Exploring the impact of selenium-enriched peptides from yeast autolysate on dough properties: Insights into mechanisms from gluten perspectives

This study investigated the impact of Selenium (Se)-enriched yeast autolytic peptides (SeYAP) with different Se levels on dough properties as well as the related mechanism by focusing on gluten. SeYAP prolonged the dough's development time by up to 131 % and stability time by up to 28 %. It also decreased dough's viscoelasticity and rendered dough softer. Additionally, SeYAP diminished the binding capacity of dough to water and augmented the fluidity of water. Protein composition, disulfide bonds and fluorescence spectroscopy revealed that SeYAP could induce depolymerization of glutenin aggregate through sulfhydryl/disulfide bond exchange and hydrophobic interactions. Seven Se-enriched peptides were identified from the fraction with strong ability to depolymerize gluten. Specifically, six peptides contained selenocysteine, while another peptide contained selenomethionine. Molecular docking indicated that Se-enriched peptides could interact with amino acids (such as glutamine, tyrosine and proline) in gluten via hydrophobic interactions and/or hydrogen bonds.