Interaction of soy protein isolate with hydroxytyrosol based on an alkaline method: Implications for structural and functional properties.

[Display omitted] • The soy protein isolate covalently bound to hydroxytyrosol by alkaline method. • The addition of HT transformed the structure of SPI into a disordered one. • SPI-HT adducts have enhanced emulsifying, foaming and antioxidant properties. • The adducts with different concentrations of HT have different optimal properties. This study investigated the effect of different concentrations of hydroxytyrosol (HT) covalently bound to soy protein isolate (SPI) by the alkaline method on the structure and function of the adducts. The amount of polyphenol bound to SPI first increased to a maximum of 42.83 % ± 1.08 % and then decreased. After the covalent binding of HT to SPI, turbidity and in vitro protein digestibility increased and decreased significantly with increasing concentrations of HT added, respectively, and the structure of SPI was changed. The adducts had a maximum solubility of 52.52 % ± 0.33 %, and their water holding capacity reached a maximum of 8.22 ± 0.11 g/g at a concentration of 50 μmol/g of HT. Covalent modification with HT significantly increased the emulsifying and foaming properties and antioxidant activity of SPI; the DPPH and ABTS radical scavenging rates increased by 296.89 % and 33.80 %, respectively, at a concentration of 70 μmol/g of HT. [ABSTRACT FROM AUTHOR]