Spectroscopic Studies on the Interaction of Rutin and Lysozyme
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Abstract:
The interaction of rutin with lysozyme (LYZ) was studied in simulating physiological condition (pH 7.40) at 298 K, 304 K and 310 K by ultraviolet-vis (UV) absorption and fluorescence spectroscopy. The results showed that rutin quenched the endogenous fluorescence of LYZ via a static quenching procedure and the interaction between them was a spontaneous process. The number of binding sites was approximately 1. Van der Waals' forces and hydrogen bonds played major roles in stabilizing rutin-LYZ complex, and the distance between the donor and acceptor was 4.02 nm (298 K). The UV absorption, synchronous fluorescence and three-dimensional fluorescence spectra showed that the conformation of LYZ became more tightly packed. The turbidimetric analysis showed that rutin decreased LYZ activity. Rutin may be bad for the hydrogen-bonding receptor catalysis activity of Asp-52 by affecting the micro-environment of lysozyme activity site (Asp-52).
