Alterations in the multilevel structure and depolymerization behavior of gluten induced by selenium in fermented dough

This study was conducted to evaluate the alterations of multilevel structure of gluten induced by selenium (Se) and their relationship with the properties of the fermented dough. The results of molecular weight distributions indicated that the degree of gluten aggregation decreased as the Se content in the fermented dough increased. Moreover, the elevated Se content led to a higher percentage of beta-sheet in the dough proteins, indicating a more stable structure after depolymerization. Intermolecular interactions indicated that Se disrupted covalent cross -linking between gluten by affecting disulfide (SS) bonds. The levels of glutathione (GSH), free sulfhydryl and SS bond in the dough increased with increasing Se content. This suggested that more GSH was produced by Se induced yeast, which reacted with intermolecular SS in gluten, resulting in reduced gluten cross-linking. Meanwhile, Se affected the viscoelasticity and enhanced the height of the fermented dough. Improved quality of the steamed bread was found with even pore distributions and reduced hardness. This study has the potential to expand the application of Se in the fermented food industry and offer practical ways to increase Se consumption in Se-deficient areas.