Biochemical features of an alkaline protease for symbiotic bacterium of bacillus sp CH96

Proteases constitute one of the most important groups of commercial enzymes accounting for approximately 60-65% of the global enzyme market. These enzymes have diverse applications in a variety of industrial processes involving detergents, brewing, photographic, medical diagnostics, food, pharmaceutical, silk, and leather processing. In this study a monomeric protease with an approximate molecular mass of 25.79 kDa was purified from Bacillus sp CH96. The enzyme exhibited a maximal activityat pH 8 and 60 °C. The enzyme was stable and active in the presence of surfactants including Tween 80, SDS, CTAB, triton X-100 and oxidizing agent hydrogen peroxide. Its activity increased in the presence of Mg2+, K +, Ca2+ and Fe2+ ions, but Hg2+ and Ba2+ reduced activity.

کلیدواژه ها:

Bacillus sp CH96 ، biochemical properties ، protease