ISOLATION, PURIFICATION, AND PROPERTIES OF CELLULASES FROM ASPERGILLUS TERREUS AND PENICILLIUM VARIABILE

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Abstract
Cellulases from A. terreus and P. variabile were isolated and purified nearly 100-fold. Enzyme production reached a maximum on the seventh day of incubation. The properties and activities of the purified cellulases were studied. At constant enzyme concentration, the activity increased with the increase in substrate concentration but the percentage of the substrate hydrolyzed decreased. Of the two purified cellulases, that from A. terreus seemed to be a purer product and was tested for its homogeneity and enzymic nature. A unienzymic nature was indicated by the observation that no resolution of the enzyme could be effected by electrophoresis. Standard solubility and diffusion tests gave no indication of heterogeneity in the purified cellulase; this finding was confirmed by the presence of only one peak in both gel filtration and ion-exchange chromatography. Random splitting of α-cellulose and carboxymethylcellulose (CMC) was indicated.