The Brønsted exponents for the alkaline hydrolysis of alkyl esters are 1.3 and 0.4 for substitution in the acyl and alcohol portions, respectively, which is indicative of a transition state which resembles the anionic tetrahedral intermediate with a localised negative charge. By contrast, the rate of the pig liver esterase (PLE)-catalysed hydrolysis shows little dependence upon the electron-withdrawing power of substituents. The values of k_cat are independent of the pK_a of the leaving group alcohol suggesting rate-limiting deacylation. There is a small steric effect of α-substitution in both the alcohol and carboxylic acid residues for the enzyme-catalysed reactions but the enzyme rate enhancement factor remains high for most esters. There is no substantial ee observed for the hydrolysis of racemic esters although the kinetic data can be used for determining the regioselective hydrolysis of diesters. Unsubstituted lactones are poor substrates for PLE but derivatives with hydrophobic substituents show k_cat/K_m values similar to those for acyclic esters. Dihydrocoumarin undergoes transesterification catalysed by PLE, k_cat increases with increasing alcohol concentration indicative of rate-limiting deacylation. There is enantioselectivity in the PLE-catalysed hydrolysis of some racemic lactones but little or none in the transesterification of racemic alcohols with dihydrocoumarin.