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Simulation and optimization of Novozym 40086 kinetic resolution of α‐cyclopentylphenylacetic acid enantiomers
Author(s) -
Zhang Panliang,
Cheng Qing,
Xu Weifeng,
Tang Kewen
Publication year - 2019
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.6163
Subject(s) - enantiomer , chemistry , kinetic resolution , hydrolysis , resolution (logic) , aqueous solution , substrate (aquarium) , peg ratio , kinetic energy , solubility , phase (matter) , aqueous two phase system , enantioselective synthesis , chromatography , catalysis , organic chemistry , physics , quantum mechanics , artificial intelligence , computer science , oceanography , finance , geology , economics
BACKGROUND Enzymatic resolution of enantiomers by hydrolysis is a popular method, yet most enantiomers have low solubility in the aqueous phase, resulting in low conversion. Notwithstanding this, the simulation and optimization of the reaction process by modelling has been reported only rarely. Thus, PEG was added to the aqueous phase and a mathematical model was established to obtain optimal conditions. RESULTS The effects of various parameters were investigated to build an optimized reaction system. The results indicated that temperature and pH had little effect on enantiomeric excess, but they had significant effect on conversion. Conversion was enhanced by 85% with the addition of PEG 400. Kinetic studies showed that pentanol competitively inhibited enzyme activity. A mathematical model was developed, and forward and reverse reactions were taken into consideration. Through simulation and optimization of model, the optimum conditions were obtained as follows: 10 mg mL −1 Novozym 40086, 10 mmol L −1 substrate, 30% PEG 400, temperature 45 °C, pH 6.5 and reaction time 36 h. CONCLUSION Chiral resolution of α‐cyclopentylphenylacetic acid enantiomer (CPPA) was achieved by Novozym 40086 enantioselective hydrolysis of the CPPA ester. Under optimum conditions, ee p and c s were 95.83% and 88.52%, respectively. The relative errors between predicted values and experimental values were <5%, confirming that the model could accurately predict the enzymatic resolution reaction. © 2019 Society of Chemical Industry