Kinetic resolution of PPA enantiomers through enzymatic hydrolysis of racemic PPA ester was performed in an aqueous system. A reaction system was constructed by investigating the effects of reaction conditions including lipase type, substrate structure, temperature and pH. On the basis of interfacial reaction mechanism, a mathematical model was developed and the kinetic parameters were estimated by fitting the data to the model. By simulation and optimization, the optimum conditions were obtained as follows: 20 mg mL(-1) lipase PS, 30 mmol L-1 substrate, reaction for 26 hat 55 degrees C and pH of 6.0, under which the enantiomeric excess and conversion of (R)-enantiomer could reach up to 99.59% and 91.12% with the relative errors of 1.2% and 0.010% compared with the model predictions, respectively. The model predictions are in good agreement with the experimental data, which provides a powerful tool for process optimization of enantioselective hydrolysis. (C) 2019 Institution of Chemical Engineers. Published by Elsevier B.V. All rights reserved.