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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.

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Authors and Affiliations

  1. Laboratory of Biophysical Chemistry, Department of Chemistry, University of Isfahan, Isfahan, Iran, 81746-73441

    A. K. Bordbar, R. Hosseinzadeh & M. H. Norozi

  2. Food and Chemical Analysis Research Laboratory, Jahad-E-Daneshgahi, Urmia University, Urmia, Iran

    R. Hosseinzadeh

Authors
  1. A. K. Bordbar
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  2. R. Hosseinzadeh
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  3. M. H. Norozi
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Correspondence to A. K. Bordbar.

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Bordbar, A.K., Hosseinzadeh, R. & Norozi, M.H. Interaction of a homologous series of n-alkyl trimethyl ammonium bromides with eggwhite lysozyme. J Therm Anal Calorim 87, 453–456 (2007). https://doi.org/10.1007/s10973-005-6906-2

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