Studies on the interaction between homological proteins and anthocyanins from purple sweet potato (PSP): Structural characterization, binding mechanism and stability.

Rui Zhang, Shuxin Ye, Ying Guo, Muci Wu, Sijia Jiang, Jingren He

Food chemistry 2023 Jan 30

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The protein-bound anthocyanin complexes are naturally existed in food systems by their spontaneous interaction. In this study, the interaction mechanism of homological proteins (p-PSP) and anthocyanins (FAC-PSP) was investigated to explore the binding characteristic of native protein-bound anthocyanins from purple sweet potato (p-BAC-PSP). The structural characterization, stability and anti-ultraviolet property of p-BAC-PSP were also evaluated. Results revealed that hydrophobic interaction is dominant binding force for forming p-BAC-PSP. The binding resulted in protein secondary structure changes with more β-sheet and lower β-turn, random coil structures. Fluorescence spectroscopy demonstrated that FAC-PSP quenched p-PSP fluorescence in a combination of static and dynamic mode (static dominant) with a binding constant of 105 L/mol reflecting strong affinity of FAC-PSP to p-PSP. Moreover, the complex form exhibited better protective effects on anthocyanins for pH, light, thermal stabilities and higher anti-ultraviolet activity. These findings further expanded the application of anthocyanins as stable, functional food and cosmetic ingredients. Copyright © 2022 Elsevier Ltd. All rights reserved.

Citation

Rui Zhang, Shuxin Ye, Ying Guo, Muci Wu, Sijia Jiang, Jingren He. Studies on the interaction between homological proteins and anthocyanins from purple sweet potato (PSP): Structural characterization, binding mechanism and stability. Food chemistry. 2023 Jan 30;400:134050