Abstract
Enzyme catalyzed transesterification of rac-2-chloro-1-(2-furyl)ethanol rac- 1 using vinyl acetate afforded the enantiomers of 2-chloro-1-(2-furyl)ethanol 1 and 2-chloro-1-(2-furyl)ethyl acetate 2 in high enantiomeric excess. Several lipases were used for the kinetic resolution of racemic 2-chloro-1-(2-furyl)ethanol l, in which the lipases from Pseudomonas cepacia, Candida antarctica and Candida cylindracea displayed high enantioselectivity towards 1.
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