3.2.1.91: cellulose 1,4-beta-cellobiosidase (non-reducing end)
This is an abbreviated version!
For detailed information about cellulose 1,4-beta-cellobiosidase (non-reducing end), go to the full flat file.
Word Map on EC 3.2.1.91
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3.2.1.91
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trichoderma
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reesei
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chitinase
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cellulases
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glucans
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xylanase
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cellobiohydrolases
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cellulolytic
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biocontrol
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pathogenesis-related
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laminarin
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cellulose-binding
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lignocellulosic
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saccharification
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chrysosporium
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cellulosic
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microcrystalline
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pectinase
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beta-1,3-glucans
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cbhii
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beta-glucans
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mannanase
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cellulomonas
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cellotriose
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phanerochaete
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hypocrea
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succinogenes
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humicola
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harzianum
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cellotetraose
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galactanase
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thermocellum
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lichenan
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mycoparasite
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fibrobacter
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thaumatin-like
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cellulosomal
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stover
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insolens
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biotechnology
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synthesis
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textile production
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paper production
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industry
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detergent
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degradation
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analysis
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biofuel production
- 3.2.1.91
- trichoderma
- reesei
- chitinase
- cellulases
- glucans
- xylanase
- cellobiohydrolases
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cellulolytic
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biocontrol
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pathogenesis-related
- laminarin
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cellulose-binding
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lignocellulosic
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saccharification
- chrysosporium
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cellulosic
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microcrystalline
- pectinase
- beta-1,3-glucans
- cbhii
- beta-glucans
- mannanase
- cellulomonas
- cellotriose
- phanerochaete
- hypocrea
- succinogenes
- humicola
- harzianum
- cellotetraose
- galactanase
- thermocellum
- lichenan
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mycoparasite
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fibrobacter
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thaumatin-like
- cellulosomal
- stover
- insolens
- biotechnology
- synthesis
- textile production
- paper production
- industry
- detergent
- degradation
- analysis
- biofuel production
Reaction
2 cellohexaose
+
2 H2O
=
2 cellotriose
+
Synonyms
1,4-beta-cellobiohydrolase, 1,4-beta-D-glucan cellobiohydrolase, 1,4-beta-glucan cellobiohydrolase, 1,4-beta-glucan cellobiosidase, avicelase, avicelase II, beta-1,4-glucan cellobiohydrolase, beta-1,4-glucan cellobiosylhydrolase, beta-1,4-glycanase, Beta-1,4-glycanase CEX, Beta-glucancellobiohydrolase, C1 cellulase, CBH, CBH 1, Cbh C, CBH I, CBH Ib, CBH II, CBH IIb, CBH1, CBH2, Cbh6B, Cbh9A, CbhA, CBHI, CBHII, Cbhl.2, CBM3-GH5, CBP120, CBP95, CbsA, Cel5A, Cel6, Cel6A, Cel6B, Cel6C, Cel7A, Cel7D, CelA, CelAB, CelB, CelC7, CelK, cellobiohydrolase, cellobiohydrolase 1, cellobiohydrolase 9A, cellobiohydrolase A, cellobiohydrolase class II, cellobiohydrolase I, cellobiohydrolase II, cellobiohydrolase, exo-, cellobiosidase, cellobiosidase, 1,4-beta-glucan, Celluclast 1.5, Cellulase, cellulase, C1, Cex, Csac_1078, Ex-1, Ex-4, exo-1,4-beta-D-glucan cellobiohydrolase, exo-1,4-beta-D-glucanase, exo-beta-1,4-cellobiohydrolase, exo-beta-1,4-glucan cellobiohydrolase, exo-cellobiohydrolase, exocellobiohydrolase, exocellulase, exocellulase E3, exoglucanase, GH5, glucanase, Huta_2387, More, nonreducing end-acting cellobiohydrolase, oligosaccharide-specific cellobiohydrolase, PSCase, SCO6546, Ta Cel7A, THITE_126432, TTCBH6B
ECTree
3.2.1.91 cellulose 1,4-beta-cellobiosidase (non-reducing end)Advanced search results
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Application on EC 3.2.1.91 - cellulose 1,4-beta-cellobiosidase (non-reducing end)
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
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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
biofuel production
cellulose hydrolysis is an important step in the production of bioethanol from cellulosic biomass. Two key cellulase enzymes, celB from Caldicellulosiruptor saccharolyticus and beta-glucosidase, are covalently immobilised on polystyrene treated with plasma immersion ion implantation (PIII) which creates radicals that form covalent bonds. The immobilized enzymes are used to produce glucose from carboxymethyl cellulose (CMC), a solubilised form of cellulose. The highest activity of the immobilised celB on PIII treated surfaces was achieved when their immobilisation is carried out at a pH in the range 5-6.5. The immobilized celB on the PIII treated surface had the same activation energy as free celB showing substrate accessibility is not affected by the presence of the surface. The Vmax and Km values of immobilized celB are comparable to those of equal free celB concentrations. The areal density of immobilized celB on the PIII treated surface is estimated to be 0.0003 mg/cm2. The polystyrene surface with immobilized celB at 45°C can be reused over four times (23 hours each) with approximately 30% total activity loss. High ratios of beta-glucosidase to celB enhance the activity of immobilized celB for hydrolysis of carboxymethyl cellulose
biotechnology
fusion of the C-terminus of Caulobacter crescentus surface (S)-layer protein RsaA with the beta-1,4-glycanase Cex from the cellulolytic bacterium Cellulomonas fimi yielding a robust, catalytically active product, biocatalyst system evaluation
degradation
industry
synthesis
additional information
degradation
application of recombinant CBH II in hydrolysis of corn stover and rice straw pretreated with sodium hydroxide by improving the exo-exosynergism between CBH II and CBH I in Hypocrea jecorina. The yields 94.7% and 83.3% are achieved in the enzymatic hydrolysis of corn stover and rice straw pretreated by sodium hydroxide, respectively
degradation
construction of a consolidated bioprocessing-enabling yeast by constitutive expression of genes Cbh1 from Aspergillus aculeatus, Cbh1 and Cbh2 from Hypocrea jecorina. Additionally, Hypocrea jecorina Eg2, Aspergillus aculeatus Bgl1 are integrated into the Saccharomyces cerevisiae chromosome. The resultant strains expressing uni-, bi-, and trifunctional cellulases, respectively, exhibit corresponding cellulase activities and both the activities and glucose producing activity ascends. Evaluation in acid- and alkali-pretreated corncob containing media with 5 FPU exogenous cellulase/g biomass loading shows that compared with the control strains, the engineered strains efficiently ferment pretreated corncob to ethanol
degradation
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using enzymatic extract from Myceliophthora 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
combined use of isoforms CBH A and Cbh C on degradation of cotton. Conversion after 72 h is about 19 % by weight, with an almost fourfold increase in enzymatic hydrolysis yield by intermittent product removal of cellobiose with membrane filtration. A synergistic effect, achieving about 27 % substrate conversion, is obtained by addition of endo-1,4-beta-D-glucanase
degradation
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combined use of isoforms CBH A and Cbh C on degradation of cotton. Conversion after 72 h is about 19 % by weight, with an almost fourfold increase in enzymatic hydrolysis yield by intermittent product removal of cellobiose with membrane filtration. A synergistic effect, achieving about 27 % substrate conversion, is obtained by addition of endo-1,4-beta-D-glucanase
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degradation
Thermothelomyces thermophilus JCP 1-4
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using enzymatic extract from Myceliophthora 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
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industry
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development of efficient degradation of cellulosic biomass using cellulolytic enzymes, e.g. Ex-4, of white rot fungi
industry
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development of efficient degradation of cellulosic biomass using cellulolytic enzymes, e.g. Ex-4, of white rot fungi
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synthesis
expression in Pichia pastoris after codon optimization and using the strong methanol-inducible promoter AOX1. 5.84 U CBH II per ml can be obtained at 96 h
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
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 might influence substrate specificity by affecting the local structure of the CelK-specific N-terminal region containing an immunoglobulin-like domain
synthesis
SCHEMA structure-guided recombination of fungal class II cellobiohydrolases (CBH II cellulases) from Humicola insolens, Hypocrea jecorina and Chaetomium thermophiulum and mathematical modeling yields a collection of highly thermostable CBH II chimeras with more activity than Humicola insolens CBH II after incubation at 63 °C. The total of 15 validated thermostable CBH II enzymes have high sequence diversity, differing from their closest natural homologs at up to 63 amino acid positions. Selected purified thermostable chimeras hydrolyze phosphoric acid swollen cellulose at temperatures 7 to 15°C higher than the parent enzymes. These chimeras also hydrolyze as much or more cellulose than the parent CBH II enzymes in long-time cellulose hydrolysis assays and have pH/activity profiles as broad, or broader than, the parent enzymes. The best chimera with buildung blocks from all three organisms exhibits both relatively high specific activity and high thermostability
synthesis
SCHEMA structure-guided recombination of fungal class II cellobiohydrolases (CBH II cellulases) from Humicola insolens, Hypocrea jecorina and Chaetomium thermophiulum and mathematical modeling yields a collection of highly thermostable CBH II chimeras. The total of 15 validated thermostable CBH II enzymes have high sequence diversity, differing from their closest natural homologs at up to 63 amino acid positions. Selected purified thermostable chimeras hydrolyze phosphoric acid swollen cellulose at temperatures 7 to 15°C higher than the parent enzymes. These chimeras also hydrolyze as much or more cellulose than the parent CBH II enzymes in long-time cellulose hydrolysis assays and have pH/activity profiles as broad, or broader than, the parent enzymes. The best chimera with buildung blocks from all three organisms exhibits both relatively high specific activity and high thermostability
synthesis
Thermochaetoides thermophila
SCHEMA structure-guided recombination of fungal class II cellobiohydrolases (CBH II cellulases) from Humicola insolens, Hypocrea jecorina and Chaetomium thermophiulum and mathematical modeling yields a collection of highly thermostable CBH II chimeras. The total of 15 validated thermostable CBH II enzymes have high sequence diversity, differing from their closest natural homologs at up to 63 amino acid positions. Selected purified thermostable chimeras hydrolyze phosphoric acid swollen cellulose at temperatures 7 to 15°C higher than the parent enzymes. These chimeras also hydrolyze as much or more cellulose than the parent CBH II enzymes in long-time cellulose hydrolysis assays and have pH/activity profiles as broad, or broader than, the parent enzymes. The best chimera with buildung blocks from all three organisms exhibits both relatively high specific activity and high thermostability
synthesis
Acetivibrio thermocellus DSM 1237
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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 might influence substrate specificity by affecting the local structure of the CelK-specific N-terminal region containing an immunoglobulin-like domain
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additional information
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ability to amplify a key fungal cellobiohydrolase I gene involved in plant litter decomposition has the potential to unlock the identity and dynamics of the cellulolytic fungal community in situ
additional information
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ability to amplify a key fungal cellobiohydrolase I gene involved in plant litter decomposition has the potential to unlock the identity and dynamics of the cellulolytic fungal community in situ
additional information
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ability to amplify a key fungal cellobiohydrolase I gene involved in plant litter decomposition has the potential to unlock the identity and dynamics of the cellulolytic fungal community in situ
additional information
-
ability to amplify a key fungal cellobiohydrolase I gene involved in plant litter decomposition has the potential to unlock the identity and dynamics of the cellulolytic fungal community in situ
additional information
-
ability to amplify a key fungal cellobiohydrolase I gene involved in plant litter decomposition has the potential to unlock the identity and dynamics of the cellulolytic fungal community in situ
