Thermal stability of lysozyme and myoglobin in the presence of anionic surfactants
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.
Keywordslysozyme myoglobin thermal denaturation thermodynamics UV absorbance
Unable to display preview. Download preview PDF.
- 4.E. D. Goddard, Interactions of Surfactants with Polymers and Proteins, CRC Press, 1993.Google Scholar
- 6.Moosavi-Movahedi, AA 2005J. Iranian Chem. Soc.2189Google Scholar
- 7.A. A. Saboury, H. Ghourchaei, M. H. Sanati, M. S. Atri and M. Rezaei-Tawirani, J. Therm. Anal. Cal., OnlineFirst, DOI:10.1007/s10973-006-7533-2.Google Scholar
- 17.Becktel, WJ 1987Biochemistry261859Google Scholar