Lipase-catalyzed transesterification of aryl-substituted alkanols in an organic solvent

Lipase-catalyzed transesterifications of aryl-substituted alcohols with vinyl acetate in organic solvents have been investigated. V-max of (R)-1-phenylethanol is much larger than its (S)-counterpart, although their K(m)s are similar each other. It is proposed that a lipase from Pseudomonas cepacia can form a complex easily with each enantiomer, although the complex with the (S)-enantiomer is abortive. Enantioselectivity for the ortho-substituted 1-phenylethanol is smaller than those for the others. A three-dimensional model for the active domain of the lipase has been proposed to explain the enantioselectivity and substrate selectivity of the lipase.