Résumé
Natural protein sources often display a huge complexity, being composed of a blend of polypeptides of various molecular weight, pHi and charge density. Gluten, the proteins extracted from wheat flour is one of such. Gluten is widely used for its viscoelastic properties as an improver of cereal products (bread, pastry, etc.). It is composed of two classes of proteins, named gliadin and glutenin, similar in their amounts in glutamine (30%) and proline (10%). The more than 25 different polypeptides belonging to the gliadin class are hard to fractionate into individual components because of high redundancy in the primary sequences. Glutenin are in the form of polymers made from several distinct polypeptides concatenated through inter-chain disulfide bonds. Their molecular weights are evenly distributed from 100 kg/mol to 7,000 kg/mol.While it is well established that gliadin confers viscosity to gluten whereas glutenin polymers are at the origin of its elastic resistance, the interactions existing between both classes of gluten protein remain unknown. We previously showed by SLS and multi-angle DLS that gluten proteins suspended in ethanol/water (50/50, v/v), a theta solvent, includes large proteins assemblies (26,000 kg/mol, Rh 100nm) displaying an internal dynamic1. To get a better insight of the composition of those assemblies, we combined biochemical and physicochemical approaches. On the one hand, gluten proteins suspended in ethanol/water were fractionated by Asymmetrical- Flow-Field-Flow Fractionation (A4F) coupled to UV, SLS and QELS detectors. On the other hand, gluten proteins were partitioned by liquid-phase decomposition in respect with temperature. Protein composition of partitioned phases and eluting fractions recovered from A4F were characterized by size-exclusion chromatography. A specific interaction between omega-gliadin and glutenin polymers was evidenced.This result strengthens a very recent study that demonstrates a significant positive correlation between glutenin polymeric proteins, the ω‐gliadin fraction, and dough properties.