期刊
MOLECULES
卷 26, 期 6, 页码 -出版社
MDPI
DOI: 10.3390/molecules26061721
关键词
soy protein isolate; hydrolysate; cyanidin-3-O-glucoside; noncovalent interaction; antioxidant capacity
资金
- National Natural Science Foundation of China [31771978]
- Six Talent Peaks Project in Jiangsu Province [NY-095]
- National First-Class Discipline Program of Food Science and Technology [JUFSTR20180201]
- Innovation and Exploration Fund of State Key Laboratory of Food Science and Technology, Jiangnan University [SKLFZZB-201904]
- Fundamental Research Funds for the Central Universities [JUSRP21802]
The study revealed that SPI and SPIHs interacted with C3G mainly through hydrophobic interactions, with SPI showing stronger binding affinity than SPIHs. The interaction with C3G did not significantly alter the secondary structures of the proteins, but decreased their surface hydrophobicity and average particle size, leading to an antagonistic effect on the antioxidant capacity of the complex system.
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.
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