TTCBH6B contains a familial 6-glycosyl hydrolase catalytic domain and a type I carbohydrate binding module, the enzyme belongs to the glycosyl hydrolase family 6, GH6
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
the enzyme is a key virulence factor of Xanthomonas oryzae pv. oryzae and also a potent inducer of innate immune responses of rice. The specific exoglucanase activity of the enzyme is required for this protein to promote the growth of Xanthomonas oryzae pv. oryzae in rice
cellobiohydrolases (CBHs) are important components of cellulose degrading enzyme systems especially secreted by fungi. Classified as exoglucanases, CBHs liberate cellobiose units from reducing and nonreducing ends of cellulose
cellobiohydrolases (CBHs) are important components of cellulose degrading enzyme systems especially secreted by fungi. Classified as exoglucanases, CBHs liberate cellobiose units from reducing and nonreducing ends of cellulose
cellobiohydrolases (CBHs) are important components of cellulose degrading enzyme systems especially secreted by fungi. Classified as exoglucanases, CBHs liberate cellobiose units from reducing and nonreducing ends of 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
cellobiohydrolases (CBHs) are important components of cellulose degrading enzyme systems especially secreted by fungi. Classified as exoglucanases, CBHs liberate cellobiose units from reducing and nonreducing ends of cellulose
cellobiohydrolases (CBHs) are important components of cellulose degrading enzyme systems especially secreted by fungi. Classified as exoglucanases, CBHs liberate cellobiose units from reducing and nonreducing ends of cellulose
cellobiohydrolases (CBHs) are important components of cellulose degrading enzyme systems especially secreted by fungi. Classified as exoglucanases, CBHs liberate cellobiose units from reducing and nonreducing ends of cellulose
cellobiohydrolases (CBHs) are important components of cellulose degrading enzyme systems especially secreted by fungi. Classified as exoglucanases, CBHs liberate cellobiose units from reducing and nonreducing ends of cellulose
the enzyme is a key virulence factor of Xanthomonas oryzae pv. oryzae and also a potent inducer of innate immune responses of rice. The specific exoglucanase activity of the enzyme is required for this protein to promote the growth of Xanthomonas oryzae pv. oryzae in rice
the enzyme from overexpressing line C10 performs better than the wild-type from ZU-02 in enzymatic hydrolysis because the exoexo-synergism plays a role, overview
celB and beta-glucosidase function effectively together to produce glucose from carboxymethyl cellulose covalently immobilised on plasma immersion ion implantation treated polystyrene. Recombinant celB is optimally immobilised in a pH range 5-6.5 and exhibits a maximum activity when used at pH 5.5. Immobilized celB shows a similar activation energy to the free enzyme in hydrolysis of carboxymethyl cellulose. The areal density of immobilized celB is estimated to be 0.3 mg/cm2. Immobilized celB retains 70% of its initial activity after 4 uses of 23 hours each. High ratio of immobilized beta-glucosidase enhances the activity of immobilized celB in hydrolysis of carboxymethyl cellulose
study of adsorption to microcrystalline cellulose (Avicel) of pure cellobiohydrolase I from Trichoderma reesei. Adsorption isotherms of the enzyme are measured. Several models (Langmuir, Freundlich, Temkin, Jovanovic) are tested to describe the experimental adsorption isotherms. The isotherms do not follow the basic (one site) Langmuir equation. The experimental isotherms are best described by a model of Langmuir type with two adsorption sites and by a combined Langmuir-Freundlich model (analogous to the Hill equation). The isotherms when analyzed with the combined Langmuir-Freundlich model indicated presence of unequal binding sites on cellulose and/or negative cooperativity in the binding of the enzyme molecules
study of adsorption to microcrystalline cellulose (Avicel) of pure cellobiohydrolase I from Trichoderma reesei. Adsorption isotherms of the enzyme are measured. Several models (Langmuir, Freundlich, Temkin, Jovanovic) are tested to describe the experimental adsorption isotherms. The isotherms do not follow the basic (one site) Langmuir equation. The experimental isotherms are best described by a model of Langmuir type with two adsorption sites and by a combined Langmuir-Freundlich model (analogous to the Hill equation). The isotherms when analyzed with the combined Langmuir-Freundlich model indicated presence of unequal binding sites on cellulose and/or negative cooperativity in the binding of the enzyme molecules
study of adsorption to microcrystalline cellulose (Avicel) of pure cellobiohydrolase I from Trichoderma reesei. Adsorption isotherms of the enzyme are measured. Several models (Langmuir, Freundlich, Temkin, Jovanovic) are tested to describe the experimental adsorption isotherms. The isotherms do not follow the basic (one site) Langmuir equation. The experimental isotherms are best described by a model of Langmuir type with two adsorption sites and by a combined Langmuir-Freundlich model (analogous to the Hill equation). The isotherms when analyzed with the combined Langmuir-Freundlich model indicated presence of unequal binding sites on cellulose and/or negative cooperativity in the binding of the enzyme molecules
the enzyme from overexpressing line C10 performs better than the wild-type from ZU-02 in enzymatic hydrolysis because the exoexo-synergism plays a role, overview