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Lipase‐catalyzed hydrolysis of (+,‐)‐2‐(4‐methylphenyl) propionic methyl ester enhanced by hydroxypropyl‐β‐cyclodextrin

Liu, Guangyong, Zhang, Panliang, Xu, Weifeng, Wang, Lujun, Tang, Kewen
Journal of chemical technology and biotechnology 2019 v.94 no.1 pp. 147-158
Candida rugosa, agitation, carboxylic ester hydrolases, catalytic activity, enantioselectivity, hydrolysis, models, pH, propionic acid, response surface methodology, temperature
BACKGROUND: Enzymatic kinetic resolution is an attractive technology for production of enantiomerically pure compounds. The objective of this research is to investigate the enantioselective hydrolysis of (+,‐)‐2‐(4‐methylphenyl) propionic methyl ester (2‐(4‐MP)PPAME) to (+)‐2‐(4‐methylphenyl) propionic acid ((+)‐2‐(4‐MP)PPA) catalyzed by enzyme in an aqueous medium. RESULTS: Lipase AY from candida rugosa (CRL) was screened as the best lipase. Novozym 435 IM and lipopan S BG show higher catalytic activity but the enantioselectivity is very low. By addition of hydroxypropyl‐β‐cyclodextrin (HP‐β‐CD) to the aqueous system, an increased substrate conversion of 45.28% was obtained, the high enantiomeric excess remaining compared with the conversion of 28.05% without HP‐β‐CD. Response surface methodology and central composite design were employed to model and optimize the reaction system. CONCLUSION: Under the optimal conditions including pH of 6.60, 12.5 mg mL⁻¹ enzyme, 35 mmol L⁻¹ HP‐β‐CD, 0.06 mmol substrate, temperature 39°C, agitation speed 400 rpm and 40 h reaction time, the substrate conversion was up to 40.32% and the optical purity of the product (+)‐2‐(4‐methylphenyl) propionic acid was up to 95.22%. © 2018 Society of Chemical Industry