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Integration of reactive membrane extraction with lipase‐hydrolysis dynamic kinetic resolution of naproxen 2,2,2‐trifluoroethyl thioester in isooctane
Author(s) -
Lu ChuHsun,
Cheng YuChi,
Tsai ShauWei
Publication year - 2002
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/bit.10274
Subject(s) - naproxen , chemistry , racemization , hydrolysis , thioester , lipase , kinetic resolution , chromatography , organic chemistry , oxazoline , product inhibition , hollow fiber membrane , enantioselective synthesis , fiber , catalysis , enzyme , medicine , alternative medicine , non competitive inhibition , pathology
Lipases immobilized on polypropylene powders have been used as the biocatalyst in the enantioselective hydrolysis of (S)‐naproxen from racemic naproxen thioesters in isooctane, in which trioctylamine was added to perform in situ racemization of the remaining (R)‐thioester substrate. A detailed study of the kinetics for hydrolysis and racemization indicates that increasing the trioctylamine concentration can activate and stabilize the lipase as well as enhance the racemization and non‐stereoselective hydrolysis of the thioester. Effects of the aqueous pH value and trioctylamine concentration on (S)‐naproxen dissociation and partitioning in the aqueous phase as well as the transportation in a hollow fiber membrane were further investigated. Good agreements between the experimental data and theoretical results were obtained when the dynamic kinetic resolution process was integrated with a hollow fiber membrane to reactively extract the desired (S)‐naproxen out of the reaction medium. © 2002 Wiley Periodicals, Inc. Biotechnol Bioeng 79: 200–210, 2002.