Regulation of activity of chloroperoxidase from Serratia marcescens

摘要

The effect of many factors on the halogenating activity of chloroperoxi-dase from Serratia marcescens have been investigated. The enzyme was only active in acetate buffer with the pH optimum between pH 4,2 and 5,8. The brominating activity was inhibited by F, Cu~(2+), [Fe(CN)_6]~(4+) and [Fe(CN)_6]~(3+). Chloroperoxidase is thermostable and very resistant to alkohols.