3.2.1.176: cellulose 1,4-beta-cellobiosidase (reducing end)
This is an abbreviated version!
For detailed information about cellulose 1,4-beta-cellobiosidase (reducing end), go to the full flat file.
Word Map on EC 3.2.1.176
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3.2.1.176
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crew
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subsystem
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mission
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hydroponic
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cellulosome
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thermocellum
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bioregenerative
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life-support
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cellulases
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lunar
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long-duration
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inedible
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degradation
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breadboard
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avicel
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dockerin
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moon
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synthesis
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biotechnology
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biofuel production
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analysis
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paper production
- 3.2.1.176
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crew
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subsystem
-
mission
-
hydroponic
- cellulosome
- thermocellum
-
bioregenerative
-
life-support
- cellulases
-
lunar
-
long-duration
-
inedible
- degradation
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breadboard
- avicel
-
dockerin
-
moon
- synthesis
- biotechnology
- biofuel production
- analysis
- paper production
Reaction
2 cellohexaose
+
2 H2O
=
2 cellotriose
+
Synonyms
1,4-beta-D-glucan cellobiohydrolase I, 1,4-beta-D-glucan-cellobiohydrolase I, CBH, CBH I, CBH Ib, CBH-1, CBH1, CBH2, Cbh3, Cbh7B, CbhA, CBHI, CbhI.1, Cel48A, Cel48C, Cel48S, Cel48S cellulase, Cel48Y cellulase, Cel6A, Cel7A, Cel7B, Cel7D, Cel9B, cellobiohydrolase, cellobiohydrolase 1, cellobiohydrolase A, cellobiohydrolase CelS, cellobiohydrolase class I, cellobiohydrolase I, cellobiohydrolase I-I, cellobiohydrolase I-II, cellobiohydrolase II, cellobiohydrolase II-I, Celluclast, Cellulase SS, CelO, celS, CelSS, CelY, Ct-Cel5F, DDB0202233, DICPUDRAFT_151874, EG I, EgxS, endoglucanase, endoglucanase SS, exo-1,4-beta-glucanase, exo-acting cellulase, exo-beta-1,4-glucanase, exocellulase, exocellulase E4, exocellulase E6, exoglucanase, exoglucanase S, exoglucanase-1, GH7 CBH, More, reducing end acting processive exocellulase, reducing end-acting CBH, Tfu_1959, ThCel7A, THITE_62596, Tr-Cel7A
ECTree
3.2.1.176 cellulose 1,4-beta-cellobiosidase (reducing end)Advanced search results
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results (Application
Application on EC 3.2.1.176 - cellulose 1,4-beta-cellobiosidase (reducing end)
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
biofuel production
biotechnology
degradation
paper production
synthesis
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
analysis
development of an optical tweezers-based single-molecule motility assay for precision tracking of Cel7A. Direct observation of motility during degradation reveals processive runs and distinct steps on the scale of 1 nm. Cel7A is not mechanically limited, can work against 20 pN loads and speeds up when assisted. The fundamental stepping cycle likely includes energy from glycosidic bonds and other sources. The catalytic domain alone is sufficient for processive motion
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
analysis
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development of an optical tweezers-based single-molecule motility assay for precision tracking of Cel7A. Direct observation of motility during degradation reveals processive runs and distinct steps on the scale of 1 nm. Cel7A is not mechanically limited, can work against 20 pN loads and speeds up when assisted. The fundamental stepping cycle likely includes energy from glycosidic bonds and other sources. The catalytic domain alone is sufficient for processive motion
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biofuel production
successful expression of a chimeric cellobiohydrolase I with essentially full native activity in Yarrowia lipolytica. Yarrowia lipolytica strains can be genetically engineered, ultimately by heterologous expression of fungal cellulases and other enzymes, to directly convert lignocellulosic substrates to biofuels
biofuel production
successful expression of a chimeric cellobiohydrolase I with essentially full native activity in Yarrowia lipolytica. Yarrowia lipolytica strains can be genetically engineered, ultimately by heterologous expression of fungal cellulases and other enzymes, to directly convert lignocellulosic substrates to biofuels
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
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. Two of the most stabilizing blocks are predicted to be from the parent CelS at blocks located in the C-terminus of the catalytic domain, close to where the dockerin attaches. Two of the highly stable chimeras also hydrolyze more cellulose than the most active parental enzyme
biotechnology
Acetivibrio thermocellus DSM 1237
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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. Two of the most stabilizing blocks are predicted to be from the parent CelS at blocks located in the C-terminus of the catalytic domain, close to where the dockerin attaches. Two of the highly stable chimeras also hydrolyze more cellulose than the most active parental enzyme
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biotechnology
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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
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degradation
commercial cellulases contain mannan hydrolysing enzymes. Addition of 10 mg/ml mannan reduces the glucose yield of avicel (at 20 g/l) from 40.1 to 24.3%. The inhibitory effect is at least partly attributed to the inhibition of Cel7A(CBHI), but not on beta-glucosidase
degradation
comparison of the activity w ith Humicola jecorina Cel7A reveals a much higher hydrolytic rate for Humicola grisea Cel7A at both 65°C (4.8fold higher initial rate) and 38°C (3.3fold higher)
degradation
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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
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
development of optimal enzyme mixtures of six Trichoderma reesei enzymes and five thermostable enzyme for the hydrolysis of hydrothermally pretreated wheat straw, alkaline oxidised sugar cane bagasse and steam-exploded bagasse by statistically designed experiments. The composition of optimal enzyme mixtures depends clearly on the substrate and on the enzyme system studied. The optimal enzyme mixture of thermostable enzymes is dominated by Cel7A and requires a relatively high amount of xylanase, whereas with Hypocrea jecorina enzymes, the high proportion of Cel7B appears to provide the required xylanase activity
degradation
enzyme works synergistically with the commercial enzyme cocktail Cellic R CTec2 to enhance saccharification by 39% when added to a reaction mixture containing 0.25% alkaline pretreated oil palm empty fruit bunch
degradation
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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
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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
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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
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enzyme works synergistically with the commercial enzyme cocktail Cellic R CTec2 to enhance saccharification by 39% when added to a reaction mixture containing 0.25% alkaline pretreated oil palm empty fruit bunch
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paper production
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wild-type and recombinant endoglucanases Cel9B and Cel48C associated with endo- or exo-acting glucanases from Thermobifida fusca synergistically enhance the enzyme activity useful in pulpe and paper manufacturing, optimization, overview
paper production
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wild-type and recombinant endoglucanases Cel9B and Cel48C associated with endo- or exo-acting glucanases from Thermobifida fusca synergistically enhance the enzyme activity useful in pulpe and paper manufacturing, optimization, overview
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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
recombinant enzyme expressed in Zea mays is glycosylated and 6 kDa smaller than the native fungal protein. The cellobiohydrolase performs as well as or better than its fungal counterpart in releasing sugars from complex substrates such as pretreated corn stover or wood
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 does not affect enzyme performance when assayed on carboxymethyl cellulose, phosphoric acid swollen cellulose, and microcrystalline cellulose
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