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The interaction of soy protein isolate (SPI) and its hydrolysates (SPIHs) with cyanidin-3- O -glucoside (C3G) at pH 7.0 were investigated to clarify the changes in the antioxidant capacity of their complexes. The results of intrinsic fluorescence revealed that C3G binds to SPI/SPIHs mainly through hydrophobic interaction, and the binding affinity of SPI was stronger than that of SPIHs. Circular dichroism and Fourier-transform infrared spectroscopy analyses revealed that the interaction with C3G did not significantly change the secondary structures of SPI/SPIHs, while the surface hydrophobicity and average particle size of proteins decreased. Furthermore, the SPI/SPIHs-C3G interaction induced an antagonistic effect on the antioxidant capacity (ABTS and DPPH) of the complex system, with the masking effect on the ABTS scavenging capacity of the SPIHs-C3G complexes being lower than that of the SPI-C3G complexes. This study contributes to the design and development of functional beverages that are rich in hydrolysates and anthocyanins.

molecules/molecules online/molecules annual

Interaction of Soy Protein Isolate Hydrolysates with Cyanidin-3-O-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral Condition