Summary
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.
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Ottolina, G., Bovara, R., Riva, S. et al. Activity and selectivity of some hydrolases in enantiomeric solvents. Biotechnol Lett 16, 923–928 (1994). https://doi.org/10.1007/BF00128626
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DOI: https://doi.org/10.1007/BF00128626