Purification and Characterization of Thermostable Cellulase from Soil Bacteria of Northwestern Himalayas

Microbial degradation of cellulose has economic potential in enzyme industry as well as for the production of biofuels from plant biomass. In this study bacteria were isolated from soil sample of Leh region and screened for different hydrolases. The strain Bacillus SL4 was found as potent producer of cellulase. The enzyme from Bacillus SL4 was purified by ion exchange chromatography and characterized. The molecular weight of enzyme was 82kDa. Enzyme showed an optimum activity at pH 6.0 and highly stable between 55-65 °C. The crude cellulase had activity toward CMC, avicell, β- glucan and cellobiose, but there was no detectable activity on xylan and p-nitrophenyl-β-d-glucopyranoside (PNPG). The rate of CMC degradation was higher than any other substrates used in this study. The enzyme reported in this paper was able to hydrolyze both -β-1, 4 and β-1,3 glycosidic linkages and thermostable at high temperature.