Purification and properties of proteolytic enzyme[s] from bacillus licheniformis, G-19 growing on wheat straw using solid state fermentation

ABSTRACT

Solid state fermentation was used for the production of proteolytic enzyme[s] by Bacillus licheniformis G-19 while incubated in the open air [at room temperature] The partial purification methods were achieved by filtration, dialysis and precipitation with ammonium sulfate The partially purified enzyme was purified 28.5 folds by fractionation by column chromatography on sephadex G-200 The purified enzyme showed maximal activity at pH 6.8 [using phosphate buffer 0.2 M] and at 50COn the other hand, enzyme activity was inhibited in the presence of Cu2+ and Co2+ at certain levels, while Ca2+ and Mg2+ had an activating effectThe amino acids composition of the purified enzyme was also determined