Study on the interaction and functional properties of Dolichos lablab L. protein-tea polyphenols complexes

Tea polyphenols (TP) and plant proteins are significant materials in the food industry, the interactions between them are beneficial for their stability, functional properties, and biological activity. In this study, the mechanism and interaction between Dolichos lablab L. protein (DLP) obtained from nine treatments and three tea polyphenol monomers (EGCG, ECG, and EGC) were investigated. The results showed that the fluorescence of DLP was noticeably quenched and exhibited static quenching after the addition of polyphenols. DLP exhibited 1-2 binding sites for EGCG and ECG, but weakly binding to EGC (<1). The binding sites of DLP-TP were found to be in close proximity to the tyrosine residues, primarily interacting through hydrophobic interactions, van der Waals forces, and hydrogen bonds. The antioxidant capacity of DLP-TP compound was significantly improved after digestion. ECG showed a strong resistance to intestinal digestion. Compared with ECG (653.456 μg/mL), the content of free tea polyphenols of 20/40 kHz-ECG after digestion was 732.42 μg/mL. DLP-TP complexes significantly improved the storage stability, thermal stability, and bioaccessibility of tea polyphenols. The interaction between TP and DLP, as a protein-polyphenol complex, has great potential for application in preparing emulsion delivery systems due to their antioxidant activity and improved stability.