The surface properties of aqueous dispersions of worm-like ovalbumin fibrils are determined on a water/air interface by the methods of surface rheology and tensiometry. These properties depend strongly on the degree of purification and elimination of peptides having a high surface activity. Purified dispersions are characterized by slower variations in the surface properties compared to native protein solutions. At the same time, the steady-state values of the surface elasticity of the dispersions turn out to be approximately 1.5-fold lower and the surface tension is higher than the corresponding values for native protein solutions, thereby indicating the formation of a continuous loose adsorption layer of ovalbumin fibrils on the dispersion surface. The conclusions inferred from the data of surface rheology and tensiometry are confirmed by atomic force microscopy.
Akentiev et al. (Wed,) studied this question.
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