Modulation of gluten network structure, dough rheology, and Chinese steamed bread quality by wheat bran albumin through molecular interactions with gluten proteins.

Impacts of wheat bran albumin (WBA) upon dough rheological properties alongside Chinese steamed bread quality were investigated, with emphasis on its interactions with gluten proteins and gluten network formation. WBA reduced dough viscoelasticity while significantly enhancing extensibility up to 85% with only 0.6% WBA addition, resulting in a 28.4% increase in specific volume of steamed bread. Molecular structure analysis revealed WBA induced gluten protein disaggregation by disrupting disulfide bonds in glutenin, and concomitantly promoted the aggregation through newly formed disulfide bonds and dityrosine cross-links involving gliadin subunits. These corresponded well with the increased endpoints rate and junction density of gluten network. At WBA addition ≤0.6%, protein aggregation predominated, accompanied by synergistically enhanced hydrophobic and hydrogen bonds interactions, together with super alterations in protein secondary and tertiary conformations. Overall, WBA, as a non-gluten protein, exhibited strong potential to regulate gluten network structure and improve flour processing performance.