초록
<P>Stereoselective resolution of (<I>R</I>,<I>S</I>)-carprofen methyl ester (CPOMe) by lipase-catalyzed hydrolysis to (<I>S</I>)-carprofen (CP) was investigated in an aqueous medium. With the highest catalytic activity, <I>Candida antarctica</I> Lipase A (CALA) was selected as catalyst compared with eight other lipases. Hydroxyethyl-β-cyclodextrin (HE-β-CD) was added to enhance the solubility of (<I>R</I>,<I>S</I>)-CPOMe, which significantly raised the conversion of substrate from 11.12% to 30.84%. Response surface methodology (RSM) was adopted to evaluate the influence of factors on the substrate conversion (<I>c</I>) and enantiomeric excess of product (ee<SUB>p</SUB>), such as pH, concentrations of enzyme and HE-β-CD, temperature, substrate loading, and reaction time. The optimal conditions were obtained, including pH 6.0, 40 mg/mL CALA, 0.05 mmol substrate, 35 mmol/L HE-β-CD, agitation speed of 600 rpm, temperature of 76 °C, and reaction time of 30 h. Under the above conditions, (<I>S</I>)-CP as the desired product was obtained with an enantiomeric excess of 96.24% and overall conversion of 46.07%.</P><BR>[FIG OMISSION]</BR>