Laboratory of Microbial Science and Technology, Division of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University
九州大学大学院生物資源環境科学研究科応用微生物学講座
Laboratory of Microbial Science and Technology, Division of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University
九州大学大学院生物資源環境科学研究科応用微生物学講座
Laboratory of Microbial Science and Technology, Division of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University
Laboratory of Microbial Science and Technology, Division of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University
Laboratory of Microbial Science and Technology, Division of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University
九州大学大学院生物資源環境科学研究科応用微生物学講座
Laboratory of Microbial Science and Technology, Division of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University
九州大学大学院生物資源環境科学研究科応用微生物学講座
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 10,800Umg, 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 ausorption 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.