Characterisation of purified protease from Bacillus subtilis BS166

Proteases are enzymes that break up the peptide bonds of proteins to release amino acids. Proteases showing better stability at alkaline pH and higher temperatures have potential applications in several industrial processes. The present study was aimed at determining the kinetic properties of the partially purified protease obtained from Bacillus subtilis BS166. Bacillus subtilis BS166 can produce protease above 30 ^oC and at pH 7.0. The protease was extracted with 0.1 M phosphate buffer of pH 7.0 and precipitated with ammonium sulfate. The activity of the purified protease was higher at pH 9.0 and 40 ^οC and showed zero order kinetics for 10 minutes. When the optimum enzyme concentration was 95.52 μg, a straight line was obtained in the Lineweaver-Burk plot graph. Michaelis constant for the purified enzyme was 50.9 μM and Vmax was 2833.4 pmolmin^-1 at pH 9.0 and 40 ^oC.