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Abstract: alpha-Chymotrypsin exhibits photoswitchable activities in an organic solvent after covalent modification of the protein backbone with thiophenefulgide active ester (2). The thiophenefulgide-modified alpha-chymotrypsin exhibits reversible photoisomerizable properties between states (3)-E and (3)-C. The modified alpha-chymotrypsin, where nine lysine residues are substituted by thiophenefulgide units, retains 60% of the activity of the native enzyme. The activities of thiophenefulgide-modified alpha-chymotrypsin toward esterification of N-acetyl-L-phenylalanine (4) by ethanol in cyclohexane are controlled by the configuration of the attached photoisomerizable component and by prior bioimprinting of the protein backbone with the reaction substrate (4). The esterification of(4) in cyclohexane using bioimprinted (3)-C is two-fold faster than in the presence of(3)-E. In the presence of a nonbioimprinted enzyme, esterification of(4) by (3)-C is five-fold faster than with (3)-E. The activity of bioimprinted (3)-E toward esterification of(4) is 4.5-fold higher than that of nonbioimprinted (3)-E. Switchable cyclic esterification of(4) is accomplished by sequential photoisomerization of the thiophenefulgide-modified alpha-chymotrypsin between states (3)-C and (3)-E