Catalytic properties of cross-linked enzyme crystals in organic media

The activity and the enantioselectivity of cross-linked enzyme crystals (CLECs) of subtilisin in the transesterification between N-acetyl-l-phenylalanine ethyl ester and n-propanol have been examined in various organic solvents. The activity of CLECs of subtilisin in decane was 780 times greater than that in triethylamine. CLECs of subtilisin preferred l-enantiomer in the transesterification between N-acetyl-phenylalanine ethyl ester and n-propanol, and the (kcat/KM)L/(kcat/KM)D ratio was 20 000 in cyclohexane.