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We investigate the structure of gluten polymer-like gels in a binary mixtureof water/ethanol, $50/50$ v/v, a good solvent for gluten proteins. Glutencomprises two main families of proteins, monomeric gliadins and polymerglutenins. In the semi-dilute regime, scattering experiments highlight twoclasses of behavior, akin to standard polymer solution and polymer gel,depending on the protein composition. We demonstrate that these two classes areencoded in the structural features of the proteins in very dilute solution, andare correlated with the presence of proteins assemblies of typical size tens ofnanometers. The assemblies only exist when the protein mixture is sufficientlyenriched in glutenins. They are found directly associated to the presence inthe gel of domains enriched in non-exchangeable H-bonds and of size comparableto that of the protein assemblies. The domains are probed in neutron scatteringexperiments thanks to their unique contrast. We show that the samplevisco-elasticity is also directly correlated to the quantity of domainsenriched in H-bonds, showing the key role of H-bonds in ruling thevisco-elasticity of polymer gluten gels.

Impact of the protein composition on the structure and viscoelasticity of polymer-like gluten gels