Spontaneous gelation of wheat gluten proteins in a food grade solvent

Mohsen Dahesh (1, 2) , Amélie Banc (2) , Agnès Duri-Bechemilh (1) , Marie Helene Morel (1) , Laurence Ramos (2)

1 UMR IATE - Ingénierie des Agro-polymères et Technologies Émergentes
2 L2C - Laboratoire Charles Coulomb

Structuring wheat gluten proteins into gels with tunable mechanical properties would provide more versatility for the production of plant protein-rich food products. Gluten, a strongly elastic protein material insoluble in water, is hardly processable. We use a novel fractionation procedure allowing the isolation from gluten of a water/ethanol soluble protein blend, enriched in glutenin polymers at an unprecedented high ratio (50%). We investigate here the viscoelasticity of suspensions of the protein blend in a water/ethanol (50/50 v/v) solvent, and show that, over a wide range of concentrations, they undergo a spontaneous gelation driven by hydrogen bonding. We successfully rationalize our data using percolation models and relate the viscoelasticity of the gels to their fractal dimension measured by scattering techniques. The gluten gels display self-healing properties and their elastic plateaus cover several decades, from 0.01 to 10,000 Pa. In particular very soft gels as compared to standard hydrated gluten can be produced.

Mots clés: Near critical gel; Protein; Gluten; Hydrogen bonding; Fractal dimension; Percolation

Domaines: Ingénierie des aliments

Mohsen Dahesh, Amélie Banc, Agnès Duri-Bechemilh, Marie Helene Morel, Laurence Ramos. Spontaneous gelation of wheat gluten proteins in a food grade solvent. Food Hydrocolloids, 2016, 52, pp.1-10. ⟨10.1016/j.foodhyd.2015.06.014⟩. ⟨hal-01269395⟩