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Volume 27, Issue 1, Pages 27-34

Fluorescence spectroscopic study on interaction of retinol with β-lactoglobulin in the presence of cetylpyridinium chloride

Mehdi Sahihi,1 Yousef Ghayeb,1 and Abdol-Khalegh Bordbar2,3

1Department of Chemistry, Isfahan University of Technology, Isfahan, Iran
2Department of Chemistry, University of Isfahan, Isfahan, Iran
3Department of Chemistry, University of Isfahan, Isfahan 81746-73441, Iran

Copyright © 2012 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


In our previous study thermodynamic denaturation of bovine β-lactoglobulin variant A (BLG-A), has been investigated in the presence of cetylpyridinium chloride (CPC) as a cationic surfactant. Here, the retinol binding property of BLG was determined at 298 K and pH 8.0 by spectrofluorimeter titration method, in the presence of CPC to elucidate the still unknown structure–function relationship in this protein. Comparison of the results allowed determining the binding of retinol by BLG in the presence of CPC. The two-way chemometrics method was used, to estimate the equilibrium concentration of components by analysis of fluorescence emission spectrum, in order to obtain its equilibrium concentration. The results indicate that the retinol binding properties of BLG do not show significant changes in the presence of this surfactant.