The Candida cylindracea lipase catalyzed enantioselective esterification of 2-chloropropionic acid was studied in different solvents with constant initial water content in the reaction mixture. The effect of solvents and solvent mixtures with different hydrophobicity (e.g. log P value) on the activity and enantioselectivity of the enzyme was investigated. The log P values showed a linear correlation with the initial reaction rate as well as with the enantioselectivity. The rate increased while the enantioselectivity slightly decreased with increasing log P values. In solvent mixtures the activity of the enzyme was generally determined by the solvent with the lowest hydrophobicity while the correlation between the average log P value and the enantioselectivity was linear.