Insight into the binding mechanism of rutin and lysozyme: Based on spectroscopy and molecular simulation technology

Lysozyme (LYZ) is an excellent natural food preservative and can also be used as a bioactive carrier loading small molecules to enhance its stability and antioxidant properties. This research explored the intricate mechanism of interaction between LYZ and rutin. Multiple spectroscopic techniques was used first to confirm that rutin caused a fluorescence burst in LYZ. LYZ amino acid microenvironment was altered. The main driving forces driving the formation of the complex between rutin and LYZ were hydrogen bonding and van der Waals forces. In addition, the incorporation of rutin improved the overall stability and oxidation resistance of the complexes. The results of molecular docking and molecular dynamics simulation further show that rutin and LYZ are stably bound by hydrogen bonds and other interactions. The investigation contributed precious information for the development of novel natural preservatives and the design of advanced small molecular carriers.