Studies on Industrially Significant Haloalkaline Protease from Bacillus sp. JSGT Isolated from Decaying Skin of Tannery
Eight bacterial strains were isolated from collagen layer of decaying skin sample. Three isolates exhibited the prominent zones of clearance on skim milk agar medium at pH 9.5. These isolates were then characterized and identified. One of the haloalkalophilic isolates belonged to the genus Bacillus. Maximum enzyme activity (228.29 ± 1.89 PU/ ml) was found at pH 9 and temperature 37°C in the strain which is designated as Bacillus sp. JSGT. Basic properties such as effects of different temperature, pH, metal ions and inhibitors on protease activity were also studied. Maximum activity was obtained at pH 9 at 55°C. Ca+2 and Mg+2 ions were found to enhance the relative enzyme activity up to 158 and 136% respectively. However, the activity of protease was completely inhibited by phenyl methyl sulfonylflouride (PMSF) that showed its serine nature. The results indicated that enzyme produced by Bacillus sp. JSGT is active within broad ranges of temperature and pH. These characteristics render its potential use in leather and detergent industries.
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