Abstract
Structural investigation of gluten-glycerol blends subjected to heat-treatment was carried out by size-exclusion high performance liquid chromatography (SEC) and stress-strain tests. SEC is a valuable tool to investigate the size distribution of gluten protein chains, while the molecular weight between network junctions (M-e) can be estimated from the elastic plateau modulus. Wheat gluten aggregation upon thermosetting seems to proceed through direct covalent cross-linking between glutenin oligomers and the gluten macropolymer. The time course of the reaction, which showed a slow-down of the reaction rate with time, was described by a simple mechanistic model. The deceleration of the reaction rate was presumably due to the development of a three-dimensional protein network, which decreased the accessibility of reactive groups. The network formation could be evidenced separately by the decrease of M-e during the heat-treatment.