Journal of Thermal Analysis and Calorimetry

, Volume 87, Issue 1, pp 211–215

Thermal stability of lysozyme and myoglobin in the presence of anionic surfactants

  • Elena Blanco
  • J. M. Ruso
  • J. Sabín
  • G. Prieto
  • F. Sarmiento
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DOI: 10.1007/s10973-006-7842-5

Cite this article as:
Blanco, E., Ruso, J.M., Sabín, J. et al. J Therm Anal Calorim (2007) 87: 211. doi:10.1007/s10973-006-7842-5

Abstract

The interactions of lysozyme and myoglobin with anionic surfactants (hydrogenated and fluorinated), at surfactant concentrations below the critical micelle concentration, in aqueous solution were studied using spectroscopic techniques. The temperature conformational transition of globular proteins by anionic surfactants was analysed as a function of denaturant concentration through absorbance measurements at 280 nm. Changes in absorbance of protein-surfactant system with temperature were used to determine the unfolding thermodynamics parameters, melting temperature, Tm, enthalpy, ΔHm, entropy, ΔSm and the heat capacity change, ΔCp, between the native and denatured states.

Keywords

lysozyme myoglobin thermal denaturation thermodynamics UV absorbance 

Copyright information

© Springer-Verlag 2007

Authors and Affiliations

  • Elena Blanco
    • 1
  • J. M. Ruso
    • 1
  • J. Sabín
    • 1
  • G. Prieto
    • 1
  • F. Sarmiento
    • 1
  1. 1.Group of Biophysics and Interfaces, Department of Applied Physics, Faculty of PhysicsUniversity of Santiago de CompostelaSantiago de CompostelaSpain

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