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Kinetic study of lipase catalyzed esterification reactions in water‐in‐oil microemulsions
Author(s) -
Stamatis Haralambos,
Xenakis Aristotelis,
Menge Ulrich,
Kolisis Fragiskos N.
Publication year - 1993
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.260420803
Subject(s) - microemulsion , chemistry , lipase , lauric acid , micelle , kinetics , catalysis , kinetic energy , water activity , enzyme kinetics , menthol , sodium , organic chemistry , chromatography , enzyme , pulmonary surfactant , active site , fatty acid , biochemistry , water content , physics , geotechnical engineering , quantum mechanics , aqueous solution , engineering
The kinetics of the esterification of lauric acid by (‐)menthol, catalyzed by Penicillium simplicissimum lipase, was studied in water/bis‐(2‐ethylhexyl)sulfosuccinate sodium salt (AOT)/isooctane microemulsions. Due to their low water content, microemulsions assist in reversing the direction of lipase activity, favoring synthetic reactions. The kinetics of this synthesis follows a Ping‐Pong BiBi mechanism. The values of all apparent kinetic parameters were determined. The theoretical model for the expression of enzymic activity in reverse micelles, proposed by Verhaert et al. (Verhaert, R., Hilhorst, R., Vermüe, M., Schaafsma, T. J., Veeger, C. 1990. Eur. J. Biochem. 187: 59–72) was extended to express the lipase activity in an esterification reaction involving two hydrophobic substrates in microemulsion systems. The model takes into account the partitioning of the substrates between the various phases and allows the calculation of the intrinsic kinetic constants. The experimental results showing the dependence of the initial velocity on the hydration ratio, W o = [H 2 O]/[AOT], of the reverse micelles, were in accordance with the theoretically predicted pattern. © 1993 John Wiley & Sons, Inc.