Hostname: page-component-78c5997874-m6dg7 Total loading time: 0 Render date: 2024-11-05T02:01:10.322Z Has data issue: false hasContentIssue false
  • English
  • Français

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]
Get access Rights & Permissions [Opens in a new window]

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

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Acharya, KR, Stuart, DI, Walker, NP, Lewis, M & Phillips, DC 1989 Refined structure of baboon α-lactalbumin at 1·7 Å resolution: Comparison with C-type lysozyme. Journal of Molecular Biology 208 99–127CrossRefGoogle ScholarPubMed
Beg, OU, von Bahr-Lindstrom, H, Zaidi, ZH & Jornvall, H 1985 The primary structure of a-lactalbumin from camel milk. European Journal of Biochemistry 147 233–239CrossRefGoogle Scholar
Böhm, G, Muhr, R & Jaenicke, R 1992 Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Engineering Design and Selection 5 191–195CrossRefGoogle ScholarPubMed
Bradford, MM 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical biochemistry 72 248–254CrossRefGoogle ScholarPubMed
Calderone, V, Giuffrida, MG, Viterbo, D, Napolitano, L, Fortunato, D, Conti, A & Acharya, KR 1996 Amino acid sequence and crystal structure of buffalo α-lactalbumin. FEBS Letters 394 91–95CrossRefGoogle ScholarPubMed
Cardamone, M & Puri, NK 1992 Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochemical Journal 282 589–593CrossRefGoogle ScholarPubMed
Casbarra, A, Birolo, L, Infusini, G, Dal Piaz, F, Svensson, M, Pucci, P, Svanborg, C & Marino, G 2004 Conformational analysis of HAMLET, the folding variant of human α-lactalbumin associated with apoptosis. Protein Science 13 1322–1330CrossRefGoogle ScholarPubMed
Chrysina, ED, Brew, K & Acharya, KR 2000 Crystal Structures of Apo- and Holo-bovine α-Lactalbumin at 2·2-Å Resolution Reveal an Effect of Calcium on Inter-lobe Interactions. Journal of Biological Chemistry 275 37021–37029CrossRefGoogle Scholar
Conti, A, Godovac Zimmermann, J, Napolitano, L & Liberatori, J 1985 Identification and characterization of two alpha-lactalbumins from Somali camel milk Camelus dromedaries. Milchwissenschaft 40 673–675Google Scholar
Elagamy, EI 2000 Effect of heat treatment on camel milk proteins with respect to antimicrobial factors: a comparison with cows' and buffalo milk proteins. Food Chemistry 68 227–232CrossRefGoogle Scholar
El-Hatmi, H, Levieux, A & Levieux, D 2006 Camel (Camelus dromedarius) immunoglobulin G, α-lactalbumin, serum albumin and lactoferrin in colostrum and milk during the early post partum period. Journal of Dairy Research 73 288–293CrossRefGoogle ScholarPubMed
El-Hatmi, H, Girardet, JM, Gaillard, JL, Yahyaoui, MH & Attia, H 2007 Characterisation of whey proteins of camel (Camelus dromedarius) milk and colostrums. Small Ruminant Research 70 267–271CrossRefGoogle Scholar
Ewbank, JJ & Creighton, TE 1993 Structural Characterization of the Disulfide Folding Intermediates of Bovine α-Lactalbumin. Biochemistry 32 3694–3707CrossRefGoogle ScholarPubMed
Gómez, J, Hilser, VJ, Xie, D & Freire, E 1995 The heat capacity of proteins. Proteins: Structure, Function, and Bioinformatics 22 404–412CrossRefGoogle ScholarPubMed
Farah, Z 1986 Effect of heat treatment on whey proteins of camel milk. Milchwissenschaft 41 763–765Google Scholar
Farah, Z & Atkins, D 1992 Heat coagulation of camel milk. Journal of Dairy Research 59 229–231CrossRefGoogle Scholar
Greene, LH, Grobler, JA, Malinovskii, VA, Tian, J, Acharya, KR & Brew, K 1999 Stability, activity and flexibility in α-lactalbumin. Protein Engineering 12 581–587CrossRefGoogle ScholarPubMed
Griko, YV & Remeta, DP 1999 Energetics of solvent and ligand-induced conformational changes in α-lactalbumin. Protein Science 8 554–561CrossRefGoogle ScholarPubMed
Griko, YV, Freire, E & Privalov, PL 1994 Energetics of the α-lactalbumin states: a calorimetric and statistical thermodynamic study. Biochemistry 33 1889–1899CrossRefGoogle Scholar
Haddadin, MSY, Gammoh, SI & Robinson, RK 2008 Seasonal variations in the chemical composition of camel milk in Jordan. Journal of Dairy Research 75 8–12CrossRefGoogle ScholarPubMed
Hawe, A, Sutter, M & Jiskoot, W 2008 Extrinsic Fluorescent Dyes as Tools for Protein Characterization. Pharmaceutical Research 25 1487–1499CrossRefGoogle ScholarPubMed
Hendrix, T, Griko, YV & Privalov, PL 2000 A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin. Biophysical Chemistry 84 27–34CrossRefGoogle ScholarPubMed
Hill, RL & Brew, K 1975 Lactose synthetase. Advances in enzymology and related areas of molecular biology 43 411–490Google ScholarPubMed
Kelly, SM & Price, NC 2000 The use of circular dichroism in the investigation of protein structure and function. Current Protein and Peptide Science 1 349–384CrossRefGoogle ScholarPubMed
Kuhlman, B, Boice, JA, Wu, WJ, Fairman, R & Raleigh, DP 1997 Calcium Binding Peptides from α-Lactalbumin: Implications for Protein Folding and Stability. Biochemistry 36 4607–4615CrossRefGoogle ScholarPubMed
Lala, AK & Keul, P 1992 Increased Exposure of Hydrophobic Surface in MG-State of α-Lactalbumin. Journal of Biological Chemistry 267 19914–19918CrossRefGoogle Scholar
Laleye, L, Jobe, B & Wasesa, AAH 2008 Comparative study on heat stability and functionality of camel and bovine milk whey proteins. Journal of Dairy Science 91 4527–4534CrossRefGoogle ScholarPubMed
Levieux, D, Levieux, A, El-Hatmi, H & Rigaudière, JP 2006 Immunochemical quantification of heat denaturation of camel (Camelus dromedarius) whey proteins. Journal of Dairy Research 73 1–9CrossRefGoogle ScholarPubMed
Norma, J & Greenfield, NJ 1999 Applications of circular dichroism in protein and peptide analysis. Trends in analytical chemistry 18 236–244Google Scholar
Paci, E, Smith, LJ, Dobson, CM & Karplus, M 2001 Exploration of partially unfolded states of human alpha-lactalbumin by molecular dynamics simulation. Journal of Molecular Biology 306 329–347CrossRefGoogle ScholarPubMed
Permyakov, EA & Berliner, LJ 2000 α-lactalbumin: Structure and function. FEBS Letters 473 269–274CrossRefGoogle ScholarPubMed
Polverino de Laureto, P, Frare, E, Gottardo, R & Fontana, A 2002 Molten Globule of Bovine α-Lactalbumin at Neutral pH Induced by Heat, Trifluoroethanol, and Oleic Acid: A Comparative Analysis by Circular Dichroism Spectroscopy and Limited Proteolysis. Proteins: Structure, Function, & Genetics 49 385–397CrossRefGoogle ScholarPubMed
Rao, KR & Brew, K 1989 Calcium regulates folding and disulfide-bond formation in α-lactalbumin. Biochemical and Biophysical Research Communications 163 1390–1396CrossRefGoogle ScholarPubMed
Sanchez-Ruiz, JM 1995 Differential scanning calorimetry of proteins. Subcellular Biochemistry 24 133–176CrossRefGoogle ScholarPubMed
Schägger, H & von Jagow, G 1987 Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Analytical Biochemistry 166 368–379CrossRefGoogle ScholarPubMed
Semisotnov, GV, Rodionova, NA, Kutyshenko, VP, Ebert, B, Blanck, J & Ptitsyn, OB 1987 Sequential mechanism of refolding of carbonic anhydrase B. FEBS Letters 224 9–13CrossRefGoogle ScholarPubMed
Sturtevant, JM 1987 Biochemical applications of differential scanning calorimetry. Annual Review of Physical Chemistry 38 463–88CrossRefGoogle Scholar
Svensson, M, Hakansson, A, Mossberg, AK, Linse, S & Svanborg, C 2000 Conversion of α-lactalbumin to a protein inducing apoptosis. Proceedings of the National Academy of Sciences of the United States of America 97 4221–4226CrossRefGoogle ScholarPubMed
Vanderheeren, G & Hanssen, I 1994 Thermal Unfolding of Bovine α-Lactalbumin. The Journal of Biological Chemistry 269 7090–7094CrossRefGoogle ScholarPubMed
Vanhooren, A, Vanhee, K, Noyelle, K, Majer, Z, Joniau, M & Janssens, I 2002 Structural basis for difference in heat capacity increments for Ca2+ binding to two α-lactalbumins. Biophysical Journal 82 407–417CrossRefGoogle ScholarPubMed
Yang, F, Zhang, M, Chen, J & Liang, Y 2006 Structural changes of α-lactalbumin induced by low pH and oleic acid. Biochimica et Biophysica Acta 1764 1389–1396CrossRefGoogle Scholar