Unexpected differences in the behavior of ovotransferrin at the air-water interface at pH 6.5 and 8.0.
2011
Le Floch-Fouéré, Cécile | Pezennec, Stéphane | Pézolet, Michel | Rioux-Dubé, Jean-François | Renault, Anne | Beaufils, Sylvie | Science et Technologie du Lait et de l'Oeuf (STLO) ; Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST | Centre de recherche sur les matériaux avancés (CERMA) ; Université Laval [Québec] (ULaval) | Institut de Physique de Rennes (IPR) ; Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)
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Mostrar más [+] Menos [-]Inglés. Adsorption of purified apo-ovotransferrin at the air-water interface was studied by ellipsometry, surface tension, polarization-modulation infrared reflection-absorption spectroscopy (PM-IRRAS), and shear elastic constant measurements. No significant difference was observed between pH 6.5 and 8.0 as regards the final value of surface concentration and surface pressure. However at low concentration, a weak barrier to adsorption is evidenced at pH 6.5 and confirmed by PM-IRRAS measurements. At a pH where the protein net charge is negative (pH 8.0), the behavior of ovotransferrin at the air-water interface is more influenced by charge effects rather than bulk concentration effects. At this pH, the interface exhibits a low shear elastic constant and a spectral signature not usual for globular proteins.
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