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

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

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

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Il lavoro di studio e di ricerca è stato pubblicato su Biotechnology & Bioengineering, rivista scientifica internazionale pubblicata dalla Wiley & Sons avente un Impact Factor di 2.173. Il lavoro ha carattere multidisciplinare, con competenze nella scienza e tecnologia delle membrane, preparazione e caratterizzazione di emulsioni olio in acqua al di sotto del micron, fenomeni interfacciali, immobilizzazione di enzimi su membrana, biocatalisi eterogenea mediata da enzimi (in particolare phase transfer catalysis), stereochimica. (literal)

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The work show that immobilised enzyme can have high catalytic activity, high enantioselectivity and high stability when working in proper condition of microenvironment reaction and mass transfer properties and that the generally observed behaviour of increase of stability and decrease of activity and selectivity is not necessarily a general rule. The organic/aqueous interface played an important role in lipase enantiocatalytic hydrolysis of racemic naproxen ester both in stirred tank reactor and in lipase-immobilised membrane reactor. In stirred tank reactor, enzyme selectivity was very good (about 98%) but stability was low (about 15 hours of half-life time). As a comparison, lipase immobilised in membrane reactor showed stable activity and selectivity during 250 hours of reaction process. By combining the advantage of emulsion in its large interfacial area and the advantage of membrane reactor for stable enzyme activity and simultaneous separation of product from reaction microenvironment, the emulsion enzyme membrane reactor in the present study showed good performance in lipase enantiocatalytic reaction measured by production, enantiomeric excess and enantioselectivity. The organic/aqueous ratio and permeation rate of aqueous phase are two important parameters due to effect on reaction rate and product expelling rate. The fine controlling of these two parameters leads to stable performance of emulsion membrane reactor. (literal)

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1) Istituto per la Tecnologia delle Membrane, CNR; 2) Department of Environmental and Chemical Engineering, Xian Jiao Tong University, Xian, 710049, China (literal)

Titolo

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

Abstract

The enantiocatalytic performance of immobilised lipase in an emulsion membrane reactor using stable emulsion prepared by membrane emulsification technology has been studied. The production of optical pure (S)-naproxen from racemic naproxen methyl ester has been used as 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 immobilised in the sponge layer (shell side) of capillary polyamide membrane with 50 kDa cut-off. The results evidenced that lipase maintained stable activity during all the operation time (more than 250 hours), showing an enantiomeric excess (96 ±2%) comparable to the free enzyme (98 ± 1%) and much higher compared to similar lipase-loaded membrane reactors used in two-separate phase systems (90%). The results demonstrate that immobilised enzymes can achieve high stability as well as high catalytic activity and enantioselectivity. (literal)

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