ArticleFood chemistry: X2025
Whey protein isolate-reuterin complexes: Structure and functional properties.
Article in Food chemistry: X, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
This study aimed to explore the structural and functional characteristics of complexes that were formed between whey protein isolate (WPI) and reuterin at different concentrations (0-3.12 mg/mL). SDS-PAGE confirmed the formation of the complexes. Fluorescence spectroscopy, FTIR spectroscopy and molecular docking indicated that the binding of reuterin to WPI primarily involved hydrophobic interactions and hydrogen bonding. The results of free sulfhydryl groups, free amino groups, surface hydrophobicity, particle size and zeta potential indicated that reuterin caused partial unfolding of the WPI structure. Scanning electron microscopy showed that the complexes became more ordered and compact compared to native WPI. Additionally, reuterin can increase the emulsifying activity of WPI by 48.78 % and the foaming capacity by 12.15 %, and the formation of the complexes did not affect the antibacterial activity of reuterin. These discoveries serve as a theoretical basis for the employment of reuterin as a modifier for proteins.
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