Journal of Oleo Science
Online ISSN : 1347-3352
Print ISSN : 1345-8957
ISSN-L : 1345-8957
Biochemistry and Biotechnology
Kinetic Studies on Lipase-Catalyzed Acetylation of 1-Alkanol with Vinyl Acetate in Organic Solvent
Hirofumi HIRATAGen KONDOKeiyo KAWAUCHIYun-Gang CHENKeiji SAKAKIHiroshi YANAGISHITA
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2006 Volume 55 Issue 5 Pages 239-248

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Abstract

Lipase-catalyzed acetylation of 1-alkanol with vinyl acetate to give alkyl acetate has been studied kinetically using Burkholderia cepacia lipase, six alcohols and different organic solvents. The rate constants kA and kB with respect to vinyl acetate and 1-alkanol determined from the double reciprocal plots, v-1 vs. [vinyl acetate]-1 and v-1 vs. [1-alkanol]-1 respectively, where v is the initial rate of the reaction. The rate ratio kB/kA was larger than unity except some cases: the rate in acetylation of active serine residue in the lipase with vinyl acetate was slower than that of 1-alkanol with the acetyl-enzyme intermediate. The rate constant kA was independent of the solvent hydrophobicity log P (where P is a partition coefficient of a given solvent between octanol and water), however, kB increased with log P. Both rate constants were different depending on the structure (carbon number CN) of 1-alkanol.

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© 2006 by Japan Oil Chemists' Society
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