ArticleMolecules (Basel, Switzerland)2025
Enhancement of Physicochemical and Functional Properties of Chicken Breast Protein Through Polyphenol Conjugation: A Novel Ingredient for Protein Supplements.
Article in Molecules (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Impact of Quercetin on the Functional and Structural Properties of Chitooligosaccharide (CHOS)-Enriched Surimi.Gels (Basel, Switzerland) · 2026Article
- Impact of xylose-mediated Maillard reaction on antioxidant capacity and digestibility of alcalase-hydrolyzed porcine liver during simulated canine digestion.Food science of animal resources · 2026Article
- Quality attributes of chicken breast proteins following sequential enzymatic hydrolysis and polyphenol conjugation.Poultry science · 2026Article
- Recent Insights into Protein-Polyphenol Complexes: Molecular Mechanisms, Processing Technologies, Synergistic Bioactivities, and Food Applications.Molecules (Basel, Switzerland) · 2026Review
- The Influence of pH-Driven Interaction Between Soy Protein Isolate and Soy Isoflavones on the Structural and Functional Properties of Their Complexes.Foods (Basel, Switzerland) · 2025Article
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Authors and funding
7 authors.
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Abstract
Polyphenol conjugation has emerged as a promising approach to enhance the technological properties and physiological benefits of food proteins. This study investigated the effects of polyphenol conjugation on the technological properties, antioxidant capacity, and in vitro digestibility of chicken breast (CB) proteins. Conjugation with (-)-epigallocatechin 3-gallate (EGCG) and tannic acid (TA) significantly reduced sulfhydryl content. EGCG conjugates exhibited higher turbidity and greater molecular weight aggregates (>245 kDa). Fourier-transform infrared spectroscopy (FTIR) revealed alterations in protein secondary structures, with shifts in amide I and II bands. Polyphenol conjugation significantly enhanced the water-holding capacity of chicken muscle proteins, particularly for CB-TA (3.29 g/g) and CB-EGCG (3.13 g/g) compared to the control (2.25 g/g). The emulsion stability index improved notably in CB-EGCG (96.23 min) and CB-TA (87.24 min) compared to the control (69.05 min). Color analysis revealed darker and more intense hues for CB-EGCG, while CB-TA maintained a lighter appearance, making it potentially preferable for industrial applications requiring neutral-colored powders. Moreover, polyphenol conjugation could enhance antioxidant capacity, particularly in conjugates with EGCG (
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