Publisher Summary The ability of enzymes to catalyze enantioselective and enantiospecific reactions is evident from the large variety of enantiomerically pure natural products. Their potential as catalysts for asymmetric synthesis and racemate resolution in organic synthetic applications has obtained much attention. The majority of enzymes presently used for this purpose belong to the class of hydrolases, comprising lipases, esterases, and proteases. The stereochemical features of hydrolases can be utilized both in hydrolytic and in condensation reactions. Replacing bulk water with organic solvents has been reported to affect enzymes in various ways. Changes of stability, activity, and selectivity have been observed. This chapter presents solvent effects of practical importance for the application of lipases in racemate resolutions. Thermodynamic effects of the solvent become clear when thermodynamic activities are introduced as the mass action equivalents of the concentrations of all species involved in regular rate equations. Rationalization for this choice has been given elsewhere. Also, in this case, representation of rate equations in terms of thermodynamic activities narrows the range of α-selectivities observed in the solvents studied, emphasizing the intrinsic value of this parameter.
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