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Enzyme‐Catalyzed Kinetic Resolution of 1,3‐ anti ‐Diol Monoesters – Efficient Preparation of Enantiomerically Highly Enriched and Unsymmetrically Substituted 1,3‐ anti ‐Diols
Author(s) -
Jakob Florian,
Schneider Christoph
Publication year - 2007
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.200700096
Subject(s) - chemistry , kinetic resolution , candida antarctica , enantiomer , diol , enantioselective synthesis , lipase , hydrolysis , enantiomeric excess , catalysis , organic chemistry , acetylation , triacylglycerol lipase , stereochemistry , enzyme , biochemistry , gene
Candida antarctica Lipase B (CALB) catalyzed the highly enantioselective acetylation of 1,3‐ anti ‐diol monoesters which have been obtained through a zirconium‐catalyzed aldol‐Tishchenko reaction. The product 1,3‐ anti ‐diol diesters were formed in yields close to 50 % and >98 % ee . Separation from the unreactive enantiomers and subsequent hydrolysis furnished both enantiomers of unsymmetrically substituted 1,3‐ anti ‐diols in high optical purities. Alternatively, the kinetic resolution process can be performed on the free 1,3‐ anti ‐diols even more rapidly with equally good results. A slow acyl migration during the reaction slightly deteriorated the enantiomeric excess of the unreactive enantiomers. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2007)