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Plant protein‐dietary polyphenol interactions: Implications for protein structural and functional properties and digestibility

Mylvaganam, Harthika, Nurkolis, Fahrul, Tsopmo, Apollinaire·2025·Food Chemistry International
DOI 10.1002/fci2.70013
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Abstract

The interaction between plant proteins and dietary polyphenols has garnered significant interest due to its impact on the structural, functional, and digestibility properties of proteins. This review explores the mechanisms underlying protein–polyphenol interactions, including noncovalent (hydrogen bonding, hydrophobic interactions, and electrostatic forces) and covalent bonding, and their implications on structural and functional properties of proteins and their digestibility. Various factors influencing these interactions, such as polyphenol structure, protein composition, temperature, and pH, are discussed. The review examines data on the impact of polyphenols on protein digestibility, shedding light on the mechanisms underlying these modifications and emphasizing the need for a thorough understanding of these processes. It further highlights the role of polyphenols on digestive enzymes, which can either enhance or hinder their enzymatic activities. A structural and molecular levels elucidation of these interactions provides valuable insights for enhancing the functionality and efficacy of plant‐based proteins in food applications.

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  • Legume and oat proteins provide the more direct structural and colloidal comparison for interpreting pseudocereal protein functionality.

    “legume and oat proteins provide the more direct structural and colloidal comparison for interpreting pseu­ docereal protein functionality (Graziano et al., 2022; Mylvaganam et al., 2025; Yan et al., 2025).”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Mylvaganam et al., 2025

    The Introduction and the protein–polyphenol table discuss structural and functional properties of legume proteins, including pea and soy. They do not establish that legume and oat proteins are a more direct comparison for interpreting pseudocereal functionality; the oat-related reference concerns phenolics rather than oat protein structure or colloidal properties. No page numbers are available in our copy. (LLM, conf=0.79)

    Experimental — accuracy not yet measured

  • Genetic polymorphisms, isoforms, and processing-derived modifications adjust charge, hydrophobicity and redistribute aggregation, so the same nominal isolate can map to different SEC and DLS states, ζ-potential and interfacial behaviors.

    “Genetic polymorphisms, isoforms, and processing-derived modifications adjust charge, hydrophobicity and redistribute aggrega­ tion, so the same nominal isolate can map to different SEC and DLS states, ζ -potential and interfacial behaviors (Mylvaganam et al., 2025; Yan et al., 2025).”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Mylvaganam et al., 2025

  • The ingredient is a proteoform ensemble rather than a single molecule, which is a persistent reason why protein datasets diverge across studies.

    “A persistent reason why protein datasets diverge across studies is that the ingredient is a proteoform ensemble rather than a single molecule.”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Mylvaganam et al., 2025

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Cited by

Sorted by citations

Authors
Mylvaganam, H., Nurkolis, F., & Tsopmo, A.
Affiliations
  • Food Science Department of Chemistry Carleton University Ottawa Ontario Canada
  • Faculty of Medicine Universitas Airlangga Surabaya Indonesia
ORCID
Venue
Food Chemistry International
Publisher
Wiley
Published
2025-06
Volume
1
Issue
2
Pages
110-125
ISSN
3065-9027
DOI
10.1002/fci2.70013
Cited by
25
References
0
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor, 60 d)

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