Abstract
A combined site-directed mutagenesis and chemical modification strategy has been used to create superior enzyme catalysts for the resolution of racemic primary and secondary alcohols using a transesterification reaction. The chemically modified mutant, N62C–S–CH 3, of subtilisin Bacillus lentus catalyzes the transesterification of N-acetyl-L-phenylalanine vinyl ester with β-branched primary alcohols faster than wild type. The cysteine mutant, M222C, of subtilisin Bacillus lentus gives higher yields (98% and 92% yields with 1-phenylethanol and 2-octanol, respectively, versus 19% and 10% for wild type) and better enantioselectivity than wild type when secondary alcohols are used.
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