Enzymatic Enantioselective Hydrolysis of 2-(3-Chlorophenyl) Propionic Acid Ester Enhanced by PEG: Experiment and Optimization

Chiral resolution of 2-(3-chlorophenyl) propionic acid (CPA) via the hydrolysis of CPA ester catalyzed by lipase PS from Pseudomonas cepacia is reported. With polyethylene glycol (PEG 400) as a cosolvent, the substrate conversion is increased by 88% with high enantioselectivity. Important factors including lipase type, substrate structure, cosolvent, temperature, pH, enzyme loading, PEG 400 and substrate concentrations, and reaction time were investigated, and the optimal conditions including 15 mg mL–1 lipase PS, 20 mmol L–1 substrate, 30% (m/m) PEG 400, reaction for 36 h at 70 °C and pH 6.5 were obtained, where the enantiomeric excess and overall conversion rate could reach up to 99.02% and 42.09%, respectively. An uncompetitive inhibition kinetic model was applied to simulate the reaction process, and the model predictions are in good agreement with the experimental data, which is important for a deep understanding of the reaction mechanism, and then for process design and operation.