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Lipase‐catalyzed dynamic kinetic resolution of ( R , S )‐fenoprofen thioester in isooctane
Author(s) -
Chen ChiaYin,
Cheng YuChi,
Tsai ShauWei
Publication year - 2002
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.625
Subject(s) - thioester , racemization , lipase , chemistry , kinetic resolution , catalysis , hydrolysis , enantioselective synthesis , substrate (aquarium) , organic chemistry , enzyme catalysis , enzyme , oceanography , geology
A lipase‐catalyzed enantioselective hydrolysis process under in situ racemization of the remaining ( R )‐thioetser substrate with trioctylamine as the catalyst was developed for the production of ( S )‐fenoprofen from ( R,S )‐fenoprofen 2,2,2‐trifluoroethyl thioester in isooctane. Detailed investigations of trioctylamine concentration on the enzyme activation and the kinetic behavior of the thioester in racemization and enzymatic reactions were conducted, in which good agreement between the experimental data and theoretical results was observed. © 2002 Society of Chemical Industry