Gliadins are edible wheat storage proteins well known for their surface active properties. In this paper, we present experimental results on the interfacial properties of acidic solutions of gliadin studied over 5 decades of concentrations, from 0.001 to 110 g/L. Dynamic pendant drop tensiometry reveals that the surface pressure  of gliadin solutions builds up in a multistep process. The series of curves of the time evolution of collected at different bulk protein concentrations C can be merged onto a single master curve when  is plotted as a function of t where t is the time elapsed since the formation of the air/water interface and  is a shift parameter that varies with C as a power law with an exponent 2. The existence of such time-concentration superposition, which we evidence for the first time, indicates that the same mechanisms govern the surface tension evolution at all concentrations and are accelerated by an increase of the bulk concentration. The scaling of  with C is consistent with a kinetic of adsorption controlled by the diffusion of the proteins in the bulk. Moreover, we show that the proteins adsorption at the air/water interface is kinetically irreversible. Correlated evolutions of the optical and elastic properties of the interfaces, as probed by ellipsometry and surface dilatational rheology respectively, provide a consistent physical picture of the building up of the protein interfacial layer. A progressive coverage of the interface by the proteins occurs at low . This stage is followed, at higher , by conformational rearrangements of the protein film, which are identified by a strong increase of the dissipative viscoelastic properties of the film concomitantly with a peculiar evolution of its optical profile that we have rationalized. In the last stage, at even higher surface pressure, the adsorption is arrested; the optical profile is not modified while the elasticity of the interfacial layer dramatically increases with the surface pressure, presumably due to the film ageing.