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

G Rezaei Behbehani, A Taherkhani, A A Saboury and A A Divsalar

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.