The equations of state, adsorption isotherms and functions of the distribution of protein molecules in liquid interfacial layers with respect to molar area and the equations for their viscoelastic behavior are presented. This theory was used to determine the adsorption characteristics of β-casein and β-lactoglobulin at water/oil interfaces. The experimental results are shown to be describable quite adequately by the proposed theory with consistent model parameters. The data analysis demonstrated that the β-casein molecule adsorbed at equilibrium conditions is more unfolded as compared with dynamic conditions, and this fact causes the significant increase of the adsorption equilibrium constant. The theory assumes the adsorption of protein molecules from the aqueous solution and a competitive adsorption of alkane molecules from the alkane phase. The comparison of the experimental equilibrium interfacial tension isotherms for β-lactoglobulin at the solution/hexane interface with data calculated using the proposed theoretical model demonstrates that the assumption of a competitive adsorption is essential, and the influence of the hexane molecules on the shape of the adsorption isotherm does in fact exist.
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