Kinetic Studies on Lipase-Catalyzed Acetylation of 1-Alkanol with Vinyl Acetate in Organic Solvent
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- HIRATA Hirofumi
- Department of Bioscience and Technology, School of Engineering, Hokkaido Tokai University
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- KONDO Gen
- Department of Bioscience and Technology, School of Engineering, Hokkaido Tokai University
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- KAWAUCHI Keiyo
- Department of Bioscience and Technology, School of Engineering, Hokkaido Tokai University
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- CHEN Yun-Gang
- Division of Core Studies, School of Engineering, Hokkaido Tokai University
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- SAKAKI Keiji
- AIST Tsukuba Central 5, National Institute of Advanced Industrial Science and Technology
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- YANAGISHITA Hiroshi
- AIST Tsukuba Central 5, National Institute of Advanced Industrial Science and Technology
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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.<br>
Journal
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- Journal of Oleo Science
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Journal of Oleo Science 55 (5), 239-248, 2006
Japan Oil Chemists' Society
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Details 詳細情報について
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- CRID
- 1390282679069711488
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- NII Article ID
- 130000055565
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- NII Book ID
- AA11503337
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- ISSN
- 13473352
- 13458957
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- NDL BIB ID
- 7883762
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed