Abstract
AbstractThe catalytic activity of bovine serum albumin (BSA) modified physically 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 the type of Michaelis‐Menten reaction in ethyl acetate solution. The enzymatic activity of Imp‐BSA was competitively inhibited by (4R,4S)‐4‐hydroxy‐4‐(4‐nitrophenyl)butan‐2‐one (4).
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