3.2.1.4: cellulase
This is an abbreviated version!
For detailed information about cellulase, go to the full flat file.
Word Map on EC 3.2.1.4
-
3.2.1.4
-
cellulose
-
trichoderma
-
biomass
-
reesei
-
xylanase
-
cellulolytic
-
saccharification
-
lignocellulosic
-
cellobiose
-
straw
-
lignin
-
polysaccharide
-
aspergillus
-
glycoside
-
beta-glucosidase
-
corn
-
biofuels
-
pectinase
-
xylan
-
hemicellulose
-
bagasse
-
penicillium
-
endoglucanases
-
bioethanol
-
xylose
-
amylase
-
polygalacturonase
-
sugarcane
-
carbohydrate-binding
-
feedstock
-
viride
-
glucans
-
thermocellum
-
bran
-
carboxymethylcellulose
-
microcrystalline
-
exoglucanase
-
cellulose-binding
-
laccase
-
biorefinery
-
rumen
-
biotechnology
-
analysis
-
novozyme
-
silage
-
endoxylanase
-
compost
-
industry
-
textile industry
-
food industry
-
biofuel production
-
agriculture
-
deconstruct
-
xylobiose
-
diagnostics
-
harzianum
-
degradation
-
chrysosporium
-
synthesis
-
detergent
-
environmental protection
-
xyloglucans
- 3.2.1.4
- cellulose
- trichoderma
- biomass
- reesei
- xylanase
-
cellulolytic
-
saccharification
-
lignocellulosic
- cellobiose
- straw
- lignin
- polysaccharide
- aspergillus
- glycoside
- beta-glucosidase
- corn
-
biofuels
- pectinase
- xylan
- hemicellulose
- bagasse
- penicillium
- endoglucanases
-
bioethanol
- xylose
- amylase
- polygalacturonase
- sugarcane
-
carbohydrate-binding
-
feedstock
- viride
- glucans
- thermocellum
- bran
- carboxymethylcellulose
-
microcrystalline
- exoglucanase
-
cellulose-binding
- laccase
-
biorefinery
- rumen
- biotechnology
- analysis
-
novozyme
-
silage
- endoxylanase
-
compost
- industry
- textile industry
- food industry
- biofuel production
- agriculture
-
deconstruct
- xylobiose
- diagnostics
- harzianum
- degradation
- chrysosporium
- synthesis
- detergent
- environmental protection
- xyloglucans
Reaction
Synonyms
(1->4)-beta-D-glucan 4-glucanohydrolase, 1,4-beta-D-endoglucanase, 1,4-beta-D-glucan-4-glucanohydrolase, 168cel5, 9.5 cellulase, Abscission cellulase, AEG, Ag-EGase III, AgCMCase, alkali cellulase, Alkaline cellulase, AnCel5A, AtCel5, ATEG_07420, avicelase, BC-EG70a, Bc22Cel, BCE1, BcsZ, beta-1,4-endoglucan hydrolase, beta-1,4-endoglucanase, beta-1,4-glucanase, Bgl7A, bifunctional endoglucanase/xylanase, BlCel9, BP_Cel9A, Bx-ENG-1, Bx-ENG-2, Bx-ENG-3, C4endoII, carbomethyl cellulase, Carboxymethyl cellulase, Carboxymethyl-cellulase, carboxymethylcellulase, Cat 1, Caylase, CBH45-1, cbh6A, CBHI, CBHII, CcCel6C, CEL1, Cel1 EGase, Cel12A, Cel1753, Cel28a, Cel44A, Cel45A, Cel48A, Cel5, Cel5A, cel5B, Cel5E, Cel6A, Cel6A (E2), Cel6B, Cel6C, CEL7, Cel7A, Cel7B, Cel8, Cel8A, Cel8M, Cel8Y, Cel9A, CEL9A-50, CEL9A-65, Cel9A-68, CEL9A-82, Cel9A-90, Cel9B, CEL9C1, Cel9K, Cel9M, Cel9Q, CelA, CelB, CelC2 cellulase, CelCM3, CelDR, CelE, CelF, Celf_1230, Celf_3184, CelG, CelG endoglucanase, CelI15, cell-bound bacterial cellulase, CelL15, CelL73, cellic Ctec2, cellobiohydrolase, cellobiohydrolase I, celluase A, Celluclast, celludextrinase, Cellulase, cellulase 12A, cellulase A, cellulase A 3, cellulase Cel48F, cellulase Cel9A, cellulase Cel9M, cellulase CelC2, cellulase CelE, cellulase CM3, Cellulase E1, Cellulase E2, Cellulase E4, Cellulase E5, cellulase EGX, cellulase II, cellulase III, cellulase K, Cellulase SS, cellulase T, Cellulase V1, cellulase Xf818, cellulases I, cellulases III, cellulosin AP, Cellulysin, CelP, celS, CelStrep, celVA, CelX, CenA, CenC, CfCel6A, CfCel6C, CfEG3a, CHU_1280, CHU_2103, CjCel9A, Clocel_2741, CMCase, CMCase-I, CMCax, CMcellulase, Csac_1076, Csac_1078, CSCMCase, ctCel9D-Cel44A, CTendo45, ctendo7, CtGH5, Cthe_0435, CTHT_0045780, CX-cellulase, CyPB, DCC85_10145, DK-85, Dockerin type 1, Dtur_0671, E1 endoglucanase, Econase, EfPh, EG I, EG III, EG1, EG12, EG2, EG25, EG271, EG28, EG3, EG35, EG44, EG47, EG51, Eg5a, EG60, EGA, EGase, EGase II, EGB, EGC, EGCCA, EGCCC, EGCCD, EGCCF, EGCCG, EGD, EGE, EGF, egGH45, EGH, EGI, EGII, EGII/Cel5A, EGIV, EGL, EGL 1, Egl-257, Egl1, Egl499, Egl5a, EglA, eglB, EglC, EGLII, EglS, EGM, EGPf, EGPh, EGSS, EgV, EGX, EGY, EGZ, endo-1,4-B-glucanase, endo-1,4-beta-D-glucanase, endo-1,4-beta-glucanase, endo-1,4-beta-glucanase 1, endo-1,4-beta-glucanase 2, endo-1,4-beta-glucanase E1, endo-1,4-beta-glucanase V1, endo-beta-1,3-1,4-glucanase, endo-beta-1,4-glucanase, endo-beta-1,4-glucanase 1, endo-beta-1,4-glucanase 2, endo-beta-1,4-glucanase CMCax, endo-beta-1,4-glucanase EG27, endo-beta-1,4-glucanase EG45, endo-beta-D-1,4-glucanohydrolase, endo-beta-glucanase, endo-glucanase, ENDO1, ENDO2, endocellulase, endocellulase E1, endocellulases I, endocellulases II, endocellulases III, endocellulases IV, endogenous beta-1,4-endoglucanase, endogenous cellulase, endoglucanase, endoglucanase 1, endoglucanase 35, endoglucanase 47, endoglucanase CBP105, endoglucanase Cel 12A, endoglucanase Cel 5A, endoglucanase Cel 7B, endoglucanase Cel5A, endoglucanase Cel6A, endoglucanase D, endoglucanase EG-I, endoglucanase EG25, endoglucanase EG28, endoglucanase EG44, endoglucanase EG47, endoglucanase EG51, endoglucanase EG60, endoglucanase H, endoglucanase II, endoglucanase IIa, endoglucanase IV, endoglucanase L, endoglucanase M, endoglucanase V, endoglucanase Y, endolytic cellulase, EngA, EngH, EngL, EngM, engXCA, EngY, EngZ, family 7 cellobiohydrolase, FI-CMCASE, FnCel5A, FpCel45, Fpcel45a, GE40, GE40 endoglucanase, GH12 endo-1,4-beta-glucanase, GH124 endoglucanase, GH45 endoglucanase, gh45-1, GH5 cellulase, GH5 endoglucanase, GH6 endoglucanase, GH7 endoglucanase, GH9 termite cellulase, Glu1, Glu2, glycoside hydrolase family 9 endoglucanase, GtGH45, Lp-egl-1, manganese dependent endoglucanase, Maxazyme, Meicelase, mesophilic endoglucanase, mgCel6A, More, MtGH45, nmGH45, Onozuka R10, pancellase SS, PaPopCel1, PF0854, PH1171, PttCel9A, RCE1, RCE2, Roth 3056, RtGH124, Rucel5B, Sl-cel7, Sl-cel9C1, SnEG54, SoCel5, ssgluc, SSO1354, SSO1354 enzyme, SSO1354 protein, SSO1949, SSO2534, STCE1, Sumizyme, T12-GE40, TC Serva, TeEG-I, TeEgl5A, TfCel9A, ThEG, theme C glycoside hydrolase family 9 endo-beta-glucanase, Thermoactive cellulase, thermostable carboxymethyl cellulase, THITE_2110957, TM_1525, TM_1751, umcel5G, umcel9y-1, Vul_Cel5A
ECTree
3.2.1.4 cellulaseAdvanced search results
results (
results (Application
Application on EC 3.2.1.4 - cellulase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
agriculture
analysis
biofuel production
biotechnology
degradation
detergent
diagnostics
-
labeled Trichoderma reesei cellulase is useful as a marker for Acanthamoeba cyst wall cellulose in infected tissues
environmental protection
food industry
industry
synthesis
textile industry
-
enzymatic deinking experiments, the ink removal rate in samples treated with the catalytic module is only slightly higher (about 8%), than that of untreated controls, whereas that of the EG1-treated samples is 100% higher. Bio-stoning of denim with EG1-CM results in increases of 48% and 40% in weight loss and indigo dye removal, respectively compared with untreated controls. These increases are considerably lower than the corresponding values of 219% and 133% obtained when samples are treated with EG1
agriculture
in the treatment of agricultural waste at high temperature and low pH. Utilization in the biofuel industry after thermal pre-treatment in an acidic environment (e.g., steam explosion) of corncob, sugarcane bagasse and several types of agricultural waste to hydrolyze them down to fermentable sugars
agriculture
Saccharolobus solfataricus Oalpha
-
in the treatment of agricultural waste at high temperature and low pH. Utilization in the biofuel industry after thermal pre-treatment in an acidic environment (e.g., steam explosion) of corncob, sugarcane bagasse and several types of agricultural waste to hydrolyze them down to fermentable sugars
-
analysis
endo-beta-1,4-D-glucanase can be used as a marker to study root development in Arabidopsis
analysis
-
labeled Trichoderma reesei cellulase is useful as a marker for Acanthamoeba cyst wall cellulose in infected tissues
analysis
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. Hydrolysis by exo-acting enzymes such as beta-glucosidase and exo-beta-glucanase is prevented by the presence of the benzylidene group on the non-reducing end D-glucosyl residue. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture. The reaction is terminated and colour developed by the addition of a weak alkaline solution. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation
analysis
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. Hydrolysis by exo-acting enzymes such as beta-glucosidase and exo-beta-glucanase is prevented by the presence of the benzylidene group on the non-reducing end D-glucosyl residue. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture. The reaction is terminated and colour developed by the addition of a weak alkaline solution. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation
analysis
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. Hydrolysis by exo-acting enzymes such as beta-glucosidase and exo-beta-glucanase is prevented by the presence of the benzylidene group on the non-reducing end D-glucosyl residue. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture. The reaction is terminated and colour developed by the addition of a weak alkaline solution. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation
analysis
-
method for zymographic detection of specific cellulases in a complex (endocellulase, exocellulase, and cellobiase) from crude fermentation extracts, after a single electrophoretic separation. Cellulases are printed onto a membrane and, subsequently, substrate gel. Cellobiase isoforms are detected on the membrane using esculine as substrate, endocellulase isoforms on substrate gel with copolymerized carboxymethyl cellulose, while exocellulase isoforms are detected in electrophoresis gel with 4-methylumbelliferyl-beta-D-cellobioside
analysis
-
polymerization-based assay for determining the potency of cellulolytic enzyme formulations on pretreated biomass substrates by monitoring the autofluorescence of cellulose. The one-pot method is label-free, rapid, highly sensitive, and requires only a single pipetting step. Using model enzyme formulations derived from Trichoderma reesei, Trichoderma longibrachiatum, Talaromyces emersonii and recombinant bacterial minicellulosomes from Clostridium thermocellum, enzyme performance based on differences in thermostability, cellulose-binding domain targeting, and endo/exoglucanase synergy can be differentiated
analysis
-
screening for thermostable cellulase using 2% carboxymethyl cellulose and congo red as an indicator at temperatures 0°C, 37°C, 45°C and 50°C,respectively. Eight isolates were selected for further screening and show the abilities to secrete cellulases by forming distinct halo zones on selective agar plate. The maximum halo zones ranging from 32 mm to 35 mm are obtained after 72 hours incubation at 50°C
analysis
-
construction of a pipeline based on Leishmania tarentolae cell-free system to characterize 30 putative thermostable endo-1,4-beta-glucanases and xylanases identified in public genomic databases. The system uses high-throughput assays for glucanase and xylanase activities that rely on solubilisation of labelled particulate substrates performed in multiwell plates
analysis
-
construction of a pipeline based on Leishmania tarentolae cell-free system to characterize 30 putative thermostable endo-1,4-beta-glucanases and xylanases identified in public genomic databases. The system uses high-throughput assays for glucanase and xylanase activities that rely on solubilisation of labelled particulate substrates performed in multiwell plates
analysis
-
construction of a pipeline based on Leishmania tarentolae cell-free system to characterize 30 putative thermostable endo-1,4-beta-glucanases and xylanases identified in public genomic databases. The system uses high-throughput assays for glucanase and xylanase activities that rely on solubilisation of labelled particulate substrates performed in multiwell plates
analysis
rapid, selective, quantitative assay based on substrate 44-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside and reaction of product 4,6-O-(3-oxobutylidene)-beta-D-cellotriose with beta-glucosidase
analysis
rapid, selective, quantitative assay based on substrate 44-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside and reaction of product 4,6-O-(3-oxobutylidene)-beta-D-cellotriose with beta-glucosidase
analysis
rapid, selective, quantitative assay based on substrate 44-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside and reaction of product 4,6-O-(3-oxobutylidene)-beta-D-cellotriose with beta-glucosidase
analysis
-
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. Hydrolysis by exo-acting enzymes such as beta-glucosidase and exo-beta-glucanase is prevented by the presence of the benzylidene group on the non-reducing end D-glucosyl residue. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture. The reaction is terminated and colour developed by the addition of a weak alkaline solution. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation
-
biofuel production
the enzyme is a candidate for the utilization of agro-industrial waste for fuel production
biofuel production
the enzyme is a tool for biomass conversion. The recombinant enzyme acts in high concentrations of ionic liquids and can therefore degrade alpha-cellulose or even complex cell wall preparations under those pretreatment conditions. The enzymatic conversion of lignocellulosic plant biomass into fermentable sugars is a crucial step in the production of biofuels
biofuel production
-
enzyme degrades carbohydrates of dried seaweed Ulva lactula. About 21 mg glucose/g of dry seaweed are obtained which can be further converted to bio-fuel
biofuel production
-
recycling of enzymes during cellulosic bioethanol production in a pilotscale stripper. When increasing the temperature (up to 65°C) or ethanol content (up to 7.5% w/v), the denaturation rate of the enzymes increases. Enzyme denaturation occurs slower when the experiments are performed in fiber beer compared to buffer only. At extreme conditions with high temperature (65°C) and ethanol content (7.5% w/v), polythylenglycol added to fiber beer has no enzyme stabilizing effect
biofuel production
-
potential of using the ionic liquids-tolerant extremophilic cellulases for hydrolysis of ionic liquids-pretreated lignocellulosic biomass, for biofuel production
biofuel production
-
potential of using the ionic liquids-tolerant extremophilic cellulases for hydrolysis of ionic liquids-pretreated lignocellulosic biomass, for biofuel production
biofuel production
-
enzymatic cell wall degradation of microalgae for biofuel production: of the Chlorella strains tested, only Chlorella emersonii CCAP211/11N shows sensitivity to cellulase. As these effects of cellulase are minor, cellulose does not appear to play a major role in cell wall integrity or permeability in most of the algal species and strains tested
biofuel production
-
its thermostability, resistance to heavy metal ions and specific activity make this enzyme an interesting candidate for industrial applications
biofuel production
the enzyme can be useful for production of bioethanol and biofuel
biofuel production
the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus has great potential in generating fermentable sugars from renewable agro-residues for biofuel and fine chemical industry. Application of the fusion enzyme (EG-M-Xyn)in combination with Ctec2 (commercial enzyme) in the saccharification leads to a 10-20% net increase in fermentable sugars liberated from pretreated rice straw in comparison to the Ctec2 alone
biofuel production
-
its thermostability, resistance to heavy metal ions and specific activity make this enzyme an interesting candidate for industrial applications
-
biofuel production
-
the enzyme is a tool for biomass conversion. The recombinant enzyme acts in high concentrations of ionic liquids and can therefore degrade alpha-cellulose or even complex cell wall preparations under those pretreatment conditions. The enzymatic conversion of lignocellulosic plant biomass into fermentable sugars is a crucial step in the production of biofuels
-
biofuel production
-
the enzyme can be useful for production of bioethanol and biofuel
-
biofuel production
Saccharolobus solfataricus Oalpha
-
the enzyme is a candidate for the utilization of agro-industrial waste for fuel production
-
biofuel production
-
the enzyme can be useful for production of bioethanol and biofuel
-
biofuel production
-
enzyme degrades carbohydrates of dried seaweed Ulva lactula. About 21 mg glucose/g of dry seaweed are obtained which can be further converted to bio-fuel
-
biofuel production
-
potential of using the ionic liquids-tolerant extremophilic cellulases for hydrolysis of ionic liquids-pretreated lignocellulosic biomass, for biofuel production
-
biotechnology
-
Production of immobilized enzyme on Sepabeads EC-BU (hydrophobic interactions are the driving force for the adsorption of the enzyme to the carrier)
biotechnology
-
considering its thermostable, alkali-stable, halostable and organic solvent-tolerant properties, the enzyme might be potentially useful for future applications in biotechnological processes
biotechnology
recombination of the catalytic domains of three glycoside hydrolase family 48 bacterial cellulases (Cel48), i.e. Clostridium cellulolyticum CelF, Clostridium stercorarium CelY, and Clostridium thermocellum CelS, to create a diverse library of Cel48 enzymes with an average of 106 mutations from the closest native enzyme. The library is based on the Clostridium thermocellum CelS architecture, which consists of a 70-kDa catalytic domain connected to the organism's respective dockerin domain. Large variations in properties such as the functional temperature range, stability, and specific activity on crystalline cellulose are found. Functional status and stability are predictable from simple linear models of the sequence-property data. Recombined protein fragments contribute additively to these properties in a given chimera
biotechnology
-
considering its thermostable, alkali-stable, halostable and organic solvent-tolerant properties, the enzyme might be potentially useful for future applications in biotechnological processes
-
biotechnology
-
recombination of the catalytic domains of three glycoside hydrolase family 48 bacterial cellulases (Cel48), i.e. Clostridium cellulolyticum CelF, Clostridium stercorarium CelY, and Clostridium thermocellum CelS, to create a diverse library of Cel48 enzymes with an average of 106 mutations from the closest native enzyme. The library is based on the Clostridium thermocellum CelS architecture, which consists of a 70-kDa catalytic domain connected to the organism's respective dockerin domain. Large variations in properties such as the functional temperature range, stability, and specific activity on crystalline cellulose are found. Functional status and stability are predictable from simple linear models of the sequence-property data. Recombined protein fragments contribute additively to these properties in a given chimera
-
degradation
cellulase is an industrially important enzyme for biomass saccharification at high temperature. beta-Glucan can be completely degraded to glucose at high temperature with a combination of the hyperthermophile Pyrococcus furiosus endocellulase (EGPf) and beta-glucosidase (BGLPf). beta-Glucans are polysaccharides of D-glucose monomers formed by beta(1->3),(1->4) mixed-linkage bonds. They occur most commonly as cellulose in plants, in the bran of cereal grains, the cell wall of baker's yeast, and in certain fungi, mushrooms, and bacteria
degradation
-
a statistical optimization approach involving Plackett-Burman design and response surface methodology on submerged fermentation using cane molasses medium results in the production of 72410, 36420, 32420 and 5180 U/l of xylanase, endo-beta-1,4-glucanase, exo-beta-1,4-glucanase, and beta-glucosidase, respectively, i.e. more than fourfold improvements in production of xylanolytic and cellulolytic enzymes. Addition of microparticles engineers fungal morphology and enhances enzymes production. Maximum sugar yield of 578.12 and 421.79 mg/g substrate for waste tea cup and rice straw, respectively, are achieved after 24 h
degradation
addition of Eg5A to cellobiase (i.e. cellobiohydrolase and beta-glucosidase) results in a 53% increasing saccharification of NaOH-pretreated barley straw, and the glucose release is 47% higher than with cellobiase treatment alone
degradation
addition of isoform Eg5A to cellobiase (cellobiohydrolase and beta-glucosidase) results in a 53% increasing saccharification of NaOH-pretreated barley straw, whereas the glucose release is 47% higher than that cellobiase treatment alone
degradation
-
after hydrolysis and fermentation of wheat straw a significant amount of active enzymes can be recovered by recycling the liquid phase. In the early stage of the process, enzyme adsorbs to the substrate, then gradually returning to the solution as the saccharification proceeds. The hydrolysis yield and enzyme recycling efficiency in consecutive recycling rounds can be increased by using high enzyme loadings and moderate temperatures. The amount of enzymes in the liquid phase increases with its thermostability and hydrolytic efficiency
degradation
-
bioethanol production by Aspergillus fumigatus JCF at optimised growth conditions and Saccharomyces cerevisiae for simultaneous saccharification and fermentation. Using cotton seed as the substrate, maximum bioethanol concentration of 6.7 g/l can be achieved
degradation
cellulase complex containing cellulolytic enzymes,endoglucanase CelE, EC 3.2.1.4, and beta-glucosidase BglA, EC 3.2.1.21, to completely degrade cellulose to glucose. The cellulases are displayed on the cell surface of Corynebacterium glutamicum by using themechanosensitive channel to anchor enzymes in the cytoplasmic membrane. The displayed cellulases complexes have a synergic effect on the direct conversion of biomass to reducing sugars leading to 3.1- to 6.0fold increase compared to the conversion by the secreted cellulases complexes. The displayed cellulases complexes increase the residual activities of cCelEand cBglA at 70°C from 28.3% and 24.3% in the secreted form to 65.1% and 82.8%, respectively
degradation
-
during cultivation, consortium SV79 produces the maximum filter paper activity (FPase, 9.41 U/ml), carboxymethylcellulase activity (CMCase, 6.35 U/ml), and xylanase activity (4.28 U/ml) with sugarcane bagasse, spent mushroom substrate, and Sorbus anglica, respectively. The ethanol production using Miscanthus floridulus as substrate is up to 2.63 mM ethanol/g
degradation
-
effect of nickel-cobaltite (NiCo2O4) nanoparticles on production and thermostability of the cellulase enzyme system. Maximum production of endoglucanase (211 IU/gds), beta-glucosidase (301 IU/gds), and xylanase (803 IU/gds) is achieved after 72 h without nanoparticles, while in the presence of 1 mM of nanoparticles, endoglucanase, beta-glucosidase, and xylanase activity increase by about 49, 53, and 19.8%, respectively, after 48 h of incubation. Crude enzyme is thermally stable for 7 h at 80°C in presence of nanoparticles, as against 4 h at the same temperature for control samples
degradation
-
effects of microalgal biomass particle on the degree of enzymatic hydrolysis and bioethanol production by single enzyme hydrolysis (cellulase) and double enzyme hydrolysis (cellulase and cellobiase). The glucose yield from biomass in the smallest particle size range examined, i.e. 35 microm to 90 microm, is the highest, 134.73 mg glucose/g algae, while the yield from biomass in the larger particle size range from 295 microm to 425 microm is 75.45mg glucose/g algae. A similar trend is observed for bioethanol yield, with the highest yield of 0.47 g EtOH/g glucose obtained from biomass in the smallest particle size range
degradation
-
enzyme extracts obtained from growing Acrophialophora nainiana on cellulose, dirty-cotton residue, sugarcane bagasse and banana stem can be used in the hydrolysis of sugarcane bagasse, untreated, pre-treated by steam explosion and pretreated by acid-catalysed steam explosion. The carbohydrase activity profile of the enzyme preparations varies significantly with the used carbon source. The highest enzyme activities, especially total cellulase (0.0132 IU) and xylanase (0.0774 IU) activities, are obtained with banana stem as the carbon source. On sugarcane bagasse, total cellulase activity on filter paper and pectinase activities are predominant. The exocellulase/endocellulase activity ratio (FPAsol/FPAinsol) of the cellulases produced varies between 1 and 4 depending on the substrate. The highest endocellulase activity (FPAinsol) content is obtained when grown on sugarcane bagasse
degradation
hydrolysis of 2% carboxymethyl cellulose with purified enzyme at its optimum temperature and pH results in complete hydrolysis within 2 h yielding 18% cellotriose, 72% cellobiose and 10% glucose
degradation
-
immobilization of enzyme on functionalized magnetic silica nanospheres using glutaraldehyde. Immobilized cellulase exhibits better resistance to high temperature and pH inactivation in comparison to free cellulase. Use of cross-linking agent leads to a greater amount of immobilized cellulase and better operational stability. The amount of immobilized cellulase with the cross-linking agent is 92 mg/g support. The activity of the immobilized cellulase is still 85.5% of the initial activity after 10 continuous uses
degradation
mixtures of beta-xylosidase, xylanase, beta-glucosidase, and cellulase isolated from the metagenomic library of a long-term dry thermophilic methanogenic digester community retain high residual synergistic activities after incubation with cellulose, xylan, and steam-exploded corncob at 50°C for 72 h. About 55% dry weight of steam-exploded corncob is hydrolyzed to glucose and xylose by the synergistic action of the four enzymes at 50°C for 48 h
degradation
-
preparation of functionalized magnetic nanospheres by co-condensation of tetraethylorthosilicate with aminosilanes 3-(2-aminoethylaminopropyl)-triethoxysilane (AEAPTES), 3-(2-aminoethy-laminopropyl)-trimethoxysilane (AEAPTMES) and 3-aminopropyltriethoxysilane (APTES) and use as supports for immobilization of cellulase. The magnetic nanospheres with core-shell morphologies exhibit higher capacity for cellulase immobilization than unfunctionalized magnetic nanospheres. AEAPTMES with methoxy groups is favored to be hydrolyzed and grafted on unfunctionalized magnetic nanospheres. AEAPTMES functionalized magnetic nanospheres with the highest zeta-potential (29 mV) exhibit 87% activity recovery, and the maximum amount of immobilized cellulase is112 mg/g support at concentration of initial cellulase of 8 mg/ml. Immobilized cellulase on AEAPTMES functionalized magnetic nanospheres has higher temperature stability and broader pH stability than other immobilized cellulases and free cellulase
degradation
-
pretreatment method for lignocellulosic wheat straw to depolymerize lignin and expose the cellulose polymers to produce bioethanol. Wheat straw is pretreated with ligninolytic enzymes extract produced from Ganoderma lucidum under optimum solid state fermentation conditions. The pretreated biomass was further subjected to the enzymatic hydrolysis by crude unprocessed cellulases (beta-1,4-endoglucanase, 53.5 U/ml, beta-1,4-exoglucanase, 41.3 U/ml, beta-1,4-glucosidase, 46.8 U/ml, and xylanase 39 U/ml) produced by Trichoderma harzaianum. Under optimal conditions for enzymatic saccharification, 10% (w/v) of pretreated biomass is hydrolyzed completely and converted to 72.5 and 2.4 g/l of glucose and xylose, respectively
degradation
-
saccharification of pretreated dry potato peels, carrot peels, composite waste mixture, orange peels, onion peels, banana peels, pineapple peels by crude enzyme extract from Aspergillus niger NS-2 results in cellulose conversion efficiencies of 9298%
degradation
the purified enzyme decreases the viscosity of carboxymethyl cellulose when assessed at 70-85°C and is capable of releasing reducing sugars from acid-pretreated straw at 70 and 75°C
degradation
-
Trichoderma reesei NRRL-6156 filter paper exocellulase and endocellulase hydrolysis of sugarcane bagasse, results in 224.0 and 229 gram of total reducing sugar per kilogram of dry bagasse at 43.4°C and a concentration of enzymatic extract of 18.6% in water and ultrasound baths, respectively. The yields obtained are comparable to commercial enzymes
degradation
under simulated mashing conditions, addition of 60 U Egl5A reduces more viscosity (10.0 vs.7.6%) than 80 U of Ultraflo XL from Novozymes
degradation
under simulated mashing conditions, addition of Cel7A (99 microg) reduces the mash viscosity by 9.1% and filtration time by 24.6%
degradation
-
use of amine-functionalized cobalt ferrite (AF-CoFe2O4) magnetic nanoparticles for immobilization of cellulase. Particles show a mean diameter of about 8 nm and remain distinct with no significant change in size after binding with cellulase. The immobilized cellulase has higher thermal stability than free cellulase and shows good reusability after recovery
degradation
use of mutant T57N/E53D/S79P/T80E/V101I/S133R/N155E/G189S/F191V/T233V/G239E/V265T/D271Y/G293A7S309W/S318P and previously engineered highly active, thermostable variants of the fungal cellobiohydrolases Cel6A and Cel7A to hydrolyzes cellulose synergistically at an optimum temperature of 70°C over 60 h.The thermostable mixture produces three times as much total sugar as the best mixture of the wild type enzymes operating at their optimum temperature of 60°C
degradation
-
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows showed high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities
degradation
-
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows showed high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities
degradation
-
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows showed high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities
degradation
addition of recombinant Eg5A to cellobiase (cellobiohydrolase and beta-glucosidase) results in a 53% increase in saccharification of NaOH-pretreated barley straw, whereas the glucose release is 47% higher than with cellobiase treatment alone
degradation
Thermochaetoides thermophila
-
cellulase enzyme filtrate from Chaetomium thermophile saccharifies 5% kallar grass straw to 69% reducing sugars (quantitatively) at 50°C. Glucose concentration in the hydrolysates from different fungi is in the decreasing order of Chaetomium thermophile > Trichoderma reesei > Sporotrichum thermophile > Aspergillus fumigatus > Torula thermophila > Humicola grisea > Malbranchea pulchella. At 60°C, thermostable enzymes hydrolyse kallar grass straw at a maximum rate for the initial 20 h
degradation
-
comparison of endoglucanases able to rapidly reduce the viscosity of 15% (w/w, dry matter) hydrothermally pretreated wheat straw. Based on temperature profiling studies, Thermoascus aurantiacus EGII/Cel5A is the most promising enzyme for biomass liquefaction
degradation
crude cellulase efficiently hydrolyzes office waste paper, algal pulp (Gracillaria verulosa), and biologically treated wheat straw at 60°C with sugar release of about 830 mg/ml, 285 mg/g, and 260 mg/g of the substrate, respectively
degradation
crude thermostable cellulases and xylanase hydrolyze phosphoric acid-swollen wheat straw, avicel and untreated xylan up to 74, 71 and 90 %, respectively
degradation
-
Freeze-dried enzyme of Trichoderma reesei, even at higher enzyme concentration results in 60% reducing sugars yield (quantitatively) at 50°C. Glucose concentration in the hydrolysates from different fungi is in the decreasing order of Chaetomium thermophile > Trichoderma reesei > Sporotrichum thermophile > Aspergillus fumigatus > Torula thermophila > Humicola grisea > Malbranchea pulchella. At 60°C, thermostable enzymes hydrolyse kallar grass straw at a maximum rate for the initial 20 h
degradation
-
hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase
degradation
oligosaccharides with degree of polymerization 2-10 are formed by hydrolysis of beta-glucan. The recombinant enzyme preparations are fast and effective in decreasing the reduced viscosity of wholegrain barley extract than some commercial enzyme preparations
degradation
-
scale-up systems for cellulase production and enzymatic hydrolysis of pretreated rice straw at highsolid loadings and by Aspergillus terreus. In a horizontal rotary drum reactor at 50°C with 25 % (w/v) solid loading and 9 FPU/g substrate enzyme load up to 20 % highly concentrated fermentable sugars are obtained at 40 h with an increased saccharification efficiency of 76 % compared to laboratory findings (69.2 %). Nearly 79-84% of the cellulases and more than 90% of the sugars are recovered from the saccharification mixture
degradation
-
use of lucerne fibre as a cellulase-recycling vehicle during bioconversion processes. Adsorption of cellulase complexes is minimal at the pH optimum, 5.0, for fibre conversion to soluble sugars. Lowering of incubation temperature to 3°C enhances adsorption of fungal cellulases. The adsorptive capacity can be improved about 30% by raising the pH above the hydrolysis optimum during the recycling phase
degradation
-
use of lucerne fibre as a cellulase-recycling vehicle during bioconversion processes. Adsorption of cellulase complexes is minimal at the pH optimum, 6.2, for fibre conversion to soluble sugars. Lowering of incubation temperature to 3°C enhances adsorption of fungal cellulases. The adsorptive capacity can be improved about 30% by raising the pH above the hydrolysis optimum during the recycling phase
degradation
use to release dye in neutral pH conditions from indigo-dyed cotton-containing fabric in biostoning applications
degradation
-
using enzymatic extract from M. thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively
degradation
MG570051
addition of Cel9K to a commercial enzyme set (Celluclast 1.5L + Novozym 188) increases the saccharification of the pretreated reed and rice straw powders by 30.4% and 15.9%, respectively
degradation
-
enzyme releases high amounts of reducing sugars from wheat bran and corn cobs, being a useful biocatalyst for producing bioethanol and fine chemicals from agroresidues
degradation
-
replacement of carbohydrate-binding module by modules from enzymes with different specificities leads to enhanced activity that is affected by carbohydrate-binding module binding specificity, e.g. on ball-milled cellulose or avicel. The chimeric enzymes can efficiently degrade milled lignocellulosic materials, such as corn hulls
degradation
under acidic conditions at 50°C, the enzyme is effective in digesting the green algae Ulva pertusa
degradation
Acetivibrio thermocellus DSM 1237
-
cellulase complex containing cellulolytic enzymes,endoglucanase CelE, EC 3.2.1.4, and beta-glucosidase BglA, EC 3.2.1.21, to completely degrade cellulose to glucose. The cellulases are displayed on the cell surface of Corynebacterium glutamicum by using themechanosensitive channel to anchor enzymes in the cytoplasmic membrane. The displayed cellulases complexes have a synergic effect on the direct conversion of biomass to reducing sugars leading to 3.1- to 6.0fold increase compared to the conversion by the secreted cellulases complexes. The displayed cellulases complexes increase the residual activities of cCelEand cBglA at 70°C from 28.3% and 24.3% in the secreted form to 65.1% and 82.8%, respectively
-
degradation
-
under simulated mashing conditions, addition of Cel7A (99 microg) reduces the mash viscosity by 9.1% and filtration time by 24.6%
-
degradation
-
hydrolysis of 2% carboxymethyl cellulose with purified enzyme at its optimum temperature and pH results in complete hydrolysis within 2 h yielding 18% cellotriose, 72% cellobiose and 10% glucose
-
degradation
-
Trichoderma reesei NRRL-6156 filter paper exocellulase and endocellulase hydrolysis of sugarcane bagasse, results in 224.0 and 229 gram of total reducing sugar per kilogram of dry bagasse at 43.4°C and a concentration of enzymatic extract of 18.6% in water and ultrasound baths, respectively. The yields obtained are comparable to commercial enzymes
-
degradation
-
replacement of carbohydrate-binding module by modules from enzymes with different specificities leads to enhanced activity that is affected by carbohydrate-binding module binding specificity, e.g. on ball-milled cellulose or avicel. The chimeric enzymes can efficiently degrade milled lignocellulosic materials, such as corn hulls
-
degradation
Thermothelomyces thermophilus JCP 1-4
-
using enzymatic extract from M. thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively
-
degradation
-
effect of nickel-cobaltite (NiCo2O4) nanoparticles on production and thermostability of the cellulase enzyme system. Maximum production of endoglucanase (211 IU/gds), beta-glucosidase (301 IU/gds), and xylanase (803 IU/gds) is achieved after 72 h without nanoparticles, while in the presence of 1 mM of nanoparticles, endoglucanase, beta-glucosidase, and xylanase activity increase by about 49, 53, and 19.8%, respectively, after 48 h of incubation. Crude enzyme is thermally stable for 7 h at 80°C in presence of nanoparticles, as against 4 h at the same temperature for control samples
-
degradation
-
use to release dye in neutral pH conditions from indigo-dyed cotton-containing fabric in biostoning applications
-
degradation
-
saccharification of pretreated dry potato peels, carrot peels, composite waste mixture, orange peels, onion peels, banana peels, pineapple peels by crude enzyme extract from Aspergillus niger NS-2 results in cellulose conversion efficiencies of 9298%
-
degradation
-
under simulated mashing conditions, addition of 60 U Egl5A reduces more viscosity (10.0 vs.7.6%) than 80 U of Ultraflo XL from Novozymes
-
degradation
-
Freeze-dried enzyme of Trichoderma reesei, even at higher enzyme concentration results in 60% reducing sugars yield (quantitatively) at 50°C. Glucose concentration in the hydrolysates from different fungi is in the decreasing order of Chaetomium thermophile > Trichoderma reesei > Sporotrichum thermophile > Aspergillus fumigatus > Torula thermophila > Humicola grisea > Malbranchea pulchella. At 60°C, thermostable enzymes hydrolyse kallar grass straw at a maximum rate for the initial 20 h
-
degradation
-
hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase
-
degradation
-
enzyme releases high amounts of reducing sugars from wheat bran and corn cobs, being a useful biocatalyst for producing bioethanol and fine chemicals from agroresidues
-
degradation
-
use of mutant T57N/E53D/S79P/T80E/V101I/S133R/N155E/G189S/F191V/T233V/G239E/V265T/D271Y/G293A7S309W/S318P and previously engineered highly active, thermostable variants of the fungal cellobiohydrolases Cel6A and Cel7A to hydrolyzes cellulose synergistically at an optimum temperature of 70°C over 60 h.The thermostable mixture produces three times as much total sugar as the best mixture of the wild type enzymes operating at their optimum temperature of 60°C
-
degradation
-
crude cellulase efficiently hydrolyzes office waste paper, algal pulp (Gracillaria verulosa), and biologically treated wheat straw at 60°C with sugar release of about 830 mg/ml, 285 mg/g, and 260 mg/g of the substrate, respectively
-
degradation
-
crude thermostable cellulases and xylanase hydrolyze phosphoric acid-swollen wheat straw, avicel and untreated xylan up to 74, 71 and 90 %, respectively
-
degradation
-
effects of microalgal biomass particle on the degree of enzymatic hydrolysis and bioethanol production by single enzyme hydrolysis (cellulase) and double enzyme hydrolysis (cellulase and cellobiase). The glucose yield from biomass in the smallest particle size range examined, i.e. 35 microm to 90 microm, is the highest, 134.73 mg glucose/g algae, while the yield from biomass in the larger particle size range from 295 microm to 425 microm is 75.45mg glucose/g algae. A similar trend is observed for bioethanol yield, with the highest yield of 0.47 g EtOH/g glucose obtained from biomass in the smallest particle size range
-
degradation
-
after hydrolysis and fermentation of wheat straw a significant amount of active enzymes can be recovered by recycling the liquid phase. In the early stage of the process, enzyme adsorbs to the substrate, then gradually returning to the solution as the saccharification proceeds. The hydrolysis yield and enzyme recycling efficiency in consecutive recycling rounds can be increased by using high enzyme loadings and moderate temperatures. The amount of enzymes in the liquid phase increases with its thermostability and hydrolytic efficiency
-
degradation
-
use of amine-functionalized cobalt ferrite (AF-CoFe2O4) magnetic nanoparticles for immobilization of cellulase. Particles show a mean diameter of about 8 nm and remain distinct with no significant change in size after binding with cellulase. The immobilized cellulase has higher thermal stability than free cellulase and shows good reusability after recovery
-
degradation
-
bioethanol production by Aspergillus fumigatus JCF at optimised growth conditions and Saccharomyces cerevisiae for simultaneous saccharification and fermentation. Using cotton seed as the substrate, maximum bioethanol concentration of 6.7 g/l can be achieved
-
detergent
-
thermostability, pH-stability, good hydrolytic capability, and stability in the presence of detergents, surfactants, chelators and commercial proteases make this enzyme potentially useful in laundry detergents
detergent
-
strong resistance to anionic surfactants and oxidizing agents, might be a usefull enzyme in detergent industry
detergent
-
thermostability, pH-stability, good hydrolytic capability, and stability in the presence of detergents, surfactants, chelators and commercial proteases make this enzyme potentially useful in laundry detergents
-
environmental protection
-
cellulase producing haloarchael cells may be potentially utilized for the treatment of hypersaline waste water to remove cellulose
environmental protection
-
cellulase producing haloarchael cells may be potentially utilized for the treatment of hypersaline waste water to remove cellulose
-
food industry
-
extraction of pectins from apple pomace with monoactive preparation of endoxylanase and endcellulase. Pectin extracted with endocellulase has 1.5fold lower molecular mass but contains significantly more galacturonic acid (70.5%) of a high degree of methylation (66.3%). The simultaneous application of both enzymaticpreparations results in their cooperation, leading to a decrease of both the extraction efficiency and the molecular mass of pectin. This pectin displays the highest galacturonic acid (74.7%) and rhamnose contents
food industry
-
the capacity of Cel8A to cleave 1,3-1,4-beta-glucans is significantly affected by the presence of the barley-based feed for broilers. Exogenous 1,3-1,4-beta-glucanases (EC 3.2.1.73) but not 1,4-beta-glucanases 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
industry
-
the purified enzyme performs well in biostoning of denim fabric at neutral pH
industry
due to its acidophilic (pH 3.5) and high temperature stability (up to 90°C), CSCMCase may be useful for industrial application such as animal feed industry and clarification of fruit juices
industry
-
enzyme possesses high power of defibrillation of textile and laundry. Polypeptide can be exploited for mass production and application in local industries
industry
potent enzyme for industrial bioprocesses, including the bio-polishing of cotton products, food processing and bioethanol production
industry
because of its ability to hydrolyze celluloses at high temperatures above 90°C, as well as its thermostability, the enzyme is expected to be an excellent tool for industrial hydrolysis of cellulose, particularly for biopolishing of cotton products
industry
textile and detergent industry, combination of CBH6A and EgGH45
industry
-
economical analysis of cellulase production by solid-state fermentation in a pilot plant integrated to both a first and a second generation ethanol processes. Growth of Myceliophthora thermophila I-1D3b at 45°C during 96 h on sugarcane bagasse and wheat bran. shows that the process is economically attractive, due to its easy integration to the main process, and its revenue is up to four fold greater than electricity cogeneration
industry
-
endoglucanases from family GH45 are applied in formulation of detergents and in industrial pulp and paper processes
industry
-
endoglucanases from family GH45 are applied in formulation of detergents and in industrial pulp and paper processes
industry
-
enzyme Bc22Cel is a potential and useful candidate for industrial applications, such as the bioconversion of sugarcane bagasse to its derivatives
industry
Thermochaetoides thermophila
the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively
industry
the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus has great potential in generating fermentable sugars from renewable agro-residues for biofuel and fine chemical industry. Application of the fusion enzyme (EG-M-Xyn)in combination with Ctec2 (commercial enzyme) in the saccharification leads to a 10-20% net increase in fermentable sugars liberated from pretreated rice straw in comparison to the Ctec2 alone
industry
the thermophilic nature and biochemical properties of the enzyme indicate its potential suitability in industrial applications undertaken at high temperature, such as the production of second-generation bioethanol from lignocellulosic feedstocks and in the brewing industry
industry
Thermochaetoides thermophila IMI 039719
-
the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively
-
industry
Thermochaetoides thermophila DSM 1495
-
the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively
-
industry
-
because of its ability to hydrolyze celluloses at high temperatures above 90°C, as well as its thermostability, the enzyme is expected to be an excellent tool for industrial hydrolysis of cellulose, particularly for biopolishing of cotton products
-
industry
-
the thermophilic nature and biochemical properties of the enzyme indicate its potential suitability in industrial applications undertaken at high temperature, such as the production of second-generation bioethanol from lignocellulosic feedstocks and in the brewing industry
-
industry
-
the thermophilic nature and biochemical properties of the enzyme indicate its potential suitability in industrial applications undertaken at high temperature, such as the production of second-generation bioethanol from lignocellulosic feedstocks and in the brewing industry
-
industry
Bacillus sp. (in: Bacteria) CTP-09
-
enzyme possesses high power of defibrillation of textile and laundry. Polypeptide can be exploited for mass production and application in local industries
-
industry
-
the purified enzyme performs well in biostoning of denim fabric at neutral pH
-
industry
Thermochaetoides thermophila CBS 144.50
-
the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively
-
industry
-
economical analysis of cellulase production by solid-state fermentation in a pilot plant integrated to both a first and a second generation ethanol processes. Growth of Myceliophthora thermophila I-1D3b at 45°C during 96 h on sugarcane bagasse and wheat bran. shows that the process is economically attractive, due to its easy integration to the main process, and its revenue is up to four fold greater than electricity cogeneration
-
synthesis
-
synthesis of glyceroyl beta-N-acetyllactosaminide and derivatives, that could be used as starting material for the synthesis of neoglycolipid and new kinds of detergents and as acceptors for glycosidase and glycosyltransferase
synthesis
when the enzyme is used in combination withbeta-glucosidase, cellulose is completely hydrolyzed to glucose at high temperature, suggesting great potential for EGPh in bioethanol industrial applications
synthesis
glucose production from cellulose material using beta-glucosidase from Pyrococcus furioses and endocellulase from Pyrococcus horikoshii. The combination reaction can produce only glucose without the other oligosaccharides from phosphoric acid swollen Avicel
synthesis
-
production of enzyme in parallel-operated shake flasks and, alternatively, in parallel-operated stirred-tank bioreactors on a 10-m. scale. Reaction conditions with 53.3 g/l microcrystalline cellulose in the initial medium, no lactose feeding and 3.3 g/l and day intermittent ammonium sulfate addition are optimal. The optimum substrate supply on a liter-scale results in the production of 4.88 filter paper units of enzyme per ml with after 96 h
synthesis
-
use of a cellulase blend to evaluate its application in a simultaneous saccharification and fermentation process for second generation ethanol production from sugar cane bagasse. After enzyme production in a bioreactor and tangential ultrafiltration in hollow fiber membranes, the cellulolytic preparation is stable for at least 300 h at both 37°C and 50°C. The ethanol production is carried out by sugar cane bagasse partially delignified cellulignin fed-batch simultaneous saccharification and fermantation process, using the onsite cellulase blend. The method applied results in 100 g/l ethanol concentration at the end of the process, which corresponds to a fermentation efficiency of 78% of the maximum obtainable theoretically. The experimental results lead to the ratio of 380 l of ethanolper ton of sugar cane bagasse partially delignified cellulignin
synthesis
-
40% higher cellulase activity on filter paper in 72 h is observed with the addition of 1 mM of nickel-cobaltite (NiCo2O4) nanoparticles in the growth medium. Maximum production of endoglucanase (211 IU/gds), beta-glucosidase (301 IU/gds), and xylanase (803 IU/gds) is achieved after 72 h without nanoparticles, while in the presence of 1 mM of nanoparticles, endoglucanase, beta-glucosidase, and xylanase activity increase by about 49, 53, and 19.8%, respectively, after 48 h of incubation
synthesis
-
a medium based on starch casein minerals containing carboxymethyl cellulose and beef extract supports enhanced cellulase production. Carboxymethyl cellulose, beef extract , NaCl, temperature and pH are significant for cellulase production. Optimization of cellulase production results in an enhancement of endoglucanase activity to 27 IU per ml
synthesis
expression of enzyme in Escherichia coli and Thermotoga sp. after fusion to the signal peptides of TM1840 (amyA) or TM0070 (xynB). Expressed in Escherichia coli and Thermotoga sp. renders the hosts with increased endo- and exoglucanase activities. In Escherichia coli, the recombinant enzymes are mainly bound to the bacterial cells, whereas in Thermotoga sp., about half of the enzyme activities are observed in the culture supernatants. However, the cellulase activities are lost in Thermotoga sp. after three consecutive transfers
synthesis
expression of enzyme in Escherichia coli and Thermotoga sp. after fusion to the signal peptides of TM1840 (amyA) or TM0070 (xynB). Expressed in Escherichia coli and Thermotoga sp. renders the hosts with increased endoglucanase activities. In Escherichia coli, the recombinant enzymes are mainly bound to the bacterial cells, whereas in Thermotoga sp., about half of the enzyme activities are observed in the culture supernatants. However, the cellulase activities are lost in Thermotoga sp. after three consecutive transfers
synthesis
heterologous expression in Bacillus subtilis combined with customized signal peptides for secretion from a random libraries with 173 different signal peptides originating from the Bacillus subtilis genome. The customized signal peptide does not affect enzyme performance when assayed on carboxymethyl cellulose, phosphoric acid swollen cellulose, and microcrystalline cellulose
synthesis
-
in regulator cre1-silenced strain C88, the filter paper hydrolyzing activity and beta-1,4-endoglucanase activity are 3.76-, and 1.31fold higher, respectively, than those in the parental strain when the strains are cultured in inducing medium for 6 days. The activities of beta-1,4-exoglucanase and cellobiase are 2.64-, and 5.59fold higher, respectively, than those in the parental strain when the strains are cultured for 5 days
synthesis
-
optimization of cultural conditions for enhanced cellulase production. Under solid-state fermentation, yields of carboxymethylcellulase are 463.9 U/g, filter paper cellulase 101.1 U/g and beta-glucosidase 99 U/g
synthesis
-
alkali-pretreated roots of Taraxacum kok-saghyz (rubber dandelion), incubated with crude enzyme extracts from Thermomyces lanuginosus STm yield more natural rubber (90 mg/g dry root) than the protocols, Eskew process (24 mg/g) and commercial-enzyme-combination process (45 mg/g). The crude enzyme treatment at 91.6% rubber purity approaches the purity of the commercial-enzyme-combination process at 94.1% purity
synthesis
-
scale-up systems for cellulase production and enzymatic hydrolysis of pretreated rice straw at highsolid loadings and by Aspergillus terreus. In a horizontal rotary drum reactor at 50°C with 25 % (w/v) solid loading and 9 FPU/g substrate enzyme load up to 20 % highly concentrated fermentable sugars are obtained at 40 h with an increased saccharification efficiency of 76 % compared to laboratory findings (69.2 %). Nearly 79-84% of the cellulases and more than 90% of the sugars are recovered from the saccharification mixture
synthesis
-
under optimised conditions of growth on wheat bran, 420.8 and 22.73 units/g substrate of endo-beta-1,4-glucanase and filter paper cellulase are produced, respectively. Both endo-beta-1,4-glucanase and filter paper activity production show significant dependence on ammonium sulfate concentration and pH
synthesis
-
enhanced production of enzyme in Escherichia coli. High-cell-density and optimal CenC expression are obtained in ZYBM9 medium induced either with 0.5 mM IPTG/150 mM lactose, after 6 h induction at 37°C. Before induction, bacterial cells are given heat shock (42°C) for 1 h when culture density (OD600 nm) reached at 0.6. Intracellular enzyme activity is enhanced by 6.67- and 3.20fold in ZYBM9 (yeast extract 0.5% (w/v), NaCl 0.5% (w/v), tryptone 1.0% (w/v), NH4Cl 0.1% (w/v), KH2PO4 0.3% (w/v), Na2HPO4 0.6% (w/v), MgSO4.7H2O 1 mM, and Glucose 0.4% (w/v)) and 3×ZYBM9 medium, respectively, under optimal conditions
synthesis
-
the cold active butanol-tolerant endoglucanase is valuable for biobutanol production by a simultaneous saccharification and fermentation process
synthesis
Acetivibrio thermocellus DSM 1237
-
heterologous expression in Bacillus subtilis combined with customized signal peptides for secretion from a random libraries with 173 different signal peptides originating from the Bacillus subtilis genome. The customized signal peptide does not affect enzyme performance when assayed on carboxymethyl cellulose, phosphoric acid swollen cellulose, and microcrystalline cellulose
-
synthesis
-
in regulator cre1-silenced strain C88, the filter paper hydrolyzing activity and beta-1,4-endoglucanase activity are 3.76-, and 1.31fold higher, respectively, than those in the parental strain when the strains are cultured in inducing medium for 6 days. The activities of beta-1,4-exoglucanase and cellobiase are 2.64-, and 5.59fold higher, respectively, than those in the parental strain when the strains are cultured for 5 days
-
synthesis
-
when the enzyme is used in combination withbeta-glucosidase, cellulose is completely hydrolyzed to glucose at high temperature, suggesting great potential for EGPh in bioethanol industrial applications
-
synthesis
-
glucose production from cellulose material using beta-glucosidase from Pyrococcus furioses and endocellulase from Pyrococcus horikoshii. The combination reaction can produce only glucose without the other oligosaccharides from phosphoric acid swollen Avicel
-
synthesis
-
alkali-pretreated roots of Taraxacum kok-saghyz (rubber dandelion), incubated with crude enzyme extracts from Thermomyces lanuginosus STm yield more natural rubber (90 mg/g dry root) than the protocols, Eskew process (24 mg/g) and commercial-enzyme-combination process (45 mg/g). The crude enzyme treatment at 91.6% rubber purity approaches the purity of the commercial-enzyme-combination process at 94.1% purity
-
synthesis
-
under optimised conditions of growth on wheat bran, 420.8 and 22.73 units/g substrate of endo-beta-1,4-glucanase and filter paper cellulase are produced, respectively. Both endo-beta-1,4-glucanase and filter paper activity production show significant dependence on ammonium sulfate concentration and pH
-
synthesis
-
40% higher cellulase activity on filter paper in 72 h is observed with the addition of 1 mM of nickel-cobaltite (NiCo2O4) nanoparticles in the growth medium. Maximum production of endoglucanase (211 IU/gds), beta-glucosidase (301 IU/gds), and xylanase (803 IU/gds) is achieved after 72 h without nanoparticles, while in the presence of 1 mM of nanoparticles, endoglucanase, beta-glucosidase, and xylanase activity increase by about 49, 53, and 19.8%, respectively, after 48 h of incubation
-
synthesis
-
optimization of cultural conditions for enhanced cellulase production. Under solid-state fermentation, yields of carboxymethylcellulase are 463.9 U/g, filter paper cellulase 101.1 U/g and beta-glucosidase 99 U/g
-
synthesis
-
enhanced production of enzyme in Escherichia coli. High-cell-density and optimal CenC expression are obtained in ZYBM9 medium induced either with 0.5 mM IPTG/150 mM lactose, after 6 h induction at 37°C. Before induction, bacterial cells are given heat shock (42°C) for 1 h when culture density (OD600 nm) reached at 0.6. Intracellular enzyme activity is enhanced by 6.67- and 3.20fold in ZYBM9 (yeast extract 0.5% (w/v), NaCl 0.5% (w/v), tryptone 1.0% (w/v), NH4Cl 0.1% (w/v), KH2PO4 0.3% (w/v), Na2HPO4 0.6% (w/v), MgSO4.7H2O 1 mM, and Glucose 0.4% (w/v)) and 3×ZYBM9 medium, respectively, under optimal conditions
-
synthesis
-
use of a cellulase blend to evaluate its application in a simultaneous saccharification and fermentation process for second generation ethanol production from sugar cane bagasse. After enzyme production in a bioreactor and tangential ultrafiltration in hollow fiber membranes, the cellulolytic preparation is stable for at least 300 h at both 37°C and 50°C. The ethanol production is carried out by sugar cane bagasse partially delignified cellulignin fed-batch simultaneous saccharification and fermantation process, using the onsite cellulase blend. The method applied results in 100 g/l ethanol concentration at the end of the process, which corresponds to a fermentation efficiency of 78% of the maximum obtainable theoretically. The experimental results lead to the ratio of 380 l of ethanolper ton of sugar cane bagasse partially delignified cellulignin
-
synthesis
-
a medium based on starch casein minerals containing carboxymethyl cellulose and beef extract supports enhanced cellulase production. Carboxymethyl cellulose, beef extract , NaCl, temperature and pH are significant for cellulase production. Optimization of cellulase production results in an enhancement of endoglucanase activity to 27 IU per ml
-
synthesis
-
production of enzyme in parallel-operated shake flasks and, alternatively, in parallel-operated stirred-tank bioreactors on a 10-m. scale. Reaction conditions with 53.3 g/l microcrystalline cellulose in the initial medium, no lactose feeding and 3.3 g/l and day intermittent ammonium sulfate addition are optimal. The optimum substrate supply on a liter-scale results in the production of 4.88 filter paper units of enzyme per ml with after 96 h
-
