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 catalase, 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 spectrum of the catalase showed a soret band at 406 nm, indicating that the enzyme is a heme protein. As a result of the determination of various inhibitors on the catalase activity, ISK-1 catalase was a typical monofunctional catalase. The specific activity throughout the growth of batch culture with or without aeration was investigated and three-fold elevated activity was found in the aerobic culture.