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Regulation of activity of chloroperoxidase from Serratia marcescens
V N Burd1, O V Vasilyeva, A I Voskoboev
1Grodno State University, Grodno, 230012, Belarus. burd@univer.belpak. grodno.by.
Biochemistry. Biokhimiia
|December 29, 1998
Abstract:
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.

