Establishing a novel covalent complex of wheat gluten with tea polyphenols: Structure, digestion, and action mechanism.

Plant-based proteins represent a more sustainable alternative, the approaches to modify and enhance their functionality and application are focused on. Covalent interaction could significantly modify the structure and function properties of protein. This study investigated the effects of covalent interaction between wheat gluten and tea polyphenols on the structure, aggregation, stability, and digestive properties of their covalent complex, as well as the possible action mechanism. The results showed that tea polyphenols could interact with gluten via covalent bonds (CN and/or CS), while tea polyphenols also acted as a bridge connecting gluten molecules, thus making covalent complex to show the larger particle sizes. This covalent interaction significantly changed the secondary structure, tertiary structure, and surface hydrophobicity of gluten. Moreover, covalent complex exhibited the high polyphenols bioaccessibility during in vitro digestion. The peptide bonds of covalent complex were mainly broken in gastric digestion, while the covalent bonds between tea polyphenols and gluten were completely destroyed in intestinal digestion. In addition, their digestates exhibited excellent antioxidant capability. All results suggest that wheat gluten have potential to prepare functional carrier for transporting active compounds and protecting them during digestion.