Abstract <p>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.</p>