Phosvitin-calcium aggregation and organization at the air-water interface.

Abstract : Phosvitin, an egg yolk protein constituted by 50% of phosphorylated serines, presents good emulsifying properties whereas its interfacial properties are not yet clearly elucidated and remain object of discussion. Phosvitin has a high charge density and naturally forms aggregates through phosphocalcic bridges in egg yolk. This high charge density, doubled by this capacity to aggregate, limits the adsorption of the protein at the air-water interface. In this work, we investigated the aggregation impact by calcium ions on the organization of the phosvitin interfacial film using the atomic force microscopy. Phosvitin interfacial films without calcium ions are compared to phosvitin interfacial films formed in the presence of calcium ions in the subphase. We demonstrated that phosvitin is able to anchor at air-water interfaces in spite of its numerous negative charges. In the compression isotherm a transition was observed just before 28 mN/m signifying a possible modification of the interfacial film structure or organization. Calcium ions induce a reorganization towards a greater compaction of the phosvitin interfacial film even at low surface pressure. In conclusion we suggest that, in diluted regime, phosvitin molecules could adsorb by their two hydrophobic extremities exhibiting loops in the aqueous phase, whereas in concentred regime (high interfacial concentration) it would be adsorbed at the interface by only one extremity (brush model).
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Article dans une revue
Colloids and Surfaces B: Biointerfaces, Elsevier, 2008, 63 (1), pp.12-20. 〈10.1016/j.colsurfb.2007.10.012〉
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Contributeur : Céline Martel <>
Soumis le : vendredi 7 septembre 2012 - 16:01:39
Dernière modification le : mercredi 21 mars 2018 - 16:08:07

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C. Belhomme, E. David-Briand, Catherine Guérin-Dubiard, V. Vié, M. Anton. Phosvitin-calcium aggregation and organization at the air-water interface.. Colloids and Surfaces B: Biointerfaces, Elsevier, 2008, 63 (1), pp.12-20. 〈10.1016/j.colsurfb.2007.10.012〉. 〈hal-00729897〉

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