ENZYME-CATALYZED KINETIC RESOLUTION OF RACEMIC SECONDARY HYDROPEROXIDES

The kinetic resolution of 1,2,3,4-tetrahydro[1]naphthyl and other secondary and tertiary hydroperoxides has been investigated by acylation with isopropenyl acetate in the presence of various lipases, by chloroperoxidase-catalyzed asymmetric oxidation of sulfides, and by horseradish peroxidase (HRP)-catalyzed reduction in the presence of guaiacol. For preparative purposes, the latter method is the best one and allows for the first time the isolation and characterization of the enantiomerically pure (S)-1,2,3,4-tetrahydro[1]naphthyl hydroperoxide. Tertiary hydroperoxides are not accepted as substrates by HRP.