The activity and the regio- and enantioselectivity of five lipases and one protease were investigated in the two enantiomeric solvents (R)-carvone and (S)-carvone. It was found that in all cases enzyme activity changed as a function of solvent configuration and that, for the same enzyme, it was higher in (R)-carvone or in (S)-carvone depending on the nature of the substrate. Instead, no significative variation of regio- and enantioselectivity was observed moving from one enantiomeric solvent to the other.