PURIFICATION AND CHARACTERIZATION OF CELLULOSE DEGRADING ENZYME FROM NEWLY ISOLATED CELLULOMONAS SP

In this study, a cellulolytic bacterium was isolated from soil and was identified as Cellulomonas sp. Maximum endoglucanase production was observed with an inoculum size of 1.5% (v/v), initial medium pH of 7, and substrate concentration of 3% for 48 h of incubation at 33 degrees C. Further supplementation of CMC and tryptone as carbon and nitrogen sources improved endoglucanase production, respectively. The enzyme had a molecular weight of 53.55 kDa. The enzyme had pH and temperature optima of 7.0 and 50 degrees C, respectively. The stability of the enzyme was in the pH range of 6.0 to 8.0 and at temperatures up to 50 degrees C. The metal profile showed that Co2+ and Mn2+ were activators, while Hg2+ and Fe2+ were inhibitors. The enzyme was highly stable toward alcohols. The enzyme had K-m and V-max values of 1.481 mg/mL and 13.64 mM/mL/min against CMC as substrate, respectively.