The hydrolytic resolution of (R,S)-2,2,2-trifluoroethyl alpha-chlorophenylacetate in water-saturated isooctane containing Lipase MY(I) at 35 degrees C is selected as the best reaction condition for producing (R)-alpha-chlorophenyl acetic acid. The kinetic constants, and hence an enantiomeric ratio of 33.6, are estimated and employed for the modeling of time-course conversions of both substrates by considering product inhibition and enzyme deactivation effects. A successful dynamic kinetic resolution is also achieved, giving the desired (R)-alpha-chlorophenylacetic acid of 93.0% yield and ee(P) = 89.5% when 80 mmol dm(-3) trioctylamine acting as the racemization catalyst and enzyme activator is initially added. (c) 2006 Society of Chemical Industry.