Biochemical Characterization of Alkaline Protease from Bacillus Circulans Mtcc 7906
2018
Inderjeet Kaur
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/mlusing 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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