Investigation of Binding Properties of Umbelliferone (7Hydroxycoumarin) to Lysozyme


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Gok E.

JOURNAL OF FLUORESCENCE, vol.23, no.2, pp.333-338, 2013 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 23 Issue: 2
  • Publication Date: 2013
  • Doi Number: 10.1007/s10895-012-1151-0
  • Title of Journal : JOURNAL OF FLUORESCENCE
  • Page Numbers: pp.333-338

Abstract

The binding interaction of lysozyme and umbelliferone (7hydroxcoumarin, 7HC) was investigated by UV-vis absorption and fluorescence quenching. It was obtained from fluorescence spectra that the fluorescence quenching of lysozyme by 7HC was probably a result of the formation of lysozyme-7HC complex and binding parameters were determined according to the Stern-Volmer equation. The effects of various common metal ions on the binding were also studied. The thermodynamic parameters were calculated at different temperatures which indicated that hydrophobic interaction. The binding distance (r) between the donor (lysozyme) and the acceptor (7HC) was 3.81 nm based on the Forster theory of non-radioactive resonance energy transfer.