ArticleFood chemistry: X2026
Effects of endogenous walnut pellicle polyphenols on the structure and functional properties of walnut meal isolate proteins.
Article in Food chemistry: X, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Protein-Polyphenol Interactions in Specialty Oilseeds: Multiscale Mechanisms, Physicochemical Reshaping, and Advanced Food Applications.Foods (Basel, Switzerland) · 2026Review
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This study aims to investigate how endogenous walnut pellicle polyphenols (WPP) alter the structural and functional properties of walnut protein isolate (WalPI). WPP influence was assessed by adjusting polyphenol content in walnut meal (WM) through treatments that peeled and dephenolized the pellicle. Results showed that WPP decreased the β-sheet content of unpeeled walnut protein isolate (UWalPI), increased random coil structures, and induced structural unfolding. These structural changes raised the water-holding capacity of UWalPI from 1.72 to 2.48 g/g and enhanced foaming capacity and foam stability by 31.12% and 46.44%, respectively. Conversely, surface hydrophobicity declined by 62.9%, oil-holding capacity reduced to 2.44 g/g, and emulsifying capacity, solubility, and thermal stability were compromised. Scanning electron microscopy indicated WPP-induced rearrangement and aggregation, molecular docking simulations predicted interactions between WPP and WalPI. The results clarify the mechanisms of WPP-WalPI interactions and provide strategies for the application of WM and WalPI in food processing.
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