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Kinetic resolution of amino acid esters catalyzed by lipases
Author(s) -
Houng JerYiing,
Wu MayLing,
Chen ShuiTein
Publication year - 1996
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/(sici)1520-636x(1996)8:6<418::aid-chir2>3.0.co;2-8
Subject(s) - chemistry , lipase , hydrolysis , moiety , kinetic resolution , organic chemistry , amino acid , biocatalysis , stereoselectivity , aqueous solution , catalysis , enzyme , enantioselective synthesis , biochemistry , reaction mechanism
Racemic amino acids were resolved by lipase via hydrolysis of their esters. Lipases ( Pseudomonas lipase from Amano PS, Rhizopus lipase from Serva, and porcine pancrease lipase from Sigma) could selectively hydrolyze the L‐amino acid esters in aqueous solution with high reactivities and selectivities. The effect of the structural changes in the ester moiety on the stereoselectivity of the lipases was also investigated using D , L ‐homophenylalanine as a model. Procedures were developed for the resolution of natural and unnatural amino acids. © 1996 Wiley‐Liss, Inc.