LAUSR

Anthocyanins are abundant in purple corn and beneficial to human health. Soybean protein isolate-7s (SPI-7s) could enhance the stability of anthocyanins. The stable system of soybean protein isolate-7s and delphinidin-3-O-glucoside complex (SPI-7s-D3G) was optimized using the Box-Behnken design at pH 2.8 and pH 6.8. Under the condition of pH 2.8, SPI-7s effectively improved the sunlight-thermal stabilities of delphinidin-3-O-glucoside (D3G). The thermal degradation of D3G conformed to the first order kinetics within 100 min, the negative enthalpy value and positive entropy value indicated that interaction was caused by electrostatic interaction, and the negative Gibbs free energy value reflected a spontaneous interaction between SPI-7s and D3G. The interaction of SPI-7s-D3G was evaluated by ultraviolet visible spectroscopy, circular dichroism spectroscopy and fluorescence spectroscopy. The results showed that the maximum absorption peak was redshifted with increasing the α-helix content and decreasing the β-sheet contents, and D3G quenched the intrinsic fluorescence of SPI-7s by static quenching. There was one binding site in the SPI-7s and D3G stable system. The secondary structure of SPI-7s had changed and the complex was more stable. The stabilized SPI-7s-D3G will have broad application prospects in functional foods.