Chloroperoxidase catalysed oxidation of benzyl alcohol using tert-butyl hydroperoxide oxidant in organic media

The quantitative oxidation of benzyl alcohol to benzaldehyde using the enzy me chloroperoxidase (CPO) from Caldariomyces fumago as catalyst and tert-bu tyl hydroperoxide (t-BuOOH) as a cosubstrate for the enzyme, in organic sol vent is demonstrated. The enzymatic transformation of primary alcohols to a ldehydes has not previously been shown in predominantly organic solvent usi ng CPO, and in aqueous media, has only been reported to have been effected in moderate yields. A simple procedure for this transformation was carried out using 10 mu mol each of benzyl alcohol and t-BuOOH dissolved in water-s aturated isooctane (1.5 ml), 0.5 mu l CPO solution (10 units) in pH 4.0 ace tate buffer. The reaction rates obtained in organic media were similar to t hat obtained in aqueous media, the enzyme was found to be significantly sta bilised towards peroxide dependent inactivation and no continuous addition of the peroxide was necessary.