Purification and characterization of cellulase from Pseudomonas sp. isolated from waste dumping site soil

Cellulases carry out hydrolysis of cellulose to liberate simple sugars. Cellulase is a complex enzyme which requires synergistic action of endoglucanase, exoglucanase and β-glucosidase.1 Currently, commercial cellulases are obtained from some species of fungi and bacteria. Comparatively, bacterial species have better growth rate and resistance to extreme environments.2–4 Microbial cellulases have applications in many industries, particularly in textile industry, pulp and paper industry, food industry and detergent industry as well as in cellulosic waste management.5–7 Cellulases also play an important role in the hydrolysis of renewable lignocellulosic waste materials for the production of biofuels like bioethanl.8 There is an ever increasing need for cost-effective production and identification of new sources of cellulases. Therefore, the present study was undertaken to isolate potential cellulose degrading bacteria from cellulosic waste dumping site soil. Selected bacterial isolates were screened for the endoglucanase enzyme activity using CMCase (carboxymethyl cellulase) assay. Cellulose producing Pseudomonas sp. are reported in very limited articles, although Pseudomonas can utilize cellulose as main carbon source and may serve profitably as a biological agent for isolation of cellulase enzyme.9 Therefore, the cellulase enzyme was purified from Pseudomonas sp., and various parameters for its optimum activity were characterized.