Lipase-catalyzed hydrolytic resolution of (R,S)-3-hydroxy-3-phenylpropionates in biphasic media

Lipase PS from Pseudomonas cepacia was screened as the best lipase for the hydrolytic resolution of (R,S)-ethyl 3-hydroxy-3-phenylpropionate in biphasic media. The optimal reaction conditions of using isooctane as the organic phase, aqueous pH 6, and methanol as the leaving moiety was then selected for improving the enantioselectivity in terms of VS/VR equal to 50.7. By considering the easy enzyme recovery and reduced background hydrolysis, Lipase PS covalently immobilized on Eupergi C 250L but not Sepabeads@ EC-HA was further selected for giving VS/VR = 53.6. Moreover, the kinetic analysis for each enzyme preparation was carried out and compared, showing the main effect of enzyme immobilization on decreasing the kinetic constants k2R and k2S.