Immobilization of Serratia marcescens Lipase and Catalytic Resolution of Trans-3-(4′-methoxyphenyl)glycidic Acid Methyl Ester

Abstract

Abstract Seven carriers were investigated for immobilization of the lipase from Serratia marcescens ECU1010, and diatomite and Eupergit C were found to be ideal supports. The thermal and storage stability of the lipase was significantly improved after being immobilized onto these two supports. After heating at 50$^{o}$C for 6 h, only a small decrease in the activity was observed for the diatomite-adsorbed lipase. About 50% of the initial activity was retained when the two immobilized enzyme samples were stored at 4$^{o}$C for 180 days. Operational stability tests indicated that the half-life of the lipase immobilized on Eupergit C was about 2-fold longer than that of the diatomite-immobilized lipase. The crosslinking with glutaraldehyde had no significant effect on the activity of the Eupergit C-immobilized lipase, whereas the reusability of the crosslinked diatomite-immobilized enzyme was slightly improved. Using the crosslinked diatomite-immobilized lipase, an up-scaled bioresolution of (±)-3-(4'-methoxyphenyl)glycidic acid methyl ester ((±)-MPGM) was performed in a 500-ml emulsion reactor at 30$^{o}$C with 200 ml of biphasic solution (toluene:water = 1:1) and 0.5 mol/L of (±)-MPGM in toluene. After 5 batches of reaction, crystalline (2 R , 3 S )-(–)-MPGM with a chemical purity of 100% and an optical purity of > 99% enantiomeric excess was obtained with a yield of 37.2%.