Journal of Thermal Analysis and Calorimetry

, Volume 87, Issue 1, pp 143–147

Thermodynamic study of the thermal denaturation of a globular protein in the presence of different ligands

  • Elena Blanco
  • J. M. Ruso
  • J. Sabín
  • G. Prieto
  • F. Sarmiento
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DOI: 10.1007/s10973-006-7843-4

Cite this article as:
Blanco, E., Ruso, J.M., Sabín, J. et al. J Therm Anal Calorim (2007) 87: 143. doi:10.1007/s10973-006-7843-4

Abstract

By means of difference UV-Vis spectra, the thermal denaturation of catalase has been studied in the presence of different surfactants: sodium perfluorooctanoate, sodium octanoate and sodium dodecanoate. These results indicate that hydrogenated surfactants play two opposite roles in the folding and stability of catalase, they act as a structure stabiliser at a low molar concentrations (enhancing Tm) and as a destabilizer at a higher concentrations (diminishing Tm). Meanwhile sodium perfluorooctanoate enhances Tm in the whole concentration range. An approach for the determination of the heat capacity, enthalpy and entropy has been made, finding that for the three studied surfactants, at all concentrations, the enthalpy term dominates the entropy term.

Keywords

catalase ligands thermal unfolding thermodynamics 

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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