Interactions and assemblies of wheat proteins

Dynamics in stretched nanocomposites

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.

A novel and simple method for the measurement of cloud point temperatures of solutions is presented. Cloud point determination , which is currently used to establish the phase diagrams of protein solutions, is indicative of proteins interactions and constitutes a useful tool for food products engineering. We describe a novel experimental setup that allows screening of a large number of physical-chemical conditions in one measurement and the determination of cloud point temperatures both above and below ambient temperature. We use a simple method to avoid solvent evaporation and condensation, so that the setup can be used for solutions prepared with a volatile solvent. We present the operating parameter range and the precision of the measurement. The optical properties of the system are calibrated with solutions of known transmittance, and the determination of cloud point temperatures is validated on a standard non-ionic surfactant solution. Finally, we demonstrate the efficiency of the method by determining the phase diagram of a wheat protein extract, soluble in a water/ethanol mixture. Complemented with differential scanning calorimetry measurements, the liquid-liquid phase transition can be determined up to a protein concentration of 250 g/L, a range inaccessible with conventional methods for this protein extract.

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.