抄録
An alkaline proteinase produced by Bacillus sp. was purified and crystallyzed through isopropanol or ammonium sulfate precipitation, decolorization with DEAF-cellulose and gel filtration with Sephadex G-100. The optimum pH for caseinhydrolysis was 11.5 and the activity was completely inactivated after incubation with DFP. The specific activity on Hammersten casein was about 4, 500 units/mg enzyme protein. The enzyme also hydrolyzed synthetic ester substrate such as Ac-Tyr-OEt, Ac-Phe-OEt or Bz-Met-OMe. The isoelectric point was pH 10.7, and the molecular weight was estimated to be about 17, 500 by the sedimentation equilibrium method and 16, 000 by gel filtration method. Some physicochemical properties and the amino acid composition of the enzyme were investigated, indicating that the enzyme is distinguishable from alkaline proteinase of Bacillus species so far reported.
