Partial purification and characterization of alkaline protease from halophilic bacteria bacillus sp

Alkaline protease, a hydrolytic enzyme from a novel strain of halophilic bacteria Bacillus sp. was purified up to 1.42 fold purification with a recovery of about 5% and then characterized at various operating conditions. Zymography of the different fractions showed the hydrolysis of casein by the enzyme. The maximum activity of purified alkaline protease was observed at pH 9.0 and at a temperature of 50˚C using casein as substrate, respectively. Certain metal ions like MgCl2, CaCl2 andβ-mercaptoethanol enhanced alkaline protease activity while HgCl2and EDTA inhibited the enzyme activity. TheKm and Vmax for partially purified enzyme were 1.17mg/ml and 2.22mg/ml/min respectively.