ArticleFood chemistry: X2025
Impacts of kaempferol on α-dicarbonyls mediated protein modification during simulated heat-treatment of β-lactoglobulin.
Article in Food chemistry: X, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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.
- Inhibitory Effects of Grape Seed Extract and Epicatechin on Malondialdehyde-Mediated Protein Lipoxidation.Journal of food science · 2026Article
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11 authors.
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Abstract
Thermal processing of dairy products generates α-dicarbonyl compounds such as methylglyoxal (MGO) and glyoxal (GO), which are key precursors of advanced glycation end products (AGEs). This study presents an integrated assessment of kaempferol (Kae), a flavonol polyphenol, in modulating MGO/GO-mediated AGEs formation and physicochemical alterations in β-lactoglobulin (β-LG). Kae (0.1-2 mM) dose-dependently reduced MGO/GO (1 mM)-mediated formation of fluorescent-AGEs and glycoxidation products. Further loss of protein sulfhydryl content, surface hydrophobicity and intrinsic tryptophan fluorescence were observed at Kae concentration of 2 mM, showing concentration-related dual effects of Kae. Western blot analysis revealed the binding of MGO/GO to β-LG was interrupted by Kae. Targeted sequestration of MGO resulting in the formation of mono-/di-MGO-Kae was confirmed by LC/MS. Molecular docking simulation showed Kae's preferential binding to β-LG, shielding potential glycation sites from MGO/GO. These findings collectively suggest a mitigation strategy utilizing phenolic nucleophiles to counteract MGO/GO-mediated modifications in dairy proteins.
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