Effect of heat treatment on conformation and aggregation properties of wheat bran dietary fiber-gluten protein

To understand the heat mediated cross-linking mechanism of gluten in the presence of wheat bran dietary fiber (WBDF), the effect of heat treatment on conformation and aggregation properties of wheat bran dietary fiber-gluten protein was comparatively investigated in this study. The results showed G' and G" increased after adding WBDF, then decreased after heating. The SE-HPLC, chemical interaction and surface hydrophobicity analysis revealed the WBDF participated in the rearrangement of intermolecular interactions and induced depolymerization behavior behavior of gluten via disulfide and non-covalent bonds at low temperatures (25 °C and 60 °C), but heating (at 95 °C) promoted these interactions via disulfide bonds. Besides, changes in the secondary structure of gluten protein induced by WBDF during heating were correlated with the steric hindrance and hydroxyl groups on WBDF. These results suggested that WBDF impeded the cross-linking and aggregation of gluten through the rearrangement of chemical bonds and physical entanglements, then this effect was weakened at high temperatures, most likely by improving the disulfide bonds among gluten proteins. This study consummates the understanding of the cross-linking mechanisms of gluten with WBDF during heating, and provides the theoretical basis for improving the quality and acceptability of whole wheat-based products.