Regulation of Activity of Chloroperoxidase from Serratia marcescens

V. N. Burd^1*, O. V. Vasilyeva¹, A. I. Voskoboev¹, and K.-H. van Pee²

¹Grodno State University, Pereulok Dovatora 3/1, Grodno, 230012 Belarus; fax: (0152) 44-8461; E-mail: burd@univer.belpak.grodno.by

²Institute of Biochemistry, Technical University, Dresden, Germany

^* To whom correspondence should be addressed.

Received February 5, 1998; Revision received July 7, 1998

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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.

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KEY WORDS: Serratia marcescens, chloroperoxidase, regulation of activity

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