Abstract
Wheat gluten samples were subjected to different thermo-mechanical treatments. Kinetics of protein aggregation and changes in network structure were investigated through biochemical and rheological measurements. Temperature induced protein aggregation through disulphide cross-links. Shear treatment alters the aggregation mechanism since a lower energy of activation was observed. Accumulation of aggregated protein enhances the elastic behaviour of the material. The strong correlation found between the extent of protein aggregation and the molecular weight between cross-links reveals the important role of covalent bonds in the network connectivity.