To clarify the detailed behaviors of protein, starch and interactions during complex dough processing, structural changes in dough protein and starch during continuous Mixolab processing were investigated using wheat near-isogenic lines carrying high-molecular-weight glutenin subunits 1Dx5 + 1Dy10 (5 + 10) or 1Dx2 + 1Dy12 (2 + 12) at the Glu-D1 locus. A more stable gluten network including disulfide bonds and hydrophobic interactions, was formed in the 5 + 10 dough before dough weakening at 53.5 °C, than in the 2 + 12 dough. Thereafter, thermo-mechanical treatment induced the depolymerization of gluten until starch gelatinization peak at 74.6 °C; however, from the peak to trough viscosity at 82.8 °C, additional monomeric proteins were incorporated into the repolymerized proteins characterized by increased disulfide bonds, hydrogen bonds, and β-sheets. Generally, the protein aggregates of 5 + 10 showed a higher degree of polymerization and better stability than those of 2 + 12 during dough processing, which significantly slowed starch gelatinization and recyclization. Moreover, stronger interactions between monomeric proteins and amylose/short-branch starch via glycosidic and hydrogen bonds were found in 5 + 10 dough during starch pasting and retrogradation. The findings demonstrate the feasibility of optimizing the texture and digestibility of wheat-based food products by regulating the behaviors and interactions of proteins and starch during dough processing.
Keywords: Gluten network; High-molecular-weight glutenin subunits; Mixolab; Protein–starch interaction; Starch gelatinization.
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