alexa Calorimetric Study on the Binding of Lysozyme Upon Interaction With β-Cyclodextrin
ISSN: 2157-7544

Journal of Thermodynamics & Catalysis
Open Access

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Research Article

Calorimetric Study on the Binding of Lysozyme Upon Interaction With β-Cyclodextrin

G Rezaei Behbehani1*, A Taherkhani2,3, A A Saboury4 and A A Divsalar4,5
1Chemistry Department, faculty of science, Islamic Azad University, Takestan branch, Takestan, Iran
2Member of Young Researchers Club, Islamic Azad University, Takestan Branch, Takestan, Iran
3Department of Physics, Islamic Azad University, Takestan Branch, Takestan, Iran
4Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
5Department of Biological Sciences, Tarbiat Moallem University, Tehran, Iran
Corresponding Author : Dr. G Rezaei Behbehani
Chemistry Department, faculty of science
Islamic Azad University, Takestan branch, Takestan, Iran
E-mail: [email protected]
Received November 26, 2010; Accepted December 29, 2010; Published December 31, 2010
Citation: Behbehani GR, Taherkhani A, Saboury AA, Divsalar A A (2010) Calorimetric Study on the Binding of Lysozyme Upon Interaction With β-Cyclodextrin. J Thermodyn Catal 1:103. doi:10.4172/2157-7544.1000103
Copyright: © 2010 Behbehani GR, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Abstract

Effects of ?-cyclodextrin, ?CD, on refolding of lysozyme was investigated at pH 12 employing isothermal titration calorimetry (ITC) at 300K in 30mM Tris buffer solution. ?CD was employed as an anti-aggregation agent and the heats obtained for lysozyme+?CD interactions are reported and analyzed in terms of the extended solvation model. It was indicated that there are two sets of identical and non-cooperative sites for ?CD.

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