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Calorimetric and Spectroscopic investigations οf β-lactoglobulin upon interaction with copper ion

Published online by Cambridge University Press:  19 April 2012

Adeleh Divsalar ,
Sajedeh Ebrahim Damavandi ,
Ali Akbar Saboury ,
Arefeh Seyedarabi  and
Ali Akbar Moosavi-Movahedi
Adeleh Divsalar*
Affiliation:
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran Department of Biological Sciences, Tarbiat Moallem University, Tehran, Iran
Sajedeh Ebrahim Damavandi
Affiliation:
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
Ali Akbar Saboury
Affiliation:
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
Arefeh Seyedarabi
Affiliation:
Institute of Structural and Molecular Biology, University College London, London, UK
Ali Akbar Moosavi-Movahedi
Affiliation:
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
*
*For correspondence; e-mail: [email protected]
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Abstract

The effect of copper(II) ions (Cu+2) on the structure of β-lactoglobulin (β-lg) was investigated spectroscopically using UV-visible, fluorescence and circular dichroism (CD) and calorimetrically using isothermal titration calorimetry (ITC), at different temperatures. Results of the UV-visible studies showed that adding Cu+2 to β-lg solution caused increasing turbidity, indicative of protein aggregation. It was noticeable that the rate of increasing turbidity was directly proportional to increasing temperature. The far-UV CD studies displayed that the Cu+2 cannot induce any significant changes in the secondary structures of β-lg at different temperatures. Also, the ITC data indicated that the binding process of Cu+2 to β-lg is mainly entropically driven. The results highlight that copper ions cause the tertiary structure of β-lg to change and induce a slightly open structure leading to the formation of supramolecular aggregates in β-lg which may result in the reduced allergenicity of β-lg and its increased use in industrial applications.

Keywords

β-Lactoglobulincopper ionfluorescence quenchingtitration calorimetryallergenicityturbidity
Type
Research Article
Information
Journal of Dairy Research , Volume 79 , Issue 2 , May 2012 , pp. 209 - 215
Copyright
Copyright © Proprietors of Journal of Dairy Research 2012

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