This paper reports on the resolution of (

R

S

)-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.