The preparation of Tartary buckwheat protein and phenolic extract complex by pH-driven treatment was studied. The phenols identified by HPLC-MS spectrometry mainly include rutin, quercetin and kaempferol. The content of phenol bound to protein was 33.49 and 6.31 mg/g. The FT-IR and fluorescence spectroscopy confirmed that the treatment of pH-driven and combination of phenol can affect the secondary and tertiary structure of the protein. The alteration of free sulfhydryl content indicated that there may be binding between phenol and Cys residue of protein. Molecular docking analysis showed the binding sites of the phenols and protein treated at different pH values were significantly different. Furthermore, In the simulated digestion in vitro, the digestibility of complex was significantly lower than that of protein. Pepsin can promote the antioxidant ability, and have little effect on ADH activation. The above result can play a positive role in the development of the food field.
Keywords: Biological activity; Digestion; Molecular docking; Phenol; Tartary buckwheat protein.
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