Reversible activity control of enzymatic reactions in supercritical fluid-enantioselective esterification catalyzed by a lipid-coated lipase in supercritical fluoroform

T. Mori, M. Funasaki, A. Kobayashi, Y. Okahata

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

Abstract

The lipid-coated lipase is soluble and can catalyze esterification enantioselectively in supercritical fluoroform (scCHF3). as well as organic solvents. In organic media, the lipid-coated lipase became inactive in polar solvents due to denaturation of enzymes. One of the features of supercritical fluid is that physical properties such as polarity or dielectric constant could be reversibly controlled by changing pressure or temperature of scCHF3. When the lipid-coated lipase was employed in scCHF3 by changing pressure or temperature, the reaction rate could be regulated and the conversion was kept constant in high yields. Thus, the enzyme activity could switch on and off by adjusting pressure or temperature of scCHF3. We believe that the combination of the lipid-coated enzyme and scCHF3 as reaction media will become a new system as biotransformation studies.

Original languageEnglish
Pages (from-to)564-568
Number of pages5
JournalKOBUNSHI RONBUNSHU
Volume58
Issue number10
DOIs
Publication statusPublished - 2001

Keywords

  • Dielectric constant
  • Enantioselective estirification
  • Lipid-coated enzyme
  • Organic solvents
  • Supercritical fluoroform

ASJC Scopus subject areas

  • Chemical Engineering (miscellaneous)
  • Materials Science (miscellaneous)
  • Environmental Science(all)
  • Polymers and Plastics

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