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Article 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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| http://dx.doi.org/10.1016/j.foodchem.2024.141639 | DOI Listing |
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