Dynamic Properties of β-Casein Fibril Adsorption Layers at the Air-Water Interface.

Although the formation of the layers of fibrillar aggregates at liquid-liquid and liquid-gas interfaces can significantly increase the stability of disperse systems, like foams and emulsions, any information on their structure and properties is rather limited. In the present work, surface properties of the adsorption layers of fibrils of intrinsically disordered β-casein are investigated. For unpurified dispersions of the fibrils of this protein, the dynamic surface elasticity proved to be close to the values for the native protein solutions. This behavior is typical for dispersions of fibrils of globular proteins. However, previously studied fibrils of another intrinsically disordered protein, κ-casein, do not demonstrate this similarity. The contribution of β-casein fibrils to the dynamic surface properties becomes noticeable only after the purification of the dispersions from impurities of high surface activity. The dynamic surface elasticity increases up to 48 mN/m after two purification cycles, i.e., to values 4 times higher than the steady-state values of native protein adsorption layers at the same protein bulk concentrations.