Wheat proteins play a critical role in determining the rheological and textural properties of dough and, consequently, the quality of baked products. Among the many factors affecting protein functionality, ionic interactions mediated by sodium chloride (NaCl) are particularly significant in both industrial and laboratory processing of wheat-based foods. This study investigates the interaction between sodium chloride and major wheat storage proteins—gliadin and glutenin—focusing on changes in their solubility, secondary structure, and functional behavior.

Wheat flour samples were treated with varying concentrations of NaCl (0–2.0 M) and analyzed using sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE), Fourier-transform infrared spectroscopy (FTIR), and rheological measurements. Results indicated that low NaCl concentrations enhanced protein hydration and solubility by weakening hydrophobic interactions, while higher concentrations promoted aggregation through salting-out effects. FTIR spectra revealed that moderate salt levels increased β-sheet content, suggesting structural stabilization of glutenin polymers, whereas excessive NaCl disrupted the protein network. Rheological tests showed improved dough elasticity and extensibility at 0.5 M NaCl but a decline in viscoelastic properties beyond 1.5 M.