ENANTIOSELECTIVITY OF SOME LIPASES - CONTROL AND PREDICTION

Different strategies for the resolution of racemates in lipase catalyzed hydrolyses, esterifications, and transesterifications are presented. The importance of the equilibrium conversion for the optimization of the enantiomeric excess is emphasized. Investigations have been carried out on esters of 1-phenylethanol and 2-methylalkanoic acids. Results are presented, which provide general information about important parameters for the enhancement of the enantiomeric excess and the reaction rates. The application of a 'matched strategy' stereochemical control for increasing the enantiomeric excess is presented, i.e. the use of a chiral acid for the resolution of chiral alcohols. Molecular modelling of lipase from Rhizomucor miehei as well as the use of a simple active site model of lipase from Candida cylindracea to obtain information for the prediction and modification of enzyme specificity is presented.