purification and characterization of a protease from bacillus sp.agt under solid state fermentation

Alkaline protease was produced by Bacillus SP.AGT by solid state fermentation. The protease was purified to the homogeneity. Purified protease was obtained from acetone precipitation and ion exchange chromatography. The molecular weight of the protease was 29 kDa as estimated by SDS-PAGE. The enzyme was stable and active with pH 9.0 and with temperature of 40° C. However the enzyme was quite unstable at temperature beyond 60° C and pH below 8.0 and above 10.0. Parameters such as pH and temperature with respect to enzyme activity demonstrated clearly the impact of these process parameters on