Abstract
The preparative scale kinetic resolution of racemic ethyl 2- and 3-furyl- and 2- and 3-thienyl-3-hydroxypropanoates has been performed by Candida antarctica lipases A and B with vinyl esters. A study based on the present work together with the literature has been carried out in terms of lipase enantiopreference and substrate structure. We also discuss the excellent behavior of the lipase A in O-acylations of secondary alcohols with respect to enantiopreference.
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