Use of Stable Emulsion to Improve Stability, Activity, and Enantioselectivity of Lipase Immobilized in a Membrane Reactor (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Use of Stable Emulsion to Improve Stability, Activity, and Enantioselectivity of Lipase Immobilized in a Membrane Reactor (Articolo in rivista) (literal)

Anno

• 2003-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1002/bit.10826 (literal)

Alternative label

• Giorno, L., Li, N., Drioli, E. (2003)
  Use of Stable Emulsion to Improve Stability, Activity, and Enantioselectivity of Lipase Immobilized in a Membrane Reactor
  in Biotechnology and bioengineering (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Giorno, L., Li, N., Drioli, E. (literal)

Pagina inizio

• 677 (literal)

Pagina fine

• 685 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 84 (literal)

Rivista

• Biotechnology and bioengineering (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Istituto per la tecnologia delle Membrane (literal)

Titolo

• Use of Stable Emulsion to Improve Stability, Activity, and Enantioselectivity of Lipase Immobilized in a Membrane Reactor (literal)

Abstract

• The enantiocatalytic performance of immobilized lipase in an emulsion membrane reactor using stable emulsion prepared by membrane emulsification technology was studied. The production of optical pure (S)-naproxen from racemic naproxen methyl ester was used as a model reaction system. The O/W emulsion, containing the substrate in the organic phase, was fed to the enzyme membrane reactor from shell-to-lumen. The enzyme was immobilized in the sponge layer (shell side) of capillary polyamide membrane with 50 kDa cut-off. The aqueous phase was able to permeate through the membrane while the microemulsion was retained by the thin selective layer. Therefore, the substrate was kept in the enzyme-loaded membrane while the water-soluble product was continuously removed from the reaction site. The results show that lipase maintained stable activity during the entire operation time (more than 250 h), showing an enantiomeric excess (96 F 2%) comparable to the free enzyme (98 F 1%) and much higher compared to similar lipase-loaded membrane reactors used in two-separate phase systems (90%). The results demonstrate that immobilized enzymes can achieve high stability as well as high catalytic activity and enantioselectivity (literal)

Prodotto di

• Operazioni a membrana in processi biotecnologici (PM.P02.008.002) (Modulo)
• Institute on membrane technology (ITM) (Istituto)

Autore CNR

• ENRICO DRIOLI (Unità di personale esterno)
• LIDIETTA GIORNO (Persona)

Insieme di parole chiave

• Keywords of "Use of Stable Emulsion to Improve Stability, Activity, and Enantioselectivity of Lipase Immobilized in a Membrane Reactor" (Insieme di parole chiave)

Incoming links:

Prodotto

• Institute on membrane technology (ITM) (Istituto)
• Operazioni a membrana in processi biotecnologici (PM.P02.008.002) (Modulo)

Autore CNR di

• LIDIETTA GIORNO (Persona)
• ENRICO DRIOLI (Unità di personale esterno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Biotechnology and bioengineering (Rivista)

Insieme di parole chiave di

• Keywords of "Use of Stable Emulsion to Improve Stability, Activity, and Enantioselectivity of Lipase Immobilized in a Membrane Reactor" (Insieme di parole chiave)