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Elucidating the interaction mechanism of rutin with β-casein and β-lactoglobulin: A comprehensive analysis using
Hailin Wang1, Leiwen Xiang1, Zhuangwei Zhang2
1College of Food and Bioengineering, Fujian Polytechnic Normal University, Fuqing, Fujian, China; Fujian Province-Indonesia Marine Food Joint Research and Development Center, College of Food and Bioengineering, Fujian Polytechnic Normal University, Fuqing, Fujian, China.
Abstract:
Polyphenol-protein interactions are crucial for food processing, nutrition, and functional properties. This study investigates the interaction between rutin and β-casein (β-CAS) or β-lactoglobulin (β-LG) using multispectral analysis, molecular docking, and molecular dynamics (MD) simulations. Fluorescence spectroscopy reveals that rutin binds spontaneously (ΔG < 0) to β-CAS and β-LG, forming complexes with binding constants (Ka) at 298 K of 42.500 × 103 and 2.101 × 103 L·mol-1, respectively, and at 308 K of 5.814 × 103 and 4.350 × 103 L·mol-1. Multispectral analysis and microscopy reveal complex formation and changes in the proteins' secondary, crystalline, and microstructures. Molecular docking and MD simulations verify complex stability, showing heightened binding affinity between rutin and β-CAS. These results validate hydrophobic interactions and hydrogen bonding as the main forces between rutin and the two proteins. These findings offer insights for using milk proteins as rutin carriers and support potential food industry application.
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