Regulation of activity of chloroperoxidase from Serratia marcescens.

Autor: Burd VN; Grodno State University, Grodno, 230012, Belarus. burd@univer.belpak. grodno.by., Vasilyeva OV, Voskoboev AI, van Pee KH
Jazyk: angličtina
Zdroj: Biochemistry. Biokhimiia [Biochemistry (Mosc)] 1998 Nov; Vol. 63 (11), pp. 1299-301.
Abstrakt: The influence of various factors on the activity of chloroperoxidase from Serratia marcescens was investigated. The enzyme is active only in acetate-containing buffers within the pH range 4.2-5.8. F-, Cu2+, [Fe(CN)6]4+, and [Fe(CN)6]3+ inhibit the enzyme. The chloroperoxidase is thermostable and resistant to the effect of lower alcohols.
Databáze: MEDLINE