Protein-poly(silicic) acid interactions at the air/solution interface.
The structure of the interface generated by a spread layer of beta-casein on an aqueous colloidal poly(silicic) acid subphase is described. The results are compared with data for the protein alone spread at the air/water interface and the silicate solution. Films develop at the air-solution interface and a strong pH dependence of the interaction causing this is demonstrated. Reflectometry with X-rays and neutrons was used to probe the interaction as a function of subphase pH and film compression. Film thickness, tau/A, scattering length density, rho/A(-2), water volume fraction, phi(w), and surface coverage, Gamma/mg m(-2), were used to quantify the interfacial structure. Where possible, the X-ray and neutron data sets were co-refined enabling phi(w) to be evaluated without assumption regarding the protein density. At pH 5-7, strong protein-silicate interaction occurred, the interface comprising three regions: a discrete protein upper layer on top of a 15 +/- 2 A layer of silicated material followed by a diffuse layer that extended into the subphase.