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KINETIC-STUDY OF LIPASE-CATALYZED ESTERIFICATION REACTIONS IN WATER-IN-OIL MICROEMULSIONS

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dc.contributor.author STAMATIS, H en
dc.contributor.author XENAKIS, A en
dc.contributor.author MENGE, U en
dc.contributor.author KOLISIS, FN en
dc.date.accessioned 2014-03-01T01:09:26Z
dc.date.available 2014-03-01T01:09:26Z
dc.date.issued 1993 en
dc.identifier.issn 0006-3592 en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/10980
dc.subject LIPASE en
dc.subject MICROEMULSIONS en
dc.subject REVERSE MICELLES en
dc.subject ESTERIFICATION en
dc.subject KINETICS en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.other REVERSE MICELLES en
dc.subject.other ORGANIC-SOLVENTS en
dc.subject.other FATTY-ACIDS en
dc.subject.other ENZYMES en
dc.subject.other SURFACTANTS en
dc.subject.other ENZYMOLOGY en
dc.subject.other SYSTEMS en
dc.subject.other STATE en
dc.title KINETIC-STUDY OF LIPASE-CATALYZED ESTERIFICATION REACTIONS IN WATER-IN-OIL MICROEMULSIONS en
heal.type journalArticle en
heal.identifier.primary 10.1002/bit.260420803 en
heal.identifier.secondary http://dx.doi.org/10.1002/bit.260420803 en
heal.language English en
heal.publicationDate 1993 en
heal.abstract 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 Bi-Bi 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., Vermue, 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) = [H2O]/[AOT], of the reverse micelles, were in accordance with the theoretically predicted pattern. (C) 1993 John Wiley & Sons, Inc. en
heal.publisher JOHN WILEY & SONS INC en
heal.journalName BIOTECHNOLOGY AND BIOENGINEERING en
dc.identifier.doi 10.1002/bit.260420803 en
dc.identifier.isi ISI:A1993LY46900002 en
dc.identifier.volume 42 en
dc.identifier.issue 8 en
dc.identifier.spage 931 en
dc.identifier.epage 937 en


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