ArticleFoods (Basel, Switzerland)2024
Effect of Alkyl Peroxyl Radical Oxidation on the Oxidative Stability of Walnut Protein Emulsions and Their Adsorbed Proteins.
Article in Foods (Basel, Switzerland), 2024. 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.
- Peroxyl radical-mediated oxidative crosslinking of faba and pea proteins: Differential aggregation behavior and implications for protein structuring.Food chemistry: X · 2026Article
- Oxidative aging of plant protein-stabilized emulsions and its impact on carotenoid bioaccessibility.Food chemistry: X · 2026Review
- Combined Ultrasound and NaHCOFoods (Basel, Switzerland) · 2026Article
- Effects of 2,2'-Azobis(2-amidinopropane) dihydrochloride (AAPH) on Functional Properties and Structure of Winged Bean Protein.Foods (Basel, Switzerland) · 2025Article
- Modification approaches of walnut proteins to improve their structural and functional properties: A review.Food chemistry: X · 2024Article
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Authors and funding
4 authors.
Funding
Abstract
Walnuts are high in protein content and rich in nutrients and are susceptible to oxidation during production and processing, leading to a decrease in the stability of walnut protein emulsions. In this paper, the effect of alkyl peroxyl radical oxidation on the stability of walnut protein emulsions is investigated. With the increase of 2,2-azobis (2-methylpropionamidine) dihydrochloride (AAPH) concentration, both its protein and fat were oxidized to different degrees, and the droplets of the emulsion were first dispersed and then aggregated as seen from the laser confocal, and the stability of walnut protein emulsion was best at the AAPH concentration of 0.2 mmol/L. In addition to this, the adsorption rate of adsorbed proteins showed a decreasing and then an increasing trend with the increase in the oxidized concentration. The results showed that moderate oxidation (AAPH concentration: 0-0.2 mmol/L) promoted an increase in protein flexibility and a decrease in the protein interfacial tension, leading to the decrease in emulsion droplet size and the increase of walnut protein emulsion stability, and excessive oxidation (AAPH concentration: 1-25 mmmol/L) weakened protein flexibility and electrostatic repulsion, making the walnut protein emulsion less stable. The results of this study provide theoretical references for the quality control of walnut protein emulsions.
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