The interfacial behavior of β-casein (βCS) has been investigated in presence of the cationic surfactant dodecyl trimethyl ammonium bromide (DoTAB) at the water/hexane interface and compared to that obtained for the water/air interface. The used experimental technique is a drop profile analysis tensiometer specially equipped with a coaxial double capillary, which allows investigation of sequential adsorption of individual components besides the traditional simultaneous adsorption of two species. This method also provides the dilational rheological measurements based on low frequency harmonic drop oscillations. The tensiometric results show that the equilibrium states of the mixed βCS/DoTAB layers built up on the two different routes do not differ significantly, that is, the general compositions of the mixed layers are similar. However, the results of dilational rheology for the two adsorption strategies are remarkably different indicating different dynamic characteristics of the adsorbed layers. These findings suggest that the respective mixed layers are more proteinlike if they are formed via sequential adsorption and more surfactant-like after simultaneous adsorption. In contrast to the W/A interface, at the W/H interface proteins remain at the interface once adsorbed and cannot be displaced just by competitive adsorption of surfactants.