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- W2037650170 abstract "Competitive adsorption at pH 7 has been investigated at the emulsion droplet surface and the planar oil-water interface for binary mixtures of the egg-yolk protein, phosvitin, and a milk protein, β-caScin or β-lactoglobulin. Analysis of the aqueous phase of n-tetradecane-in-water emulsions made with a mixture of phosvitin + milk protein (0.5 wt% total protein) indicates that the milk protein predominates at the surface. This is thermodynamically consistent with the much lower surface activity of phosvitin at the n-tetradecane-water interface. In experiments involving addition of milk protein after emulsification, β-caScin displaces 70% of adsorbed phosvitin within a few minutes, and then another 10% over a period of 48 h, whereas β-lactoglobulin displaces 57% within a few minutes, but none thereafter. Taken together with previous results for the competitive adsorption of different milk proteins, the data are used to discuss how the time-dependent displacement behaviour of a disordered protein β-cascin differs from that of a structured globular protein β-lactoglobulin. Special features of the adsorption behaviorfr of phosvitin are related to its high level of phosphorylation and its high charge density." @default.
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- W2037650170 date "1991-02-01" @default.
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- W2037650170 title "Competitive adsorption of phosvitin with milk proteins in oil-in-water emulsions" @default.
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- W2037650170 doi "https://doi.org/10.1016/s0268-005x(09)80135-5" @default.
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