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Whey protein isolate-reuterin complexes: Structure and functional properties.

Mao-Cheng Sun1, Ying-Di Wang1, Jie-Ting Wang1

  • 1College of Food Science and Engineering, Changchun University, Changchun 130022, China.

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|October 6, 2025
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Summary

Whey protein isolate (WPI) complexed with reuterin, enhancing its structure and functionality. This protein modification improved emulsifying and foaming properties without compromising reuterin's antibacterial activity.

Keywords:
Functional propertiesReuterinStructural characteristicsWhey protein isolate

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Area of Science:

  • Food Science
  • Biochemistry
  • Protein Chemistry

Background:

  • Whey protein isolate (WPI) is a valuable protein source with functional properties.
  • Reuterin is a compound with potential biological activities.
  • Understanding protein-ligand interactions is crucial for food ingredient development.

Purpose of the Study:

  • To investigate the structural and functional changes in whey protein isolate (WPI) when complexed with reuterin.
  • To determine the binding interactions between reuterin and WPI.
  • To evaluate the impact of complex formation on WPI's functional properties and reuterin's bioactivity.

Main Methods:

  • Complex formation was induced at varying reuterin concentrations.
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was used to confirm complex formation.
  • Spectroscopic techniques (fluorescence, FTIR) and molecular docking elucidated binding mechanisms.
  • Physicochemical properties (surface hydrophobicity, particle size, zeta potential) were analyzed.
  • Scanning electron microscopy (SEM) visualized structural changes.
  • Emulsifying activity, foaming capacity, and antibacterial activity were assessed.

Main Results:

  • SDS-PAGE confirmed the formation of WPI-reuterin complexes.
  • Binding involved hydrophobic interactions and hydrogen bonding, leading to partial WPI unfolding.
  • Complexation resulted in more ordered and compact structures compared to native WPI.
  • Emulsifying activity increased by 48.78% and foaming capacity by 12.15%.
  • Reuterin retained its antibacterial activity within the complexes.

Conclusions:

  • Reuterin effectively modifies the structure and enhances the functional properties of WPI.
  • The WPI-reuterin complexes offer improved emulsification and foaming capabilities.
  • This study provides a theoretical foundation for using reuterin as a protein modifier in food applications.