Production and characterization of alkaline protease from <em>Halobacillus dabanensis</em>

601-610An alkaline protease producing bacteria identified as Halobacillus dabanensis by 16S rDNA gene analysis was evaluated for production and characterization of its various properties. The maximum alkaline protease production was found by incubating the production media of pH 9.0 at 37°C under shaking condition at 180 rpm in presence of 4.0 g/l of casein. The alkaline protease exhibited its maximum activity at pH 9.0 and temperature of 50°C respectively. The enzyme showed excellent thermal stability at 50°C by retaining 79% of its original activity up to 8 h. Similarly, the enzyme was highly stable at pH 9.0 and 7.0 by retaining 93% of its original activity up to 5 h. Km and Vmax values towards casein as substrate were as 24.87 mg and 81.30 U respectively. The zinc sulphate, manganese chloride and mercury chloride inhibited the alkaline protease activity as compared to control. Residual activity 83.41% and 62.26% was achieved in presence of EDTA and β-mercaptoethanol at 5 mM concentration suggesting its operational stability. The alkaline protease also showed excellent stability in presence of Triton X-100, Tween-80, detergents like Tide and Rin and hence could be exploited in detergent and leather processing units