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Updated: Feb 14, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
Effects of endogenous walnut pellicle polyphenols on the structure and functional properties of walnut meal isolate
Yunhua Cao1, Yanmei Deng1, Guohui Yuan1
1College of Biological and Food Engineering, Southwest Forestry University, Kunming 650224, China.
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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