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Titolo:
Selective extraction of lysozyme from a mixture with lactoferrin by ultrafiltration. Role of the physico-chemical environment
Autore:
Chaufer, B; Rabiller-Baudry, M; Lucas, D; Michel, F; Timmer, M;
Indirizzi:
Univ Rennes 1, INRA, Lab Proc Separat, UA 991, F-35042 Rennes, France UnivRennes 1 Rennes France F-35042 arat, UA 991, F-35042 Rennes, France INRA, Rech Technol Laitiere Lab, F-35042 Rennes, France INRA Rennes France F-35042 Technol Laitiere Lab, F-35042 Rennes, France NIZO, Dept Proc Engn, NL-6710 BA Ede, Netherlands NIZO Ede Netherlands NL-6710 BA t Proc Engn, NL-6710 BA Ede, Netherlands
Titolo Testata:
LAIT
fascicolo: 1, volume: 80, anno: 2000,
pagine: 197 - 203
SICI:
0023-7302(200001/02)80:1<197:SEOLFA>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Keywords:
ultrafiltration; protein; selectivity; electrophoretic mobility; specific adsorption;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
10
Recensione:
Indirizzi per estratti:
Indirizzo: Chaufer, B Univ Rennes 1, INRA, Lab Proc Separat, UA 991, Campus de Beaulieu,Bat 10A,CS 74205, F-35042 Rennes, France Univ Rennes 1 Campus de Beaulieu,Bat 10A,CS 74205 Rennes France F-35042
Citazione:
B. Chaufer et al., "Selective extraction of lysozyme from a mixture with lactoferrin by ultrafiltration. Role of the physico-chemical environment", LAIT, 80(1), 2000, pp. 197-203

Abstract

Variation of the physico-chemical environment was used to optimize the selective extraction of lysozyme(14 300 g.mol(-1)) from a model protein mixture with lactoferrin (77 000 g.mol(-1), in monomer form) by ultrafiltration (UF). The system protein-membrane-electrolyte was studied using electrokinetic measurements, in order to determine the charge of both free proteins andfouled membrane, depending on the physico-chemical environment (pH, ionic strength, chemical nature of added salts). This paper shows that, in order to achieve the extraction of a protein from a mixture, the following strategy can be used: the target protein recovered in the permeate has to be uncharged, whereas the retained protein has to be charged in order to exploit the electrostatic repulsion of the membrane partly fouled by the charged protein. This approach was successfully used to achieve the lysozyme/lactoferrin separation with a high selectivity (lysozyme transmission/lactoferrin transmission) using an anionic membrane of pore diameter close to 28 nm. The selectivity of the separation was studied according to the variation of theionic strength, in the range 1 to 150 mmol.L-1, with either sodium chloride or potassium phosphate. Whereas selectivities were close to 20 in sodium chloride, they were always greater in potassium phosphate and increased up to 120.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 17/01/21 alle ore 18:35:40