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Dynamic enzymatic resolution of Naproxen methyl ester in a membrane bioreactor
Author(s) -
Xin Jiaying,
Li Shuben,
Xu Yi,
Chui Junru,
Xia Chungu
Publication year - 2001
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.413
Subject(s) - racemization , chemistry , lipase , membrane reactor , kinetic resolution , substrate (aquarium) , organic chemistry , candida rugosa , product inhibition , naproxen , catalysis , hydrolysis , triacylglycerol lipase , chromatography , emulsion , bioreactor , enantioselective synthesis , enzyme , medicine , oceanography , non competitive inhibition , alternative medicine , pathology , geology
A lipase‐catalyzed enantioselective continuous hydrolysis process under in situ racemization of substrate using sodium hydroxide as catalyst was developed for the production of (S) ‐Naproxen from racemic Naproxen methyl ester in an aqueous–organic biphase system. Use of a tubular silicone rubber membrane in the stirred tank reactor to separate the chemical catalytic racemization and biocatalytic resolution processes, served to avoid the key problem associated with conventional dynamic resolution, viz the incompatibility of in situ chemical racemization with the presence of a biocatalyst. To overcome product inhibition and to facilitate product recovery from the aqueous–organic emulsion containing substrate and lipase, a hydrophilic porous semipermeable membrane was used in the stirred tank reactor. Greater than 60% conversion of the racemate with an enantiomeric excess of product (ee p ) greater than 96% was obtained. In addition, transformation of Candida rugosa lipase (CRL) isoenzymes was observed in the reaction process. © 2001 Society of Chemical Industry