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Article Dans Une Revue Food Hydrocolloids Année : 2007

Comparative behaviour of goat β and αs1-caseins at the air-water interface and in solution

Résumé

Here we present a comparative study of caprine β- and αs1-caseins behaviours at the air-water interface and in solution. Both caseins were purified from the milk of a single goat homozygous at the αs1- and β-Cn loci, with a high degree of purity (98%). Physical measurements (ellipsometry, surface pressure and surface rheology) were performed at the air-water interface, whereas SAXS measurements were performed on casein solutions. Our results clearly show that self-organizations, both at the air-water interface and in solution are different for β- and αs1-caseins. β-casein is unfolded in solution and forms a network at the interface, while αs1-casein forms compact objects in solution and is organised in fluid domains at the interface. We also show that the presence of Ca2+ in the subphase strongly disturbs the interfacial layer formed by the caseins. It is elsewhere worth noting that in solution, the aggregation of αs1-casein induced by calcium ions is associated with a pronounced change in the molecular structural organisation of the protein, which seems to adopt, in these conditions, an unfolded structure.

Dates et versions

hal-00908061 , version 1 (22-11-2013)

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Sylvie Beaufils, Rachida Hadaoui-Hammoutène, Véronique Vié, Guy Miranda, Javier Perez, et al.. Comparative behaviour of goat β and αs1-caseins at the air-water interface and in solution. Food Hydrocolloids, 2007, 21 (8), pp.1330-1343. ⟨10.1016/j.foodhyd.2006.10.014⟩. ⟨hal-00908061⟩
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