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Lipase‐catalyzed dynamic resolution of naproxen 2,2,2‐trifluoroethyl thioester by hydrolysis in isooctane
Author(s) -
Chang ChunSheng,
Tsai ShauWei,
Kuo Jimmy
Publication year - 1999
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19990705)64:1<120::aid-bit13>3.0.co;2-a
Subject(s) - naproxen , racemization , thioester , chemistry , lipase , hydrolysis , enantioselective synthesis , substrate (aquarium) , organic chemistry , kinetic resolution , yield (engineering) , catalysis , stereochemistry , enzyme , medicine , oceanography , alternative medicine , materials science , geology , pathology , metallurgy
A lipase‐catalyzed enantioselective hydrolysis process under continuous in situ racemization of substrate by using trioctylamine as an organic base was developed for the production of (S)‐naproxen from racemic naproxen thioesters in isooctane. Naproxen 2,2,2‐trifluoroethyl thioester and 45°C were selected as the best substrate and temperature, respectively, by comparing the time‐course variations for the racemization of (S)‐naproxen thioesters containing an electron‐withdrawing group. A detailed investigation of the effect of trioctylamine concentration on the kinetic behaviors of the thioester in racemization and enzymatic reaction was conducted, in which more than 70% conversion of the racemate (or 67.2% yield of (S)‐naproxen) with ee p value higher than 92% was obtained. © 1999 John Wiley & Sons, Inc. Biotechnol Bioeng 64: 120–126, 1999.