Mechanisms of maturation regulated gluten network formation: Perspectives from differential aggregation of glutenin and gliadin.

To elucidate the structural and functional evolution of glutenin (Glu) and gliadin (Gli) in wheat gluten under different maturation temperatures (15 °C, 25 °C, and 40 °C), as well as their synergistic mechanisms. Maturation at 25 °C for 50 days most effectively improved the gluten components viscoelasticity. During maturation, the content of α-/γ-gliadin decreased with prolonged maturation time, while the content of high- and low-molecular-weight glutenin subunits increased correspondingly. Further mechanistic analysis revealed that the aggregation of glutenin was primarily driven by the oxidation of free sulfhydryl groups, manifested as reduced SDS extractability, an increase in the gauche-gauche-gauche conformation of disulfide bonds, and the formation of larger aggregates. In contrast, the aggregation of Gli was mainly mediated by non-covalent interactions such as hydrophobic forces, with its stable intramolecular disulfide structure remaining largely unchanged. In summary, the improvement of the gluten network originated from the synergistic interaction between Glu and Gli during maturation.