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Exploring the binding mechanism and functional properties of lactoferrin-berberine complex: Based on multispectral
Si-Jie Wu1, Ran Feng1, Ran Meng1
1Engineering Research Center of Bio-process, Ministry of Education, Hefei University of Technology, 193 Tunxi Road, Hefei, Anhui 230009, PR China; School of Food and Biological Engineering, Hefei University of Technology, 193 Tunxi Road, Hefei, Anhui 230009, PR China.
Abstract:
Denaturation and/or aggregation of proteins under adverse environmental conditions can greatly impair their bioactivity and functional properties. Based on this, this study aims to improve the functional properties of lactoferrin by complexing with berberine and investigate the mechanism using multispectral techniques, molecular docking and dynamics simulations. The results showed that berberine bound to lactoferrin through hydrogen bonding and van der Waals forces and altered its conformation, surface hydrophobicity, amino acid microenvironment, and secondary structure. Molecular docking and dynamics simulations further revealed that berberine inhibited the drastic changes in the lactoferrin structure, contributing to the complex stability. Consequently, the denaturation temperature and degradation temperature (224 °C to 230 °C) and the tolerance to extreme pH, high temperature, and ions of the lactoferrin-berberine complex were improved. This study systematically revealed the mechanism of berberine to improve the functional properties of lactoferrin, contributing to the development and application of novel functional ingredients.
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