Enzyme catalyzed hydrolysis of the diesters of cis- and trans-cyclohexanedicarboxylic acids.

Autor: Björkling, Fredrik, Boutelje, John, Gatenbeck, Sten, Hult, Karl, Norin, Torbjörn
Zdroj: Applied Microbiology & Biotechnology; 1985, Vol. 21 Issue 1/2, p16-19, 4p
Abstrakt: Pig liver esterase (EC 3.1.1.1) catalyzed hydrolysis of the dimetrhy ester of meso-cis-1,2-cyclohexanedicarboxylic acid yielded the optically pure ( 1S,2R)-monoester. The corresponding diethyl ester yielded racemic monoester. The diethyl ester of racemic trans-1,2-cyclohexanedicarboxylic acid was kinetically resolved by partial hydrolysis with subtilisin (EC 3.4.21.14) or pig liver esterase. The ( 1R,2R)-monoester had an enantiomeric excess of 45% and was obtained in an enantiomerically pure form through recrystallisation. The remaining ( 1S,2S)-diester exhibited an enantiomeric excess of 83%. The nature of the ester function (methyl, ethyl, and propyl esters) had a great influence on the enantiomeric excess obtained and on the kinetic parameters. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index
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