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Titolo:
Transport behavior of protein in bulk liquid membrane using reversed micelles
Autore:
Nishii, Y; Kinugasa, T; Nii, S; Takahashi, K;
Indirizzi:
Niihama Natl Coll Technol, Dept Appl Chem & Biotechnol, Niihama 7928580, Japan Niihama Natl Coll Technol Niihama Japan 7928580 , Niihama 7928580, Japan Nagoya Univ, Dept Chem Engn, Chikusa Ku, Nagoya, Aichi 4648603, Japan Nagoya Univ Nagoya Aichi Japan 4648603 a Ku, Nagoya, Aichi 4648603, Japan
Titolo Testata:
JOURNAL OF MEMBRANE SCIENCE
fascicolo: 1, volume: 195, anno: 2002,
pagine: 11 - 21
SICI:
0376-7388(20020101)195:1<11:TBOPIB>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
MASS-TRANSFER; SIZE DISTRIBUTION; EXTRACTION; LYSOZYME; COLUMN;
Keywords:
liquid membrane; reversed micelles; protein; cation; interface;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Engineering, Computing & Technology
Citazioni:
16
Recensione:
Indirizzi per estratti:
Indirizzo: Nishii, Y Niihama Natl Coll Technol, Dept Appl Chem & Biotechnol, Niihama 7928580, Japan Niihama Natl Coll Technol Niihama Japan 7928580 7928580, Japan
Citazione:
Y. Nishii et al., "Transport behavior of protein in bulk liquid membrane using reversed micelles", J MEMBR SCI, 195(1), 2002, pp. 11-21

Abstract

Transport of lysozyme through a liquid membrane of reversed micelles of aerosol-OT (AOT) was studied. The feed phase was aqueous KCI or NaCl solutionof lysozyme, and the recovery phase was aqueous KCI or BaCl2 solution, while the membrane is the solutions of AOT with or without contacting the feedsolution. The cations in feed phase are transferred through the liquid membrane and this cation transfer affects that of lysozyme and the size of reversed micelles of the membrane phase. Following transfer mechanisms have been proposed for the three systems investigated: the system NaCl-KCl, for which formation of large aggregates in the membrane phase was observed, has aso flexible interface that the micelles could become unstabilized in the membrane phase. For KCl-BaCl2 system, the divalent ion Ba2+ is selectively and excessively adsorbed on the interface and the negatively charged lysozyme molecules may be re-extracted at the interface of the recovery side by the electrostatic interaction with the adsorbed Ba2+ ions. Both sides of the interfaces of the system KCI-KCI have an adequate flexibility that extraction and back-extraction of lysozyme through the membrane are attainable, although the transfer rate is rather low. (C) 2002 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 09:45:22