Lipase-Catalyzed Kinetic Resolution of Baylis-Hillman Products.

Abstract Lipase-catalyzed kinetic resolution of the various Baylis–Hillman products, α-methylene-β-hydroxy compounds, were examined. When lipase PS was used as a biocatalyst in acetonitrile, transesterification of racemic ethyl 3-hydroxy-2-methylenebutanoate or 3-hydroxy-2-methylenepentanoate proceeded in a practical enantiomeric excess. The resolution by hydrolysis of the acetate derivatives was also tried. In contrast, in case of racemic ethyl 3-acetoxy-2-methylenepentanoate, under the conditions using lipase AK, the E value of the resolution was >321.