuCelA distinguishes itself as an ideal candidate for industrial application
brewing
degradation
food industry
industry
nutrition
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the enzyme is able to reduce both the viscosity of the brewer mash and the filtration time, indicating its potential value for the brewing industry
synthesis
additional information
agriculture
1,3-1,4-beta-D-glucanase are widely used as a feed additive to help non-ruminant animals digest plant fibers, with potential in increasing nutrition turnover rate and reducing sanitary problems
agriculture
overexpression of barley (1->3,1->4)-beta-glucanase isoenzyme EII under the control of a promoter of barley D-Hordein gene Hor3-1 in barley cultivar Golden Promise. The T2 generation of transgenic lines shows increased activity of glucanase in grains. Total beta-glucan content is reduced by more than 95.73% in transgenic grains compared with the wild-type control. Overexpression leads to an increase in 1000-grain weight, which might be due to elevated amounts of starch in the grain
agriculture
enzyme shows the ability to inhibit the growth of phytopathogenic fungus Alternaria alternata
analysis
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the enzyme is used for oligosaccharide profiling of mixed-linkage glucan, beta-1,3-1,4-glucan, a characteristic hemicellulose in primary cell walls of grasses, that adsorps onto microcrystalline cellulose in a slow, irreversible, and temperature-dependent manner. The binding of the oligomer is reduced if the cellulose samples are first treated with certain cell wall polysaccharides, such as xyloglucan and glucuronoarabinoxylan
analysis
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assay procedure for the measurement of beta-glucanase and lichenase in crude enzyme extracts. Substrate 4,6-O-benzylidene-2-chloro-4-nitrophenyl-beta-3'-cellotriosyl-beta-glucopyranoside is a more generally applicable reagent. Standard curves allow the assay absorbance response to be directly converted to beta-glucanase/lichenase activity on barley beta-glucan. Manual and automated assay formats aloow the analysis of beta-glucanase in malt flour and lichenase enzyme extracts and the assays are repeatable
brewing
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the enzyme is a candidate for the production of beta-gluco-oligosaccharides and in brewing industry
brewing
Paenibacillus barengoltzii CAU904
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the enzyme is a candidate for the production of beta-gluco-oligosaccharides and in brewing industry
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degradation
hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilizedon commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed
degradation
the saccharification of untreated reed and rice straw powders by commercial enzymes (Celluclast 1.5 L and Novozym 188) is increased by 10.4 and 4.8%, respectively, by the addition of BGlc8H. In the presence of Ca2+ and BGlc8H, the saccharification of the pretreated reed and rice straw powders by the commercial enzymes is increased by 18.5 and 11.7%, respectively
degradation
fermentation capacity of recombinant Bacillus subtilis expressing mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P reaches 242.02 U ml/h. The addition of the mutant protein in Congress mashing significantly reduces the filtration time and viscosity of mash by 29.7% and 12.3%, respectively
degradation
Acetivibrio thermocellus DSM 1237
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hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilizedon commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed
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degradation
Bacillus tequilensis CGX 5-2
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fermentation capacity of recombinant Bacillus subtilis expressing mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P reaches 242.02 U ml/h. The addition of the mutant protein in Congress mashing significantly reduces the filtration time and viscosity of mash by 29.7% and 12.3%, respectively
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food industry
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the enzyme is a good candidate in the malting and brewing industry reducing the filtration time and viscosity of mash from barley grains, overview
food industry
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the enzyme is considered as a candidate for application particularly in the animal feed industry
food industry
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the secretively produced beta-1,3-1,4-glucanase shows excellent thermostability up to 80°C and a wide pH range from pH 4 to pH 11 and has a potential in the food and animal feed applications
food industry
the thermostable enzyme can be useful in mashing at 72°C of brewing processes
food industry
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enzyme can promote mashing with a reduced filtration time (14.0%) and viscosity (3.4%)
food industry
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exogenous 1,3-1,4-beta-glucanases but not 1,4-beta-glucanases (EC 3.2.1.4) are obligatory enzymes to improve the nutritive value of barley-based diets for broilers. Enzyme is completely resistant to proteolytic inactivation after a 30 min incubation with pancreatic proteases
food industry
the addition of mutant K20S/N31c/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P in congress mashing decreases the filtration time and viscosity by 21.3 and 9.6 %, respectively
food industry
the enzyme is used for production and processing of alcoholic beverages
food industry
the enzyme is used for production of oligomers as prebiotics
food industry
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the thermostable enzyme can be useful in mashing at 72°C of brewing processes
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food industry
Acetivibrio thermocellus DSM 1237
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the secretively produced beta-1,3-1,4-glucanase shows excellent thermostability up to 80°C and a wide pH range from pH 4 to pH 11 and has a potential in the food and animal feed applications
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food industry
Paenibacillus barengoltzii CAU904
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enzyme can promote mashing with a reduced filtration time (14.0%) and viscosity (3.4%)
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food industry
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the enzyme is considered as a candidate for application particularly in the animal feed industry
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food industry
Bacillus subtilis NCIB 8565
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the enzyme is used for production and processing of alcoholic beverages
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food industry
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the enzyme is used for production of oligomers as prebiotics
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food industry
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the enzyme is a good candidate in the malting and brewing industry reducing the filtration time and viscosity of mash from barley grains, overview
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industry
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properties make the enzyme highly suitable for industrial applications
industry
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properties make the enzyme highly suitable for industrial applications
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synthesis
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the unusually resistance against inactivation by heat, ethanol or ionic detergents makes the enzyme highly suitable for industrial application in the mashing process of beer brewing
synthesis
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
synthesis
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
synthesis
over-expression in Pichia pastoris, with a yield of about 1000 U/ml in a 3.7 l fermentor
synthesis
upon expression in Pichia pastoirs as active extracellular beta-1,3-1,4-glucanase, the recombinant protein is secreted predominantly into the medium and comprises up to 85% of the total extracellular proteins and reaches a protein concentration of 9.1 g/l with an activity of 55,300 U/ml in 5-l fermentor culture
synthesis
analysis of fermentation conditions for beta-1,3-1,4-glucanase production under solid-state fermentation. Under the optimized fermentation conditions, viz. oatmeal as sole carbon source, 5% (w/w) peptone as sole nitrogen source, initial moisture of 80% (w/w), initial culture pH of 5.0, incubation temperature of 50°C and incubation time of 6 days, the highest beta-1,3-1,4-glucanase activity of 20025 U/g dry substrate is achieved. The addition of the purified beta-1,3-1,4-glucanase in mash obviously reduces its filtration time (24.6%) and viscosity (2.61%)
synthesis
expression of mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P in Bacillus subtilis to maximal extracellular activity of 4840.4 U/ml
synthesis
immobilization of enzyme on porous silica using glutaraldehyde. Enzyme activity decreases sharply at high concentrations of glutaraldehyde. Immobilized protein is stable over a wide range of pH and can be stored long term at 4°C. After 10 cycles, the enzyme retains 42% of its initial catalytic activity
synthesis
the enzyme can be used in the production of anti-hypercholesterolemic agents
synthesis
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analysis of fermentation conditions for beta-1,3-1,4-glucanase production under solid-state fermentation. Under the optimized fermentation conditions, viz. oatmeal as sole carbon source, 5% (w/w) peptone as sole nitrogen source, initial moisture of 80% (w/w), initial culture pH of 5.0, incubation temperature of 50°C and incubation time of 6 days, the highest beta-1,3-1,4-glucanase activity of 20025 U/g dry substrate is achieved. The addition of the purified beta-1,3-1,4-glucanase in mash obviously reduces its filtration time (24.6%) and viscosity (2.61%)
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synthesis
Niallia circulans ATCC 21367
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the enzyme can be used in the production of anti-hypercholesterolemic agents
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synthesis
Bacillus tequilensis CGX 5-2
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expression of mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P in Bacillus subtilis to maximal extracellular activity of 4840.4 U/ml
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additional information
the alkaline beta-1,3-1,4-glucanase may have potential in industrial applications, such as detergent, paper and pulp industries
additional information
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the alkaline beta-1,3-1,4-glucanase may have potential in industrial applications, such as detergent, paper and pulp industries
additional information
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
Bacillus sp. N137
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
additional information
upon addition to a commercial cellulase cocktail, Af-EGL7 significantly improves sugarcane exploded bagasse (SEB) saccharification, which suggests that enzyme Af-EGL7 has great potential to hydrolyze complex biomass. Af-EGL7 is a promising candidate to enhance enzyme cocktails used in biorefineries such as consolidated bioprocessing
additional information
-
upon addition to a commercial cellulase cocktail, Af-EGL7 significantly improves sugarcane exploded bagasse (SEB) saccharification, which suggests that enzyme Af-EGL7 has great potential to hydrolyze complex biomass. Af-EGL7 is a promising candidate to enhance enzyme cocktails used in biorefineries such as consolidated bioprocessing
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
Acetivibrio thermocellus DSM 1237
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
Acetivibrio thermocellus NBRC 103400
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
-
additional information
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
Aspergillus fumigatus CBS 101355
-
upon addition to a commercial cellulase cocktail, Af-EGL7 significantly improves sugarcane exploded bagasse (SEB) saccharification, which suggests that enzyme Af-EGL7 has great potential to hydrolyze complex biomass. Af-EGL7 is a promising candidate to enhance enzyme cocktails used in biorefineries such as consolidated bioprocessing
-
additional information
Bacillus subtilis NCIB 8565
-
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
-
upon addition to a commercial cellulase cocktail, Af-EGL7 significantly improves sugarcane exploded bagasse (SEB) saccharification, which suggests that enzyme Af-EGL7 has great potential to hydrolyze complex biomass. Af-EGL7 is a promising candidate to enhance enzyme cocktails used in biorefineries such as consolidated bioprocessing
-
additional information
Niallia circulans ATCC 21367
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
Rhodothermus marinus ITI378
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
-
additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
Acetivibrio thermocellus VPI 7372
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
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additional information
Bacillus pumilus US570
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
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additional information
-
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
-
additional information
Aspergillus fumigatus FGSC A1100
-
upon addition to a commercial cellulase cocktail, Af-EGL7 significantly improves sugarcane exploded bagasse (SEB) saccharification, which suggests that enzyme Af-EGL7 has great potential to hydrolyze complex biomass. Af-EGL7 is a promising candidate to enhance enzyme cocktails used in biorefineries such as consolidated bioprocessing
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additional information
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
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additional information
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upon addition to a commercial cellulase cocktail, Af-EGL7 significantly improves sugarcane exploded bagasse (SEB) saccharification, which suggests that enzyme Af-EGL7 has great potential to hydrolyze complex biomass. Af-EGL7 is a promising candidate to enhance enzyme cocktails used in biorefineries such as consolidated bioprocessing
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additional information
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
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additional information
Acetivibrio thermocellus NCIMB 10682
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
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additional information
Acetivibrio thermocellus NRRL B-4536
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application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production
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additional information
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the alkaline beta-1,3-1,4-glucanase may have potential in industrial applications, such as detergent, paper and pulp industries
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