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<p>This study employed representative citrus phenolic acids (ferulic acid, FA; caffeic acid, CA) and flavonoids (naringenin, Nrg; hesperidin, Hsd) as model polyphenols to investigate non-covalent interactions between yeast protein (YP) and structurally diverse polyphenols, and their effects on protein structure and functionality. The results indicated that polyphenol binding to YP was primarily driven by hydrogen bonding and van der Waals forces, with Nrg exhibiting the highest binding affinity. Infrared spectroscopy revealed that polyphenols reduced the α-helix and β-sheet contents of YP. Fluorescence spectroscopy showed that polyphenols modulated the hydrophobic microenvironment around aromatic amino acid residues, inducing conformational changes in the tertiary structure of YP. Moreover, polyphenols shifted YP from ordered to more relaxed conformations, accompanied by decreased surface hydrophobicity, contributing to improved solubility, foaming capacity (FC), emulsion stability index (ESI), and antioxidant activity. Notably, YP–Nrg exhibited the greatest improvement in solubility (34.34%), YP–FA showed the highest FC and ABTS radical scavenging activity (35.67% and 86.68%, respectively), and YP–CA demonstrated the strongest DPPH radical scavenging capacity (88.87%). These findings indicate that structurally distinct polyphenols can modulate YP conformation and functionality, providing a basis for further mechanistic studies. However, this study was limited to in vitro systems, and further validation through in vitro and in vivo studies is required to confirm the proposed interaction mechanisms and their effects on protein structure and function.</p>

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Effects of Representative Citrus Polyphenols on the Structural and Functional Properties of Yeast Protein via Non-Covalent Interactions

  • 期刊论文

  • 发表日期：

    2026年5月7日

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  • Wenyan Du,
  • Jieqiong Yao,
  • Hongyan Zhang,
  • Xianghao Yuan,
  • Siyi Pan

摘要

This study employed representative citrus phenolic acids (ferulic acid, FA; caffeic acid, CA) and flavonoids (naringenin, Nrg; hesperidin, Hsd) as model polyphenols to investigate non-covalent interactions between yeast protein (YP) and structurally diverse polyphenols, and their effects on protein structure and functionality. The results indicated that polyphenol binding to YP was primarily driven by hydrogen bonding and van der Waals forces, with Nrg exhibiting the highest binding affinity. Infrared spectroscopy revealed that polyphenols reduced the α-helix and β-sheet contents of YP. Fluorescence spectroscopy showed that polyphenols modulated the hydrophobic microenvironment around aromatic amino acid residues, inducing conformational changes in the tertiary structure of YP. Moreover, polyphenols shifted YP from ordered to more relaxed conformations, accompanied by decreased surface hydrophobicity, contributing to improved solubility, foaming capacity (FC), emulsion stability index (ESI), and antioxidant activity. Notably, YP–Nrg exhibited the greatest improvement in solubility (34.34%), YP–FA showed the highest FC and ABTS radical scavenging activity (35.67% and 86.68%, respectively), and YP–CA demonstrated the strongest DPPH radical scavenging capacity (88.87%). These findings indicate that structurally distinct polyphenols can modulate YP conformation and functionality, providing a basis for further mechanistic studies. However, this study was limited to in vitro systems, and further validation through in vitro and in vivo studies is required to confirm the proposed interaction mechanisms and their effects on protein structure and function.