首页|Novel insights into the interaction mechanism of 5-hydroxymethyl-2-fur-aldehyde with beta-casein and its effects on the structure and function of beta-casein
Novel insights into the interaction mechanism of 5-hydroxymethyl-2-fur-aldehyde with beta-casein and its effects on the structure and function of beta-casein
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NSTL
Elsevier
5-Hydroxymethyl-2-furaldehyde (5-HMF) in dairy food products generated via Maillard reaction may bring health risks. Herein, the interaction of 5-HMF with beta-casein (beta-CN) and its influences on the structure and function of beta-CN were investigated. 5-HMF was found to quench the inherent fluorescence of beta-CN by a static mode and the binding constant was in the order of magnitude of 10(4) L mol(-1). Thermodynamic analysis indicated that hydrophobic forces played the major role in the interaction. The results of synchronous and threedimensional fluorescence revealed that 5-HMF changed the microenvironment of tyrosine and tryptophan residues and interfered the stability of the polypeptide backbone structure in beta-CN. Molecular docking revealed that 5-HMF bound to the hydrophobic cavity of beta-CN mainly interacting with the amino acid residues Pro196, Val155, Leu163, Phe157 and Leu192. The binding of 5-HMF with beta-CN caused partial unfolding of beta-CN conformation, resulting in the increase in surface hydrophobicity and emulsifiability, and decrease in emulsification stability of beta-CN, thereby reducing the solubility of beta-CN. The study might facilitate the comprehensive understanding of 5-HMF affecting the structure and functional properties of beta-CN.
NSTL
Elsevier
