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- W2019957688 abstract "Abstract Here we present a comparative study of caprine β - and α s1 -caseins behaviours at the air–water interface and in solution. Both caseins were purified from the milk of a single goat homozygous at the α s1 - 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 α s1 -caseins. β -casein is unfolded in solution and forms a network at the interface, while α s1 -casein forms compact objects in solution and is organised in fluid domains at the interface. We also show that the presence of Ca 2+ in the subphase strongly disturbs the interfacial layer formed by the caseins. It is elsewhere worth noting that in solution, the aggregation of α s1 -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." @default.
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- W2019957688 date "2007-12-01" @default.
- W2019957688 modified "2023-10-16" @default.
- W2019957688 title "Comparative behaviour of goat β and αs1-caseins at the air–water interface and in solution" @default.
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- W2019957688 doi "https://doi.org/10.1016/j.foodhyd.2006.10.014" @default.
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