BIOLOGICAL PREPARATION OF AN OPTICALLY-ACTIVE ALCOHOL .3. ENANTIOSELECTIVE HYDROLYSIS OF ALPHA-CYANO-3-PHENOXYBENZYL ACETATE WITH ARTHROBACTER LIPASE

Lipase-catalyzed enantioselective hydrolysis of the acetic ester of racemic a-cyano-3-phenoxybenzyl alcohol (CPBA) was examined to prepare (S)-CPBA. Most of the lipases tested hydrolyzed (S)-CPBA acetate preferentially, while Candida cylindracea lipase favored (R)-CPBA acetate. Enantioselective hydrolysis by Arthvobactev lipase gave the optically pure (-S)-CPBA in the reaction mixture of pH 4.0. The kinetic studies showed that (R)-CPBA acetate reacted as a competitive inhibitor. The Avthvobactev lipase solution in the water/oil biphasic reaction system could be used repeatedly. The lipase immobilized to resins had insufficient activity or low operational stability for the repeated batch reaction. The unhydrolyzed (R)-CPBA acetate was racemized by heating with triethylamine and could be reused as the substrate of the enzymatic hydrolysis. A chemico-enzymatic process for the preparation of (S)-CPBA was developed based on these studies. © 1990 by the Japan Society for Bioscience, Biotechnology, and Agrochemistry.