ENHANCING ENANTIOSELECTIVITY OF A LIPID-COATED LIPASE VIA IMPRINTING METHODS FOR ESTERIFICATION IN ORGANIC-SOLVENTS

Lipase OF from Candida showed only low enantioselectivity for esterifi cation of (R)- or S-1-phenylethanol with lauric acid (v(R)/v(S) = 5.5) . However, when lipase OF was imprinted with a substrate analogue such as (R)-1-phenylethanol and then coated with synthetic glycolipid mole cules, the imprinted lipid-coated lipase shows a large enantioselectiv ity for the esterification in anhydrous isooctane (v(R)/v(S) = 77). Wh en the native lipase OF was imprinted by the same procedure, the enant ioselectivity hardly changed. The lipid coating was important to keep the imprinted structure as well as to solubilize enzymes in organic so lvents. The improved enantioselectivity was confirmed from Michaelis-M enten kinetics as due to the intramolecular catalytic reaction and not the; substrate binding process. The improved enantioselectivity rever ts to the original non-imprinted value if kept in the organic solvents at high temperatures for days.