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.

With the demography growth, there is a huge pressure on protein demand, and the development of plant based proteins is required for a future sustainable food production. Plant proteins are efficient to stabilize interfaces in foams or emulsions, and the understanding of physical mechanisms at the origin of their interfacial behavior is important to develop new products. We investigate the adsorption of wheat grains (gliadin) and sunflower seeds (helianthinin) proteins, at air-water and oil-water interfaces, respectively. A combination of tensiometry, dilatational viscoelasticity and ellipsometry measurements is used to determine the adsorption mechanisms, and characterize the structure and properties of the interfacial protein films formed with different bulk protein concentrations. We demonstrate that a diffusion-controlled adsorption occurs at low bulk protein concentration for helianthinin whereas this mechanism occurs whatever the bulk concentration for gliadins. Surface pressure-induced film relaxation through conformation changes of proteins at the air-water interface is identified for gliadin whereas surface aggregation is observed at high helianthinin concentration. Overall, our experimental results highlight that structural flexibility of proteins appears as a key factor for their interfacial activity.

The physical behavior of colloids suspended in a fluid close to a solid wall has been well characterized in the past[1]. Conversely the dynamical behavior of a particle close to a fluid interface is a relatively new field with strong implications in green and food processing [2]. Previous focus was limited to spherical particle’s viscous drag close to the interface [3] and wetting dynamics after interface breaching [4]. In this paper we present experimental results on the dynamics of micrometric colloids(spheres and ellipsoids)close to an interface between water based solution and air prior to the particle’s interfacebreaching. In order to study such dynamics we use a home-made pending-drop setup where particles dispersed in water based solutions (mixture with heavy water and/or with salt at different molarity) sediment towards the interface with air of the drop.The drop curvature is adjusted via the water solution pressure in order to obtain a flat interface at the particle scale. All the particle’s degreesof freedom (i.e. distance from the interface, position in a plane parallel to the interface and, for ellipsoids,orientation) are measured tracking the particle-interface interference patterns using incoherent ledswith three different wavelengths. The typical dynamics of a particle approaching the interface shows an initial sedimentation regimedriven by gravity and viscous drag. Closer to the interface a second regime arises which strongly depend on the solution molarity and density and particle morphology. For both particles morphologies the sedimentation dynamics stops at a distance from the interface of the order of hundreds nanometers. At small molarity (0.5 mM) both type of particles fluctuate around this position during the entire experimental observation time interval (10^3s). Increasing the molarity, ellipsoids more easily then spheres start to escape from this position approaching rapidly the interface till a distance of few nanometers. Such observations point out the importance of the electrostatic and morphology in the interaction with the interface. A calibration of thisinteraction will be presented by taking advantage of the buoyancy driving force changing the solution density. Building up on all these experimental observations, amodel considering the interplay between all the contributing interactions (i.e. gravity with buoyancy, electrostatics and Van der Walls) will be discussed and compared to the experimental results. [1]M. Hosoda, K. Sakai, and K. Takagi, Phys. Rev. E 58, 6275 (1998).[2] V. Sarrot, Z. Huang, D. Legendre, P. Guiraud, Chem. Eng. Sci. 62, 7359–7369 (2007).[3] G. M. Wang, R. Prabhakar and E. M. Sevick, Phys. Rev. Lett. 103, 248303 (2009).[4] A. Wang, W.B. Rogers, V.N. Manoharan, arXiv:1607.08167 [cond-mat.soft].

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

Controlling the interface between TiO2 nanocrystals and ionic liquids is of high fundamental and applied interest for energy storage and conversion devices. Phase transfer of nanoparticles from a synthesis medium to a processing or an application medium plays a significant role in nanotechnology. Here we demonstrate that surface modification with phosphonic acids bearing cationic end-groups can trigger the phase transfer of TiO2 nanoparticles from an aqueous sol to a typical water-immiscible ionic liquid, [Emim][NTf2]. The transfer involves both the grafting of the phosphonic acid moiety and the exchange of the counter ion of the cationic end-group by NTf2 anions, as demonstrated by solid-state NMR, elemental analysis and independent grafting and ion exchange experiments. Furthermore, the colloidal stability of the TiO2 sols in [Emim][NTf2] strongly depends on the hydrophobic character of the cationic end-groups.

Biological or artificial microswimmers move performing trajectories of different kinds such as rectilinear, circular, or spiral ones. Here, we report on circular trajectories observed for active Janus colloids trapped at the air−water interface. Circular motion is due to asymmetric and nonuni form surface properties of the particles caused by fabrication. Motion persistence is enhanced by the partial wetted state of the Janus particles actively moving in two dimensions at the air−water interface. The slowing down of in plane and out of plane rotational diffusions is described and discussed.