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Removal of water produced from lipase‐catalyzed esterification in organic solvent by pervaporation
Author(s) -
Kwon Seok Joon,
Song Kyu Min,
Hong Won Hi,
Rhee Joon Shick
Publication year - 1995
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.260460413
Subject(s) - pervaporation , chemistry , lipase , butanol , catalysis , organic chemistry , solvent , cellulose , triacylglycerol lipase , membrane , water activity , oleic acid , chromatography , ethanol , enzyme , water content , biochemistry , permeation , geotechnical engineering , engineering
Esterification of oleic acid with n ‐butanol in the presence of Lipozyme® was carried out at 25°C in isooctane with various initial water activities. Initial reaction rate as well as equilibrium conversion decreased at high initial water activity. Therefore, removal of water present in the reaction mixtures was essential. A pervaporation process was applied to the lipase‐catalyzed synthesis of n ‐butyloleate to remove water. Pervaporation selectively separated water from the reaction mixture using a nonporous polymeric membrane, cellulose acetate. Therefore, pervaporation is potentially applicable to remove the water produced from various enzymatic processes, such as synthesis of various esters, peptides, and glycosides in a solvent system as well as in a solvent‐free system. © 1995 John Wiley & Sons, Inc.