Journal of Thermal Analysis and Calorimetry

, Volume 87, Issue 2, pp 453–456 | Cite as

Interaction of a homologous series of n-alkyl trimethyl ammonium bromides with eggwhite lysozyme

Microcalorimetric and spectroscopic study
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Abstract

The interaction of a series of n-alkyl trimethyl ammonium bromides (C12, C14 and C16) with egg white lysozyme have been studied using fluorescence and UV-Vis spectroscopies and isothermal titration calorimetry (ITC). The trend of variation of molar absorptivity at 281 nm, quantum yields (λex=281 nm) and heat of interaction with respect to surfactant concentration, were measured. The spectrophotometric results show that the hydrophobic interactions have a major role in denaturation mechanism and it would be increased with increasing in hydrocarbon tail length of surfactant. The ITC results indicated the two-step mechanism for unfolding of lysozyme due to its interaction with surfactants.

Keywords

absorption spectroscopy cationic surfactants fluorescence spectroscopy ITC lysozyme unfolding 

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Copyright information

© Springer-Verlag 2007

Authors and Affiliations

  • A. K. Bordbar
    • 1
  • R. Hosseinzadeh
    • 1
    • 2
  • M. H. Norozi
    • 1
  1. 1.Laboratory of Biophysical Chemistry, Department of ChemistryUniversity of IsfahanIsfahanIran
  2. 2.Food and Chemical Analysis Research Laboratory, Jahad-E-DaneshgahiUrmia UniversityUrmiaIran

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