Catalase of Staphylococcus warneri ISK-1 isolated from Nukadoko

An intracellular catalase from Staphylococcus warneri ISK-1 was purified to homogeneity in a six-step purification procedure. The purification of cata lase, as judged by the final specific activity of 10,800 U mg(-1), was 310- fold with a 14% yield. The native enzyme had a molecular weight of 125,000 and was composed of two subunits of equal size (64,000). The absorption spe ctrum of the catalase showed a soret band at 406 ma, indicating that the en zyme is a heme protein. As a result of the determination of various inhibit ;ors on the catalase activity, ISK-1 catalase was typical monofunctional ca talase. The specific activity throughout the growth of batch culture with o r without aeration was investigated and three-fold elevated activity was fo und in the aerobic culture.