Abstract
The dilational surface rheology is applied to solutions of globular proteins (bovine serum albumin and β-lactoglobulin) in presence of urea. The kinetic dependencies of the dynamic dilational surface elasticity become non-monotonic if the denaturant concentration exceeds a certain critical value indicating the adsorption of unfolded protein molecules. The unfolding in the surface layer occurs at lower urea concentrations than in the bulk phase similar to the case of mixed solutions of the proteins and guanidine hydrochloride. At the same time, the influence of urea on the dilational surface rheological properties of protein solutions has some peculiarities. In particular, the high values of the dynamic surface elasticity close to equilibrium indicate the limited flexibility of unfolded BLG molecules in the surface layer.
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