Abstract
CMCase, Avicelase, β-glucosidase and xylanase of thermophilic fungi, Humicola insolens YH 8, Mucor miehei YH 10 and Talaromyces byssochlamydoides YH 50 were found to possess high degrees of pH- and thermo-stabilities. The stabilities were closely related to its high content of carbohydrate moiety, containing a large amount of N-acetylglucosamine. The carbohydrate moiety was found also important in the raw starch-digestivity of glucoamylase of Aspergillus awamori var. kawachi. The carbohydrate and protein moieties of this enzyme were stepwisely degraded by the combinated actions of proteases and glycosidases, losing the raw starch-digestivity and forming the multiple types and forms of active glucoamylase. Contaminant activities of proteases and glycosidases in the fungal cultures were depressed by the selection of fungal strains, the regulations of culture conditions and the preparations of protease-glycosidase-less mutants, for the purpose of the productions of highly thermostable and raw starch-digestive enzymes.
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