Biochemical Characterization of Alkaline Protease from Bacillus Circulans Mtcc 7906
Journal Title: Research and Reviews in Biotechnology and Biosciences - Year 2018, Vol 5, Issue 1
Abstract
In the present study, an alkaline protease of Bacillus circulans MTCC 7906 was purified 16.2 folds with specific activity of 102815 U/mg in comparison to crude extract using ammonium sulphate precipitation (30-60%), dialysis and DEAE-Cellulose anion exchange chromatography. The molecular weight of the purified enzyme was found to be 46 kDa on Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE). The characterization of partially purified enzyme revealed 9.0 and 60°C as an optimum pH and temperature, respectively, with Km and Vmax of 4.5 mg/ml and 5555 U/ml using casein as substrate. The enzyme was activated by Ba2+, Ca2+, Mn2+, Co2+ and Zn2+ and inhibited by EDTA and ammonium hydroxide. The results thus indicated that the alkaline protease of B. circulans is a metalloprotease with serine at its active centre. Therefore it was concluded that this alkaline protease may be suitable candidate for commercial applications.
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