Purification and Characterization of Alkaline Proteinase from Alkalophilic Bacillus sp

Alkaline proteinase was purified from Bacillus sp. isolated from soil. The pH optimum was 11.5 at 37 degree C. Calcium divalent cation was effective in stabilizing the enzyme, especially at higher temperatures. The proteolytic activity was inhibited by the specific serine proteinase inhibitor PMSF (phenylmethylsulfonyl fluoride), and ions of Mg, Mn, Pb, Li, Zn, Ag, and Hg. The enzyme was stable in the presence of detergents, such as Triton-X100, Tween-80, SDS (sodium dodecyl sulfate), and EDTA (ethylenediaminetetraacetic acid), at pH 11.5 and 37 degree C for 30 min. The optimum pH was 11.5 at 37 degree C, and the optimum temperature was 62 degree C at pH 11.5.