Abstract
The present study deals with the characterization of keratinases from Bacillus brevis and Bacillus cereus isolated from the poultry wastes. During the enzyme-substrate reaction, the crude keratinases of the two bacteria showed their maximum activity at 35 and 500C and pH 10 and pH 8 with optimum incubation period of 80 and 70 minutes, respectively. The keratinases showed their activity towards casein, keratin, BSA and gelatine. It was found that keratinases belongs to metalloprotease and serine protease. Ca2+, Mg2+ and Triton X-100 increased the activity of both the keratinases, while Cu2+ and Hg2+ decreased the activity. β-Mercaptoethanol and Dimethyl sulfoxide increased the crude keratinase activity of B. brevis and B. cereus respectively, while β-Mercaptoethanol had negative effect on keratinase of B. cereus. The Chittagong Univ. J. B. Sci.,Vol. 7(1 &2):109-119, 2012.
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