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

Voutsas, E. C./ Stamatis, H./ Kolisis, F. N./ Tassios, D.

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.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών
Keywords: enzymes,esterification,solvent,unifac,substrate-specificity,kinetic-parameters,ester hydrolysis,systems,media,biocatalysis,coefficients,enzymes,model
ISSN: 1024-2422
Link: <Go to ISI>://000176147700003
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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