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Comparative study on heat stability of camel and bovine apo and holo α-lactalbumin

Published online by Cambridge University Press:  23 November 2009

Maliheh Sadat Atri ,
Ali Akbar Saboury ,
Reza Yousefi ,
Michèle Dalgalarrondo ,
Jean-Marc Chobert ,
Thomas Haertlé  and
Ali Akbar Moosavi-Movahedi
Maliheh Sadat Atri
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
Reza Yousefi
Affiliation:
Department of Biology, University of Shiraz, Shiraz, Iran
Michèle Dalgalarrondo
Affiliation:
UR 1268 Biopolymères Interactions Assemblages, INRA, équipe Fonctions et Interactions des Protéines Laitières, B.P. 71627, 44316 Nantes Cedex 3, France
Jean-Marc Chobert
Affiliation:
UR 1268 Biopolymères Interactions Assemblages, INRA, équipe Fonctions et Interactions des Protéines Laitières, B.P. 71627, 44316 Nantes Cedex 3, France
Thomas Haertlé
Affiliation:
UR 1268 Biopolymères Interactions Assemblages, INRA, équipe Fonctions et Interactions des Protéines Laitières, B.P. 71627, 44316 Nantes Cedex 3, France
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 stability of camel α-lactalbumin (α-la) against heat denaturation was measured, using circular dichroism (CD) and fluorescence spectroscopy, as well as differential scanning calorimetry (DSC). The experiments were performed in the presence of saturating concentrations of calcium as well as in the presence of EDTA, yielding to the apo form of α-la. The change in heat capacity (ΔCp) suggests a greater contribution of hydrophobic interactions to the stability of holo camel α-la than in its bovine counterpart. Overall the results obtained in this study suggest a greater stability of camel α-la than the bovine protein in both holo and apo states. Also CD experiments showed similar secondary structure for camel and bovine α-la and secondary structure of camel α-la was better preserved than that of bovine α-la during heat denaturation. The differences in thermal stability between the proteins from two species can be primarily ascribed to the difference in the quantity of hydrophobic interactions involved in their folding.

Keywords

α-lactalbumindifferential scanning calorimetrycircular dichroismfluorescencecamel
Type
Research Article
Information
Journal of Dairy Research , Volume 77 , Issue 1 , February 2010 , pp. 43 - 49
Copyright
Copyright © Proprietors of Journal of Dairy Research 2009

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