The long-term stabilization of foams by proteins for food applications is related to the ability of proteins to form dense and mechanically strong adsorption layers that cover the bubbles in the foams. The hydrophobins represent a class of proteins that form adsorption layers of extraordinary high shear elasticity and mechanical strength, much higher than that of the common milk and egg proteins. Our investigation of pure and mixed (with added β-casein) hydrophobin layers revealed that their rheological behavior obeys a compound rheological model, which represents a combination of the Maxwell and Herschel–Bulkley laws. It is remarkable that the combined law is obeyed not only in the simplest regime of constant shear rate (angle ramp), but also in the regime of oscillatory shear strain. The surface shear elasticity and viscosity, Esh and ηsh, are determined as functions of the shear rate by processing the data for the storage and loss moduli, G′ and G′′. At greater strain amplitudes, the spectrum of the stress contains not only the first Fourier mode, but also the third one. The method is extended to this non-linear regime, where the rheological parameters are determined by theoretical fit of the experimental Lissajous plot. The addition of β-casein to the hydrophobin leads to softer adsorption layers, as indicated by their lower shear elasticity and viscosity. The developed approach to the rheological characterization of interfacial layers allows optimization and control of the performance of mixed protein adsorption layers with applications in food foams.