species of Zygentoma that displayed the highest relative cellulase activity levels when compared to all other tested insect groups under the experimental conditions, including model species for cellulolytic systems such as termite and cockroach species in Rhinotermitidae (formerly Isoptera) and Cryptocercidae (formerly Blattodea). Among Zygentoma, Thermobia domestica was found to have higher endoglucanase, xylanase and pectinase activities compared to Ctenolepisma longicaudata. Among the identified enzymes are putative endoglucanases matching to insect or arthropod enzymes and glucan endo-1,6-beta-glucosidases matching bacterial enzymes. These findings support combined activities of endogenous and symbiont-derived plant cell wall degrading enzymes in lignocellulose digestion in Zygentoma, a primitive insect group
species of Zygentoma that displayed the highest relative cellulase activity levels when compared to all other tested insect groups under the experimental conditions, including model species for cellulolytic systems such as termite and cockroach species in Rhinotermitidae (formerly Isoptera) and Cryptocercidae (formerly Blattodea). Among Zygentoma, Thermobia domestica was found to have higher endoglucanase, xylanase and pectinase activities compared to Ctenolepisma longicaudata. Among the identified enzymes are putative endoglucanases matching to insect or arthropod enzymes and glucan endo-1,6-beta-glucosidases matching bacterial enzymes. These findings support combined activities of endogenous and symbiont-derived plant cell wall degrading enzymes in lignocellulose digestion in Zygentoma, a primitive insect group
the enzyme belongs to the glycoside hydrolase family 5, GH5. The GH5 family shares a canonical (betaalpha)8-barrel structure, where each (betaalpha) module is essential for the enzyme's stability and activity. Despite their shared topology, the thermostability of GH5 endoglucanase enzymes can vary significantly, and highly thermostable variants are often sought for industrial applications
the enzyme belongs to the glycoside hydrolase family 5, GH5. The GH5 family shares a canonical (betaalpha)8-barrel structure, where each (betaalpha) module is essential for the enzyme's stability and activity. Despite their shared topology, the thermostability of GH5 endoglucanase enzymes can vary significantly, and highly thermostable variants are often sought for industrial applications
the enzyme belongs to the glycoside hydrolase family 5, GH5. The GH5 family shares a canonical (betaalpha)8-barrel structure, where each (betaalpha) module is essential for the enzyme's stability and activity. Despite their shared topology, the thermostability of GH5 endoglucanase enzymes can vary significantly, and highly thermostable variants are often sought for industrial applications
the enzyme belongs to the glycoside hydrolase family 5, GH5. The GH5 signature pattern PS00659 (174 IGADIKNEPH 185) is identified within the sequence of Vul_Cel5A
cellulolytic enzymes, including endo-beta-1,4-glucanases, EC 3.2.1.4, exo-beta-1,4-glucanases, EC 3.2.1.91, and beta-glucosidases, EC 3.2.1.21, collectively known as cellulases, act in a synergistic manner to facilitate complete cleavage of the cellulose beta-1,4-glycosidic bonds to form glucose
the complete solubilization of crystalline cellulose requires the concerted and synergistic action of three classes of glycoside hydrolases, cellulase, endoglucanase, EC 3.2.1.4, cellobiohydrolase, EC 3.2.1.74, and beta-glucosidase, EC 3.2.1.21
the mechanism for enzymatic hydrolysis of cellulose involves synergistic actions by endoglucanase, EC 3.2.1.4, exoglucanase or cellobiohydrolase, EC 3.2.1.91, and beta-glucosidase, EC 3.2.1.21
three kinds of cellulases are required to carry out cellulose hydrolysis: endoglucanases, EC 3.2.1.4, exoglucanases or cellobiohydrolases, EC 3.2.1.91, and beta-glucosidases, EC 3.2.1.21
Trichoderma reesei produces a complete set of cellulase enzymes, comprising two cellobiohydrolases, i.e. 1,4-beta-D-glucan cellobiohydrolase, endoglucanases, i.e. 1,4- beta-D-glucan-4-glucanohydrolase, and beta-glucosidase, i.e. 1,4-beta-D-glucosidase, which act synergistically to degrade crystalline cellulose to glucose
key enzyme involved in the degradation of beta-glucan cellulose biomass acting through hydrolysis of the unbranched beta-1,4-linked glucose homopolymer
three kinds of cellulases are required to carry out cellulose hydrolysis: endoglucanases, EC 3.2.1.4, exoglucanases or cellobiohydrolases, EC 3.2.1.91, and beta-glucosidases, EC 3.2.1.21
cellulolytic enzymes, including endo-beta-1,4-glucanases, EC 3.2.1.4, exo-beta-1,4-glucanases, EC 3.2.1.91, and beta-glucosidases, EC 3.2.1.21, collectively known as cellulases, act in a synergistic manner to facilitate complete cleavage of the cellulose beta-1,4-glycosidic bonds to form glucose
model of synergistic cooperation between endocellulase Cel9A and exocellulase Cel48a. Endocellulase Cel9A is most effective on fresh bacterial cellulose with a presumably uniform surface at the molecular level. Its processive activity likely erodes the surface and thus reduces its own activity. Cel48A is able to hydrolyze the Cel9A-modified substrate efficiently and replenish the uniform surface required by Cel9A, creating a feedback mechanism
recombinant expression in tobacco leaf. Activity ranges from 92 to 488 nmol 4-methylumbelliferyl-beta-D-cellobioside/min/mg, the morphology and growth behavior of the transgenic plants are not different to those of wild-type plants
strain is able to grow in cellulosic agricultural waste as a sole carbon source and shows highest cellulase activity of 120 U/ml when grown on LB medium
ball-milled crude cellulosics, such as newsprint, de-inked newsprint, glossy writing paper, toilet paper and beech sawdust are substantially solubilised by extracellular cellulases within 110 h of growth. The type of crude cellulosic material greatly influences the pattern of enzyme production. Growth on carboxymethyl cellulose medium is accompanied by high endoglucanase (EC 3.2.1.4) activity. The cellulase complex e.g. exo-/3-1,4-glucanase (EC 3.2.1.-); endo-/3-1,4-glucanase (EC 3.2.1.4) and 8-glucosidase (EC 3.2.1.21) displays quite different properties depending on whether it is formed on low or highly substituted carboxymethyl cellulose
in solid state fermentation using lignocellulosic materials as substrates, Myceliophthora thermophila JCP 1-4 is the best producer of endoglucanase (357,51 U/g), beta-glucosidase (45.42 U/g), xylanase (93,11 U/g) and avicelase (3.58 U/g) among the strain tested
of the different carbon sources tested, rice straw induces maximal levels of cellulase. The addition of ethanol (1%, v/v) results in 8fold increased expression of endoglucanase. The expression profiles of different components of cellulase complex are coregulated in Mycothermus thermophilus
strain produces considerable amounts of extracellular hydrolytic enzymes on lignocellulosic substrates at 55°C incubated for 8 days in 150 ml shake flask experiments. The maximum enzyme activities on wheat straw and guayule bagasse are: xylanase 130.1 U/mg, inulinase 34.1 U/mg, carboxymethylcellulase 4.8 U/mg, filter paper assay (FPase) 5.5 FPU/g and pectinase 3.2 U/mg, respectively
deletion of isoform Cel9C causes a modest decrease in cellulose utilization. Cells of a mutant lacking both isoforms Cel5B and Cel9C are completely deficient in growth on cellulose
enzyme is is secreted into rice plants by Nilaparvata lugens. Silencing EG1 decreases the capacity of Nilaparvata lugens to reach the phloem and reduces its food intake, mass, survival, and fecundity on rice plants. EG1 silencing has only a small effect on the survival rate of Nilaparvata lugens raised on artificial diet. EG1 secreted by Nilaparvata lugens does not elicit the production of salicylic acid, jasmonic acid, and jasmonoyl-isoleucine in rice
endo-beta-glucanases (E.C. 3.2.1.4) are able to cleave the cellulosic structure in internal sites, generating a large number of ends where exo-beta-glucanases (E.C. 3.2.1.91 and EC 3.2.1.176) are able to act on degrading the reducing and non-reducing ends of cellulose to small glucose oligomers (cellobiose and cellodextrins), which in turn are hydrolyzed to single glucose units by enzymes denominated by beta-glycosidases (E.C. 3.2.1.21)
Paenibacillus sp. strain CAA11 secretes cellulolytic enzymes by its own secretion system and produces ethanol as well as short-chain organic acids (formic acid, acetic acid, lactic acid) from cellulose with rel. low activity
the GH6 endoglucanase mgCel6A is a thermostable cellulase with activity on an industrial cellulosic substrate (sulfite-pulped Norway spruce) and a glucomannanase side activity
recombinant expression in tobacco leaf. Activity ranges from 92 to 488 nmol 4-methylumbelliferyl-beta-D-cellobioside/min/mg, the morphology and growth behavior of the transgenic plants are not different to those of wild-type plants
of the different carbon sources tested, rice straw induces maximal levels of cellulase. The addition of ethanol (1%, v/v) results in 8fold increased expression of endoglucanase. The expression profiles of different components of cellulase complex are coregulated in Mycothermus thermophilus
strain produces considerable amounts of extracellular hydrolytic enzymes on lignocellulosic substrates at 55°C incubated for 8 days in 150 ml shake flask experiments. The maximum enzyme activities on wheat straw and guayule bagasse are: xylanase 130.1 U/mg, inulinase 34.1 U/mg, carboxymethylcellulase 4.8 U/mg, filter paper assay (FPase) 5.5 FPU/g and pectinase 3.2 U/mg, respectively
deletion of isoform Cel9C causes a modest decrease in cellulose utilization. Cells of a mutant lacking both isoforms Cel5B and Cel9C are completely deficient in growth on cellulose
in solid state fermentation using lignocellulosic materials as substrates, Myceliophthora thermophila JCP 1-4 is the best producer of endoglucanase (357,51 U/g), beta-glucosidase (45.42 U/g), xylanase (93,11 U/g) and avicelase (3.58 U/g) among the strain tested
at 45°C, lignin derived from acid hydrolyzed liquid hot water pretreated bagasse completely adsorbes cellulolytic enzymes from Trichoderma reesei within 90 min, while lignin derived from enzyme hydrolyzed liquid hot water pretreated bagasse adsorbes only 60% of Trichoderma reesei endoglucanase, exoglucanase and beta-glucosidase activities, overview. At 30°C, adsorption of all of the enzymes is minimal and enzyme hydrolysis at 30°C approaches that at 45°C after 168 h. Simultaneous saccharification and fermentation (SSF) and consolidated bioprocessing (CBP), both carried out at 30-32°C, offer viable options for mitigating lignin-derived inhibition effects
compared with other non-halotolerant counterparts, enzyme NMgh45 is enriched with acidic amino acids on the protein surface, and the conformation of NMgh45 is stable at high salinity condition, three-dimensional structure, molecular modeling and dynamic simulations using the structures with PDB IDs 1L8F, 2ENG, and 5GLX_A as the templates, overview
enzyme structure analysis using small-angle X-ray scattering and homology modelling with the crystallographic model of the endoglucanase TfCel9A (PDB ID 1JS4), structure comparisons
enzyme structure analysis using small-angle X-ray scattering and homology modelling with the crystallographic model of the endoglucanase TfCel9A (PDB ID 1JS4), structure comparisons
relationship between structure and thermostability in fungal GH5 endoglucanases, hydrogen bond propensities at 25°C across all simulations for residues within the alpha1-4 or beta1-4 modules, excluding hydrogen bonds involved in helical interactions, of wild-type parent and mutant enzymes, overview, barrel stabilization by hydrogen bond networks
relationship between structure and thermostability in fungal GH5 endoglucanases, hydrogen bond propensities at 25°C across all simulations for residues within the alpha1-4 or beta1-4 modules, excluding hydrogen bonds involved in helical interactions, of wild-type parent and mutant enzymes, overview, barrel stabilization by hydrogen bond networks
relationship between structure and thermostability in fungal GH5 endoglucanases, hydrogen bond propensities at 25°C across all simulations for residues within the alpha1-4 or beta1-4 modules, excluding hydrogen bonds involved in helical interactions, of wild-type parent and mutant enzymes, overview, barrel stabilization by hydrogen bond networks
relationship between structure and thermostability in fungal GH5 endoglucanases, hydrogen bond propensities at 25°C across all simulations for residues within the alpha1-4 or beta1-4 modules, excluding hydrogen bonds involved in helical interactions, of wild-type parent and mutant enzymes, overview, barrel stabilization by hydrogen bond networks
residues N95D and D117N are both essential for the catalytic reaction. Enzyme structure homology modelling using the crystal structure of endoglucanase V-like protein PcCel45A (PDB code 3X2N) as a template. Asn92 as catalytic residue is conserved in FpCel45
the enzyme belongs to the glycosyl hydrolase family 7, GH7. Residue Glu197 acts as the active-site nucleophile and Glu202 is the acid-base catalyst, and this is consistent with a catalytic mechanism leading to a net retention of configuration at the anomeric carbon in the deep substrate binding cleft
the enzyme consists of a glycoside hydrolase family 6 catalytic domain (GH6) and a family 2 carbohydrate binding module (CBM2) that are connected by a linker rich in prolines and threonines. Comparative studies with a truncated variant of the enzyme show that the CBM increases substrate binding, while not affecting thermal stability. Importantly, at higher substrate concentrations the full-length enzyme is outperformed by the catalytic domain alone, underpinning previous suggestions that CBMs may be less useful in high-consistency bioprocessing
the molecular docking simulations of MtGH45 reveal the requirements of the sites -2, -1, +1, +2 and +3 to be occupied for hydrolysis. Molecular docking of C4, C3 and C2 is unproductive
the unique GH5 cellulase member in the extreme halotolerant fungus Aspergillus glaucus CCHA is an endoglucanase with multiple tolerance to salt, alkali and heat. Homology modeling of AgCMCase
the unique GH5 cellulase member in the extreme halotolerant fungus Aspergillus glaucus CCHA is an endoglucanase with multiple tolerance to salt, alkali and heat. Homology modeling of AgCMCase
the enzyme has no recognizable carbohydrate binding module, but a glycoside hydrolase family 6 domain
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additional information
Thermochaetoides thermophila IMI 039719
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the enzyme belongs to the glycosyl hydrolase family 7, GH7. Residue Glu197 acts as the active-site nucleophile and Glu202 is the acid-base catalyst, and this is consistent with a catalytic mechanism leading to a net retention of configuration at the anomeric carbon in the deep substrate binding cleft
the enzyme has no recognizable carbohydrate binding module, but a glycoside hydrolase family 6 domain
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additional information
Thermochaetoides thermophila DSM 1495
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the enzyme belongs to the glycosyl hydrolase family 7, GH7. Residue Glu197 acts as the active-site nucleophile and Glu202 is the acid-base catalyst, and this is consistent with a catalytic mechanism leading to a net retention of configuration at the anomeric carbon in the deep substrate binding cleft
enzyme structure analysis using small-angle X-ray scattering and homology modelling with the crystallographic model of the endoglucanase TfCel9A (PDB ID 1JS4), structure comparisons
enzyme structure analysis using small-angle X-ray scattering and homology modelling with the crystallographic model of the endoglucanase TfCel9A (PDB ID 1JS4), structure comparisons
enzyme structure analysis using small-angle X-ray scattering and homology modelling with the crystallographic model of the endoglucanase TfCel9A (PDB ID 1JS4), structure comparisons
enzyme structure analysis using small-angle X-ray scattering and homology modelling with the crystallographic model of the endoglucanase TfCel9A (PDB ID 1JS4), structure comparisons
modelling of the metal-ion sites in the protein three-dimensional structure, overview
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additional information
Thermochaetoides thermophila CBS 144.50
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the enzyme belongs to the glycosyl hydrolase family 7, GH7. Residue Glu197 acts as the active-site nucleophile and Glu202 is the acid-base catalyst, and this is consistent with a catalytic mechanism leading to a net retention of configuration at the anomeric carbon in the deep substrate binding cleft
residues N95D and D117N are both essential for the catalytic reaction. Enzyme structure homology modelling using the crystal structure of endoglucanase V-like protein PcCel45A (PDB code 3X2N) as a template. Asn92 as catalytic residue is conserved in FpCel45
the unique GH5 cellulase member in the extreme halotolerant fungus Aspergillus glaucus CCHA is an endoglucanase with multiple tolerance to salt, alkali and heat. Homology modeling of AgCMCase
enzyme structure analysis using small-angle X-ray scattering and homology modelling with the crystallographic model of the endoglucanase TfCel9A (PDB ID 1JS4), structure comparisons
enzyme structure analysis using small-angle X-ray scattering and homology modelling with the crystallographic model of the endoglucanase TfCel9A (PDB ID 1JS4), structure comparisons
enzyme structure analysis using small-angle X-ray scattering and homology modelling with the crystallographic model of the endoglucanase TfCel9A (PDB ID 1JS4), structure comparisons