Solvent effects on equilibrium position and initial rate of lipase-catalyzed esterification reactions in organic solvents: Experimental results and prediction capabilities

Voutsas, EC; Stamatis, H; Kolisis, FN; Tassios, D

dc.contributor.author	Voutsas, EC	en
dc.contributor.author	Stamatis, H	en
dc.contributor.author	Kolisis, FN	en
dc.contributor.author	Tassios, D	en
dc.date.accessioned	2014-03-01T01:18:21Z
dc.date.available	2014-03-01T01:18:21Z
dc.date.issued	2002	en
dc.identifier.issn	1024-2422	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/14952
dc.subject	Enzymes	en
dc.subject	Esterification	en
dc.subject	Solvent	en
dc.subject	UNIFAC	en
dc.subject.classification	Biochemistry & Molecular Biology	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	Alcohols	en
dc.subject.other	Catalysis	en
dc.subject.other	Enzymes	en
dc.subject.other	Esterification	en
dc.subject.other	Organic solvents	en
dc.subject.other	Rate constants	en
dc.subject.other	Solubility	en
dc.subject.other	Enzymatic reactions	en
dc.subject.other	Polar solvents	en
dc.subject.other	Catalyst activity	en
dc.subject.other	acetic acid	en
dc.subject.other	hexanol	en
dc.subject.other	octanol	en
dc.subject.other	organic solvent	en
dc.subject.other	triacylglycerol lipase	en
dc.subject.other	water	en
dc.subject.other	accuracy	en
dc.subject.other	article	en
dc.subject.other	catalysis	en
dc.subject.other	controlled study	en
dc.subject.other	correlation analysis	en
dc.subject.other	enzyme mechanism	en
dc.subject.other	equilibrium constant	en
dc.subject.other	esterification	en
dc.subject.other	experimentation	en
dc.subject.other	methodology	en
dc.subject.other	model	en
dc.subject.other	partition coefficient	en
dc.subject.other	polarization	en
dc.subject.other	prediction	en
dc.subject.other	solubility	en
dc.subject.other	solvent effect	en
dc.title	Solvent effects on equilibrium position and initial rate of lipase-catalyzed esterification reactions in organic solvents: Experimental results and prediction capabilities	en
heal.type	journalArticle	en
heal.identifier.primary	10.1080/10242420290018087	en
heal.identifier.secondary	http://dx.doi.org/10.1080/10242420290018087	en
heal.language	English	en
heal.publicationDate	2002	en
heal.abstract	The solvent effect on the equilibrium position and the initial rate of esterification of 1-hexanol with acetic acid catalyzed by a lipase has been experimentally investigated. A variety of non-polar and polar solvents have been considered and the results obtained indicate that the solvent effect on the equilibrium conversion is very important compared to that for transesterification reactions. A theoretically sound methodology using the group-contribution UNIFAC model for the prediction of solvent effects on the equilibrium position of enzymatic reactions is presented and it is applied to the reaction of 1-hexanol with acetic acid as well as to a similar reaction from the literature. The results obtained are better than those from empirical methods proposed in the literature such as correlations with the octanol-water partition coefficient of the solvent, as well as the solubility of water in the solvent. Moreover, the proposed methodology can be used for the determination of the equilibrium constant of the reaction. For the prediction of the solvent effect on the initial rate of enzymatic reactions it is found that it is more accurately determined using the product of the activities of the reactants, which can be predicted by the UNIFAC model, than the octanol-water partition coefficient of the solvent or the solubility of water in the solvent.	en
heal.publisher	TAYLOR & FRANCIS LTD	en
heal.journalName	Biocatalysis and Biotransformation	en
dc.identifier.doi	10.1080/10242420290018087	en
dc.identifier.isi	ISI:000176147700003	en
dc.identifier.volume	20	en
dc.identifier.issue	2	en
dc.identifier.spage	101	en
dc.identifier.epage	109	en