Chemically modified mutants of subtilisin Bacillus lentus catalyze transesterification reactions better than wild type

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-CH3, of subtilisin Bacillus lentus catalyzes the transesterification of N-acetyl-L-phenylalanine vinyl ester with beta-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. (C) 1998 Elsevier Science Ltd. All rights reserved.