[Hydrolysis of phosphoether bonds of heme-independent chloride peroxidase from Serratia marcescens].

Heme- and metal-independent chloroperoxidase from Serratia marcescens W 250 is shown to be capable of catalyzing the p-nitrophenyl phosphate hydrolysis. The parameters of the phosphatase reaction are determined and inhibitors and activators of the process are found. A hypothetical mechanism of the hydrolysis of phosphoesters by heme- and metal-independent haloperoxidases is suggested.

Phosphatase activity of non-heme chloroperoxidase from the bacterium Serratia marcescens.

Haloperoxidases are enzymes capable of formation of carbon-halogen bonds in the presence of hydrogen peroxide and halide ions. A mechanism of halogenation catalyzed by heme- and metal-independent bacterial haloperoxidases differs from other representatives of this group of enzymes. Here we report for the first time that bacterial non-heme haloperoxidases possess a phosphatase activity.

[Immobilization of chloroperoxidase from Serratia marcescens].

A bacterial non-heme chloroperoxidase from Serratia marcescens W 250 was immobilized in calcium-alginate gel. Methods for stabilization of the immobilized enzyme were developed, and some kinetic parameters of the immobilized preparations were determined. The enzyme encapsulated into the gel granules in the presence of potassium ferricyanide followed by treatment with glutaraldehyde demonstrated the highest stability under the reaction conditions.

Regulation of activity of chloroperoxidase from Serratia marcescens.

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.

Purification and properties of a non-haem chloroperoxidase from Serratia marcescens.

A non-haem chloroperoxidase was isolated from the enteric bacterium Serratia marcescens. The enzyme was purified to homogeneity by heat treatment, ammonium sulfate precipitation, ion exchange chromatography, gel filtration and dye-ligand affinity chromatography. Native chloroperoxidase has a molecular mass of 58 kDa and consists of two identical subunits of 29 kDa.