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Isothermal microcalorimetric study of the pH dependence of the interactions between a cellulase and a beta-blocker
Date
2004-08-01
Author
Gotmar, G
Özen, Can
Serpersu, E
Guiochon, G
Metadata
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The influence of the pH on the complexation equilibria between (S)- or (R)-alprenolol and the cellulase Cel7A was investigated by isothermal titration calorimetry. The results obtained agree with those of previous, similar studies of the same equilibria in which the protein was immobilized on silica particles, packed in a chromatographic column. The association constant and the complexation enthalpy and entropy of the (S)-enantiomer increase with increasing pH. For (R)-alprenolol, the binding is endothermic at all pH values. Thus, for both enantiomers in the pH range 5.5-6.8, the binding is an entropically driven process.
Subject Keywords
Organic Chemistry
,
Analytical Chemistry
,
Biochemistry
,
General Medicine
URI
https://hdl.handle.net/11511/57795
Journal
JOURNAL OF CHROMATOGRAPHY A
DOI
https://doi.org/10.1016/j.chroma.2004.06.089
Collections
Graduate School of Natural and Applied Sciences, Article
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G. Gotmar, C. Özen, E. Serpersu, and G. Guiochon, “Isothermal microcalorimetric study of the pH dependence of the interactions between a cellulase and a beta-blocker,”
JOURNAL OF CHROMATOGRAPHY A
, pp. 49–53, 2004, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/57795.