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

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.