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Kinetic study on enantioselective resolution of ( R,S )‐2‐phenylpropionic acid through Novozyme 435–catalyzed esterification
Author(s) -
Yuan Xin,
Zhang Panliang,
Xu Weifeng,
Tang Kewen
Publication year - 2019
Publication title -
international journal of chemical kinetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.341
H-Index - 68
eISSN - 1097-4601
pISSN - 0538-8066
DOI - 10.1002/kin.21274
Subject(s) - chemistry , kinetic resolution , catalysis , substrate (aquarium) , enantiomeric excess , enantioselective synthesis , enzyme , kinetic energy , enantiomer , enzyme catalysis , aryl , hexane , organic chemistry , stereochemistry , medicinal chemistry , oceanography , physics , alkyl , quantum mechanics , geology
2‐Phenylpropionic acid (2‐PPA) is a very important chiral intermediate in the synthesis of aryl propionic acid drugs with anti‐inflammatory and analgesic effects. Enzymatic kinetic resolution of ( R,S )‐2‐PPA using n ‐hexanol as an acyl donor was carried out in n ‐hexane. Lipases from different sources were used to catalyze the esterification of 2‐PPA, among which Novozyme 435 had the highest catalytic efficiency. The effects of reaction conditions on conversion (c) and enantiomeric excess (ee), involving temperature, substrate concentrations, enzyme loading, and reaction time were investigated. The kinetic model based on the Ping‐Pong bi‐bi mechanism was established to simulate the enzymatic esterification process. The experimental values of initial rates of various 2‐PPA concentrations were consistent with the simulated values.