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Gliadins are edible wheat storage proteins well known for their surface active properties1, 2. Although their foaming3 and emulsifying4 capability is useful in food industry, the physical mechanisms of their adsorption at an interface are not well understood and the resulting structure of the protein interfacial films not yet well characterized. In this talk, we will present experimental results on the interfacial properties of acidic gliadin solutions studied over 4 decades of concentrations from 0.01 up to 110 mg/ml.Dynamic pendant drop tensiometry reveals that the surface pressure of gliadin solutions builds up in a multistep process. We show that the series of curves of the time evolution of alpha.time collected at different protein concentrations can be merged onto a single master curve when surface pressure is plotted as a function of alpha.time where t is the time elapsed since the formation of the air/water interface and alpha is a shift parameter that varies with the bulk protein concentration as a power law with an exponent 1.6. The existence of a master curve indicates that the surface pressure is the relevant parameter to characterize the interfaces covered with gliadin proteins.Optical and elastic properties of the interfaces are studied by dilatational rheology and ellipsometry and provide a consistent physical picture of the adsorption processes. Correlated evolutions of ellipsometry and rheological properties show a simple and progressive coverage of the interface by individual proteins at low surface pressure. This stage is followed, at higher surface pressure, by conformational rearrangements of the protein film, which are identified by a strong increase of the dissipative viscoelastic properties of the film concomitantly with an anomalous evolution of its optical profile that we have quantitatively rationalized. In the last stage, at even higher surface pressure, the optical profile is not modified while the elasticity of the film dramatically increases resulting from the gelation of the film due to the formation of intermolecular bonds. [1] J.Ornebro, T. Nylander, A-C Eliasson (2000). Journal of Cereal Science 31, 195-221[2] R. C. A Keller, R. Orsel, R. J. Hamer (1997). Journal of Cereal Science 25, 175-183[3] Martin A. Bos, Bertus Dunnewind, Ton van Vliet (2003). Colloids and Surfaces B 31, 95-105[4] Y.Popineau, F.Pineau, P. Evon, S. Bérot (1999). Nahrung 6, S. 361-367