ArticleFood chemistry: X2024
Influence of phloretin on acrolein-induced protein modification and physicochemical changes in a dairy protein model.
Article in Food chemistry: X, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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
2 citing papers in PubMed.
- Inhibitory Effects of Grape Seed Extract and Epicatechin on Malondialdehyde-Mediated Protein Lipoxidation.Journal of food science · 2026Article
- Impacts of kaempferol on α-dicarbonyls mediated protein modification during simulated heat-treatment of β-lactoglobulin.Food chemistry: X · 2025Article
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11 authors.
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Abstract
Acrolein (ACR) is an α,β-unsaturated aldehyde with high reactivity towards nucleophiles in proteins. In this study, a typical phenolic compound phloretin (Phl) was employed to counteract protein modification induced by ACR (1 mM) in whey protein isolate (WPI, 10 mg/mL). The addition of Phl (2 mM) significantly reduced ACR-induced surge of protein carbonyls (from 1.65 to 0.65 μmol/mg protein) and loss of protein total sulfhydryl content (from 0.28 to 0.24 μmol/mg protein) whilst contributing to further reductions in protein surface hydrophobicity and intrinsic fluorescence. The incorporation of ACR into WPI was effectively interrupted by Phl as visualized by Western blot. Only 2.87 % of ACR remained in the presence of 2 mM Phl with the generation of Phl-ACR adducts, suggesting Phl could partially alleviate protein modification by scavenging of ACR. These findings could have important implications for employment of natural phenolic nucleophiles against the adverse effects of ACR towards dietary proteins.
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