Chloroperoxidase-Catalysed Halogenation of Apolar Compounds Using Reversed Micelles

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Abstract
The chloroperoxidase from the mold Caldariomyces fumago was entrapped into reversed micelles composed of aqueous buffer, cetyltrimethylammonium chloride or bromide, pentanol and octane. The surfactant serves a dual function: i) it stabilizes the reversed micelle, and ii) the halide counter ion is used as a substrate for the enzyme. 2-Monochlorodimedon and 1,3-dihydroxybenzene were halogenated with this system, giving their 2-halo and 4-halo derivatives, respectively. The reaction rates were about twice as high as in aqueous media. Enzyme activity was maximal at high water content of the micelles and at relatively low pentanol concentration. The enzyme was inactivated by high concentrations of hydrogen peroxide.