The influence of ionic strength on the thermal stability of wheat proteins, particularly gliadins and glutenins, has significant implications for food processing, especially in the context of breadmaking and dough processing. Ionic strength, often manipulated through the addition of salts such as sodium chloride (NaCl), affects protein solubility, structure, and stability. This study investigates how varying concentrations of sodium chloride (NaCl) influence the thermal denaturation and unfolding behavior of wheat proteins in a model system.

Thermal stability was evaluated by differential scanning calorimetry (DSC), which allows for the determination of the denaturation temperature (Tm) and the enthalpy change (ΔH) associated with protein unfolding. Results indicated that increasing ionic strength significantly increased the Tm of wheat proteins, suggesting enhanced thermal stability at higher salt concentrations. The enthalpy change also exhibited a notable shift, correlating with structural changes in the proteins under different ionic conditions.

Furthermore, the study explored the impact of ionic strength on the aggregation of wheat proteins during heating. It was found that salt concentration plays a critical role in modulating the aggregation behavior, which influences the texture and elasticity of dough, a crucial factor in bread quality. The findings highlight the complex interplay between ionic strength and wheat protein thermal behavior, suggesting that the right balance of salt can improve dough rheology and baking performance by enhancing protein stability during thermal processing.