Paper Details

Name: Inderjeet Kaur, Ramandeep Kaur
Email: kaurinder@lkc.ac.in
Country: India

Year: 2014
Volume: Volume-1, Issue-2

In the present study, an extracellular alkaline protease of Bacillus circulans was cultivated on modified Reese medium at a pH of 9.5, temperature of 28oC in 168 hours of incubation. This strain was purified 16.76 folds with specific activity of 1101.0 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 30 kDa on Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The characterization of purified enzyme revealed 9.5 and 70°C as an optimum pH and temperature, respectively. The enzyme was activated by Ba2+, Ca2+, Mn2+, Co2+ and Zn2+ and inhibited by Hg2+ and EDTA. The results thus suggested that the alkaline protease of B. circulans is a metalloprotease with serine at its active centre. The specific activity of this alkaline protease from Bacillus circulans is greater than those of other reported Bacillus sp; therefore, it was concluded that it may be suitable candidate for commercial applications.