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Lipase‐catalyzed enantioselective acidolysis of chiral 2‐methylalkanoates
Author(s) -
Engel KarlHeinz
Publication year - 1992
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02540565
Subject(s) - enantioselective synthesis , kinetic resolution , lipase , enantiomer , chemistry , catalysis , candida antarctica , heptane , organic chemistry , stereochemistry , enzyme
Lipase from Candida cylindracea catalyzes the acidolysis between racemic 2‐methylalkanoates and fatty acids in heptane with a preference for the (S)‐configurated esters. Velocity and enantioselectivity of the acyl transfer are strongly influenced by the structures of the initial substrates. The potential of this strategy for kinetic resolution of the enantiomers of chiral 2‐methylalkanoates is demonstrated. Limitations of the procedure due to the reversible character of the reaction are discussed.