Kinetics on the Optical Resolution of 2-Octanol in Tributyrylglycerolby Lipase-Catalyzed Transesterification

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  • HIRATA Hirofumi
    Department of Bioscience and Technology, School of Engineering, Hokkaido Tokai University
  • MAYAMA Motomi
    Department of Bioscience and Technology, School of Engineering, Hokkaido Tokai University
  • INADA Nobuyuki
    Department of Bioscience and Technology, School of Engineering, Hokkaido Tokai University
  • YAMADA Kazunori
    Department of Bioscience and Technology, School of Engineering, Hokkaido Tokai University
  • YANAGISHITA Hiroshi
    National Institute of Materials and Chemical Research
  • SUGIURA Masaaki
    National Institute of Materials and Chemical Research

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Other Title
  • トリブチリルグリセリン中におけるリパーゼを用いたエステル交換による2-オクタノールの光学分割の動力学
  • トリブチリルグリセリンチュウ ニ オケル リパーゼ オ モチイタ エステル コ

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Abstract

Lipase-catalyzed transesterification between tributyrylglycerol (tributyrin) (1) and 2-octanol (2) has been studied in neat at 30°C. The kinetic resolution data fit the reported theoretical equations for the equilibrium reaction. The competitive reactions of the enantiomers in (2) with theacyl-enzyme intermediate which was formed the reaction of the free enzyme and (1) was experimentally proved by an accordance of the enantiomeric excess against the extent of conversion plots for racemic and optically active (2). A reversibility of the transesterification was also shownby a decrease in enantiomeric excess of the product and the unreacted starting material duringthe reaction.

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