Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
beta-Casein adsorption at the hydrophobized silicon oxide-aqueous solutioninterface and the effect of added electrolyte
Autore:
Nylander, T; Tiberg, F; Su, TJ; Lu, JR; Thomas, RK;
Indirizzi:
Univ Lund, Ctr Chem & Chem Engn, S-22100 Lund, Sweden Univ Lund Lund Sweden S-22100 Ctr Chem & Chem Engn, S-22100 Lund, Sweden Inst Surface Chem, S-11486 Stockholm, Sweden Inst Surface Chem StockholmSweden S-11486 em, S-11486 Stockholm, Sweden Univ Surrey, Dept Chem, Guildford GU2 5XH, Surrey, England Univ Surrey Guildford Surrey England GU2 5XH ord GU2 5XH, Surrey, England Phys & Theoret Chem Lab, Oxford OX1 3PJ, England Phys & Theoret Chem Lab Oxford England OX1 3PJ , Oxford OX1 3PJ, England
Titolo Testata:
BIOMACROMOLECULES
fascicolo: 1, volume: 2, anno: 2001,
pagine: 278 - 287
SICI:
1525-7797(200121)2:1<278:BAATHS>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
SELF-ASSEMBLED MONOLAYERS; OIL-WATER INTERFACES; NEUTRON REFLECTIVITY; AIR/WATER INTERFACE; ADSORBED LAYERS; CALCIUM-IONS; PROTEIN; SURFACES; BINDING; LACTOGLOBULIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Nylander, T Univ Lund, Ctr Chem & Chem Engn, Box 124, S-22100 Lund, SwedenUniv Lund Box 124 Lund Sweden S-22100 4, S-22100 Lund, Sweden
Citazione:
T. Nylander et al., "beta-Casein adsorption at the hydrophobized silicon oxide-aqueous solutioninterface and the effect of added electrolyte", BIOMACROMOL, 2(1), 2001, pp. 278-287

Abstract

The effect of the presence of NaCl, CaCl2, or MgCl2 at the same ionic strength on the structure of beta -casein layers adsorbed on hydrophobic surfaces has been investigated by neutron reflectivity measurements. The data were fitted to a four-layer model. The volume fraction versus distance profiles have a similar shape whether beta -casein is adsorbed from NaCl, CaCl2, and MgCl2 of the same ionic strength or whether the protein concentration islowered 10 times. In particular at larger distances from the surface, the volume fraction values are low and similar. However, close to the hydrophobic surface the volume fraction of protein decreases in the order CaCl2 > MeCl2 > NaCl. We have also used a specific proteolytic enzyme, endoproteinaseAsp-N, which cleaves off the hydrophilic part of beta -casein, as a tool to reveal the interfacial structure of the protein. For all the different types of added electrolytes, endoproteinase Asp N only affects the outermost beta -casein layer. Subsequent addition of beta -casein in all cases led tolarge increases in amounts adsorbed and in the thickness of the outer layers.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 18:46:33