)-2-(4-methylphenyl) propionic acid (MPPA) enantiomers by enzymatic esterification in organic solvent. Novozym 435 (CALB) has the best catalytic performance compared with other lipases. Of the alcohols screened
n
-hexanol is the best acyl acceptor and gives the highest enzyme activity and enantioselectivity in
n
-hexane. Response surface methodology (RSM) was used to evaluate the influence of the factors
such as temperature
enzyme amount
substrate concentration and reaction time on the substrate conversion (
c
) and enantiomeric excess (ee). The correlation coefficient
R
2
for enantiomeric excess and the conversion are 0.9827 and 0.9910
respectively
indicating that can accurately predict the experimental results. By simulation and optimization
the optimal conditions were obtained
involving 600 mmol·L
-1
MPPA concentration (0.60 mmol)
850 mmol·L
-1
hexanol concentration (0.85 mmol)
58 mg enzyme amount
75 ℃ temperature and 4.5 h reaction time
respectively. Under the optimized conditions
the experimental values of conversi
on and enantiomeric excess were 89.34% and 97.84%
respectively
which are in good agreement with the model predictions.
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