Paper Title:
Thermal Study of Lysozyme Binding with β-Cyclodextrin
  Abstract

Effects of β-cyclodextrin, βCD, on refolding of lysozyme was investigated at pH 12 employing isothermal titration calorimetry (ITC) at 300K in 30mM Tris buffer solution. βCD was employed as an anti-aggregation agent and the heats obtained for lysozyme+βCD 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 βCD.

  Info
Periodical
Chapter
Chapter 10: Biomedical Manufacturing
Edited by
Wu Fan
Pages
1966-1969
DOI
10.4028/www.scientific.net/AMM.110-116.1966
Citation
G. R. Behbehani, L. Barzegar, "Thermal Study of Lysozyme Binding with β-Cyclodextrin", Applied Mechanics and Materials, Vols. 110-116, pp. 1966-1969, 2012
Online since
October 2011
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