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A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
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Pea protein isolate-quercetin covalent complexes: Structure, functionality, and molecular mechanisms underlying

Khubaib Ali1, Mingze Xu1, Qing Yin1

  • 1College of Food Science and Engineering, Yangzhou University, Yangzhou, Jiangsu 225127, China.

Food Chemistry
|March 19, 2026
PubMed
Summary

Arginine-modified pea protein isolate conjugated with quercetin enhances antioxidant and emulsifying properties. This novel complex improves the stability and oxidative resistance of myofibrillar protein emulsions.

Keywords:
AntioxidationArginine modificationEmulsifying propertyMolecular dynamic simulationPea protein isolateQuercetin grafting

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Area of Science:

  • Food Science
  • Biochemistry
  • Materials Science

Background:

  • Pea protein isolate (PPI) is a valuable protein source.
  • Enhancing PPI's functional properties, like antioxidant and emulsifying capabilities, is crucial for food applications.
  • Quercetin is a potent antioxidant polyphenol with limited bioavailability and stability.

Purpose of the Study:

  • To develop a novel PPI-Arg-quercetin complex with improved functional properties.
  • To investigate the synergistic effects of arginine modification and quercetin conjugation on PPI.
  • To evaluate the performance of the complex in myofibrillar protein (MP) composite emulsions.

Main Methods:

  • Pea protein isolate (PPI) was modified with arginine (Arg) and conjugated with quercetin via laccase catalysis.
  • Total phenol content and polyphenol binding rate were determined.
  • The complex's performance was assessed in myofibrillar protein (MP) composite emulsions, analyzing particle size, Zeta potential, and physical stability.
  • Oxidative stability was evaluated using biochemical assays.
  • Confocal laser scanning microscopy (CLSM) visualized droplet distribution.
  • Molecular docking and dynamics simulations confirmed interactions.

Main Results:

  • The 0.2% Arg modified PPI conjugated with quercetin (PA2-Q) showed the highest total phenol content and polyphenol binding rate.
  • Arg modification and quercetin grafting synergistically enhanced antioxidant activity.
  • PA2-Q significantly improved emulsifying activity, reduced particle size, increased Zeta potential, and enhanced physical stability in MP emulsions.
  • CLSM confirmed uniform droplet distribution and reduced aggregation in PA2-Q treated emulsions.
  • PA2-Q improved oxidative stability by increasing free sulfhydryl content and decreasing carbonyl and dityrosine content, effectively inhibiting oil oxidation.
  • Molecular simulations indicated stable interactions mediated by hydrogen and hydrophobic forces.

Conclusions:

  • Arginine modification and quercetin conjugation create a synergistic PPI-Arg-quercetin complex with superior antioxidant and emulsifying properties.
  • The developed complex significantly enhances the physical and oxidative stability of myofibrillar protein emulsions.
  • This study presents a promising strategy for improving the functionality of plant-based proteins for food applications.