Gluten protein transformations during bread processing: Molecular and microstructural analysis

The dynamic transformation of gluten was elucidated to understand the gluten network and texture variation during breadmaking. The results showed that as the dough progressed from mixing to baking, the content of α- and β-gliadins decreased significantly, while the glutenin subunit content and gluten macromolecular polymers increased. Moreover, the free sulfhydryl content decreased upon baking, indicating structural changes in the gluten network. As baking progressed, the role of hydrogen bonds and hydrophobic interactions diminished, while intermolecular β-sheet content increased due to protein aggregation. The compact gluten structure with a high amount of protein junctions and total protein length during mixing and shaping was significantly different from the high lacunarity ratio in gluten after baking. Based on Pearson correlation analysis, the textural features of bread dough were connected with the transformation of the gluten molecular structure during breadmaking. Research on the transformation of gluten networks during breadmaking could provide valuable mechanistic insights for improving the quality of bread. • Significant changes in gliadins and glutenin subunits occurred from mixing to baking. • Mixing and shaping created dense gluten networks with high protein junctions. • Texture of bread dough linked to gluten structure change during bread breadmaking.