Enzymatic hydrolyses of acetoxy- and phenethylbenzoates by Candida cylindracea lipase

The lipase from Candida cylindracea (CCL) deacetyles rapidly and selectively all three regioisomer methyl acetoxybenzoates. In the enzymatic hydrolyses of analogous aryl acctoxybenzoates, the difference of reactivity between the acetoxy and benzoyloxy functionalities is reduced and a methoxy group in meta position of the aryl group reverses the reactivity order making the compounds aspirin or aspirin-like prodrugs. The degree of enantioselectivity of the enzymatic hydrolysis of phenethylbenzoates is related to the position of the stereogenic center. Copyright (C) 1996 Elsevier Science Ltd