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Regulation of Activity of Chloroperoxidase from Serratia marcescens

V. N. Burd1*, 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
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.
KEY WORDS: Serratia marcescens, chloroperoxidase, regulation of activity