An enantioselective esterification process was developed for the synthesis of 2-N-morpholinoethyl (S)-ibuprofen ester prodrug from racemic ibuprofen by using Candida rugosa lipase immobilized on Accurel MP1000 in cyclohexane. Compared with the performance of Lipase MY, the immobilized lipase possesses a higher enzyme activity and thermal stability, but with a slightly suppressed enantioselectivity. A kinetic model was proposed and confirmed from experiments, for the simulation of time-course conversions of both enantiomers at various combinations of substrate concentrations in a batch reactor. Preliminary results of employing the proposed model and the immobilized lipase in a continuous packed-bed reactor were also reported and discussed.