
The five endoglucanases(CMCase) components from Aspergillus aculeatus SM-L22 were separated and purified by exclusion chromatography and ion-exchange chromatography. Five components(EG II-1, EG II-2, EG III-1, EG III-2 and EG IV) had molecular weights of 38.7, 34.4, 31.4, 36.9 and 23.7 kD by SDS-PAGE, respectively, and IEF showed their pI were pH < 3.5, < 3.5, 4.9, 4.4 and 5.0, respectively. All of them have maximum reactive activities at pH 3.5-4.0; and the optimum temperatures were 55 degrees C, 60 degrees C, 60 degrees C-70 degrees C, 60 degrees C-70 degrees C and 60 degrees C, respectively. EG II-1 and EG II-2 can only act such morphological substrates as CMC or phosphated cellulose, but EG III-1, EG III-2 and EG IV can active xylan also. The activities of all components were stimulated by Fe2+ except EG IV, EG III-2 was activited mostly by Fe2+. The kinetics' showed that there were no relativies between the affectivity of cellulases and its Km.
Fungal Proteins, Molecular Weight, Aspergillus, Cellulase, Enzyme Stability, Substrate Specificity
Fungal Proteins, Molecular Weight, Aspergillus, Cellulase, Enzyme Stability, Substrate Specificity
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