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We investigate the linear viscoelasticity of polymer gels produced by thedispersion of gluten proteins in water:ethanol binary mixtures with variousethanol contents, from pure water to 60% v/v ethanol. We show that the complexviscoelasticity of the gels exhibits a time/solvent composition superpositionprinciple, demonstrating the self-similarity of the gels produced in differentbinary solvents. All gels can be regarded as near critical gels withcharacteristic rheological parameters, elastic plateau and characteristicrelaxation time, which are related one to another, as a consequence ofself-similarity, and span several orders of magnitude when changing the solventcomposition. Thanks to calorimetry and neutron scattering experiments, weevidencea co-solvency effect with a better solvation of the complexpolymer-like chains of the gluten proteins as the amount of ethanol increases.Overall the gel viscoelasticity can be accounted for by a unique characteristiclength characterizing the crosslink density of the supramolecular network,which is solvent composition-dependent. On a molecular level, these findingscould be interpreted as a transition of the supramolecular interactions, mainlyH-bonds, from intra- to interchains, which would be facilitated by thedisruption of hydrophobic interactions by ethanol molecules. This work providesnew insight for tailoring the gelation process of complex polymer gels.

Tailoring the viscoelasticity of polymer gels of gluten proteins through solvent quality