Lipase-catalyzed Stereoselective Hydrolysis of 2-Acyloxy-3-chloropropylp-toluenesulfonate

Abstract
Lipase-catalyzed stereoselective hydrolysis of 2-acyloxy-3-chloropropyl p-toluenesulfonate (1) was investigated. From the screening tests, lipases from Pseudomonas aeruginosa, Aspergillus niger, Mucor species, Rhizopus delemar and Rhizopus japonicus were found to hydrolyze (R,S)-1 stereoselectively to afford (R)-1 and (S)-2-hydroxy-3-chloropropyl p-toluenesulfonate (2). Among these enzymes, the lipase from Pseudomonas aeruginosa was found to possess the highest hydrolytic activity and stereoselectivity in more than 99% e.e.

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