Abstract
SummaryThis study examined changes in heat‐induced gluten proteins, focusing on their structure, physicochemical properties, and molecular analysis. The results demonstrated that gliadin had a high denaturation temperature (68.04 °C) and minimal aggregation during heating (25 °C–95 °C), yet it hindered thermal reaction progress of gluten effectively. Heating caused a shift from α‐helical structure to random coil and β‐turn structures, with a decrease in fluorescence intensity. High temperature reduced sulphydryl groups in gluten and glutenin, reaching 0.64 and 0.58 mmol L−1, respectively. However, the content of sulphydryl groups in gliadin remained relatively stable at around 0.37 mmol L−1. Notably, the configuration of disulphide bonds in gliadin, particularly in the g‐g‐g configuration, displayed greater stability. Microstructure analysis revealed increased compactness in all protein fractions as temperature rose. Overall, gliadin had greater thermal stability, impeding glutenin aggregation and gluten network formation. These findings provide valuable insights for cooking, processing, and storage of gluten proteins.
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