APPLICATION OF STABLE EMULSIONS TO LIPASE IMMOBILISED MEMBRANE REACTORS FOR KINETIC RESOLUTION OF RACEMIC ESTERS

  • Giorno, Lidietta (Institute on Membrane Technology, CNR-ITM C/o University of Calabria) ;
  • Na, Li (Institute on Membrane Technology, CNR-ITM C/o University of Calabria) ;
  • Drioli, Enrico (Institute on Membrane Technology, CNR-ITM C/o University of Calabria)
  • 발행 : 2003.07.01

초록

The paper discusses the use of stable emulsion, prepared by membrane emulsification technology, to improve the enantiocatalytic performance of immobilised lipase in multiphasic membrane reactors. The production of optical pure (S)-naproxen from racemic naproxen methyl ester has been used as model reaction system. The enzyme was immobilised in the sponge layer (shell side) of capillary polyamide membrane with 50 kDa cut-off, The O/W emulsion, containing the substrate in the organic dispersed phase, was fed to the enzyme membrane reactor from shell-to-lumen. The results evidenced that lipase maintained stable activity during all the operation time (more than 250 hours), showing an enantiomeric excess (96 $\pm$2%) comparable to the free enzyme (98 $\pm$ 1%) and much higher compared to similar lipase-loaded membrane reactors used in two-separate phase systems (90%). The study showed that immobilised enzymes can achieve high stability as well as high catalytic activity and enantioselectivity.

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