Work

Impacts of kaempferol on α-dicarbonyls mediated protein modification during simulated heat-treatment of β-lactoglobulin

Year: 2025

Type: article

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. • Kae could interrupt the binding of MGO/GO to β-LG. • Direct scavenging of MGO by Kae was confirmed by the formation of Kae-MGO adducts. • Kae works as a sacrificial nucleophile in competitive inhibition of MGO/GO-induced protein modification. • Phenol-protein interactions contribute to protein physicochemical changes dose-dependently in the presence of MGO/GO.

Source: Food Chemistry X

DOI: 10.1016/j.fochx.2025.103247