Multi-scale structural deconstruction mechanism of wheat proteins induced by cold plasma treatment and its...

The aim of this study is to systematically reveal the evolution of wheat proteins from conformational transition to network deconstruction induced by cold plasma (CP) treatment, and to elucidate the mechanism of its effect on dough processing characteristics. Multiscale analysis revealed that CP treatment induced oxidation-modified conformation changes in proteins. The study found a critical threshold of 15 min of CP treatment, at which point the gluten network undergoes a qualitative transition from reorganization to deconstruction. Secondary structure underwent a marked transition from β-folding to α-helix. At the molecular level, free thiol content decreased by 18.5%. The gliadin fractions are degraded and proteins undergo deep fragmentation. These structural alterations induced a phase rearrangement of water within the dough system, significantly increasing the proportion of free water and disrupting the equilibrium of intermolecular forces. Macroscopic rheology exhibits: deterioration in powder properties, a marked decrease in viscoelastic parameters, and a transition of the dough from a robust viscoelastic state to a fragile viscous state. This discovery provides crucial theoretical underpinnings and process guidance for the precise regulation of CP technology in grain processing.