Study of four polyphenol-Coregonus peled (C. peled) myofibrillar protein interactions on protein structure and gel properties

Autor: Xin Guo, Yabo Wei, Pingping Liu, Xiaorong Deng, Xinrong Zhu, Zhouping Wang, Jian Zhang
Jazyk: angličtina
Rok vydání: 2024
Předmět:
Zdroj: Food Chemistry: X, Vol 21, Iss , Pp 101063- (2024)
Druh dokumentu: article
ISSN: 2590-1575
DOI: 10.1016/j.fochx.2023.101063
Popis: The effects of four polyphenols—chlorogenic acid (CA), gallic acid (GA), epicatechin gallate (ECG), and epigallocatechin gallate (EGCG) on the structure, gel properties, and interaction mechanisms of myofibrillar protein (MP) were studied. The changes in MP structure with polyphenols were analyzed using circular dichroism. The ultraviolet and fluorescence spectra and thermodynamic analysis indicated that the type of binding between the four polyphenols with the MP was static quenching of complex formation. GA had a more pronounced effect on improving MP gel properties. Finally, molecular docking determined that the affinity of the protein with the four polyphenols was in the order EGCG > ECG > CA > GA, with the main interaction force being hydrophobic interactions and hydrogen bonding, but hydrogen bonding dominates the interaction between GA and the protein. The findings illuminate the mechanism of MP binding to different polyphenols and facilitate the study of polyphenol–protein properties.
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