RECRUITMENT OF ENZYME-ACTIVITY IN ALBUMIN BY MOLECULAR IMPRINTING

The catalytic activity of bovine serum albumin (BSA) modified physical ly by molecular imprinting using transition-state analogue (TSA) as a template molecule was studied. The resultant imprinted serum albumin ( Imp-BSA) showed the rate acceleration of dehydrofluorination reaction from (4R,4S)-4-fluoro-4-(4-nitrophenyl)butan-2-one (1) and followed th e type of Michaelis-Menten reaction in ethyl acetate solution. The enz ymatic activity of Imp-BSA was competitively inhibited by (4R,4S)-4-hy droxy-4-(4-nitrophenyl)butan-2-one (4).