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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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References

Anandharamakrishnan, C, Rielly, CD & Stapley, AGF 2008 Loss of solubility of α-lactalbumin and β-lactoglobulin during the spray drying of whey protein. LWT-Food Science and Technology 4 270–277CrossRefGoogle Scholar
Besler, M, Eigenmann, F & Schwartz, RH 2002 Allergen data collection – update: cow's milk (Bos domesticus). Internet Symposium on Food Allergens 4 19–106Google Scholar
Chatchatee, P, Jarvinen, KM, Bardina, L, Beyer, K & Sampson, HA 2001 Identification of IgE- and IgG-binding epitopes on alpha(s1)-casein: differences in patients with persistent and transient cow's milk allergy. Journal of Allergy Clinical Immunology 107 379–383CrossRefGoogle ScholarPubMed
Chicón, R, Belloque, J, Alonso, E & López-Fandiño, R 2008 Immunoreactivity and digestibility of high-pressure-treated whey proteins. International Dairy Journal 18 367–376CrossRefGoogle Scholar
Corzo-Martínez, M, Cristina, Soria A, Belloque, J, Villamiel, M & Moreno, FJ 2010 Effect of glycation on the gastrointestinal digestibility and immunoreactivity of bovine β-lactoglobulin. International Dairy Journal 20 1–11CrossRefGoogle Scholar
Divsalar, A, Bagheri, MJ, Saboury, AA, Mansoori-Torshizi, H & Amani, M 2009 Investigation on the interaction of newly designed anticancer Pd(II) complexes with different aliphatic tails and human serum albumin. Journal of Physical Chemistry B 113 14035–14042CrossRefGoogle ScholarPubMed
Divsalar, A, Saboury, AA, Mansoori-Torshizi, H & Faizan, A 2010 Design, synthesis, and biological evaluation of a new palladium (II) complex: β-lactoglobulin and K562 as targets. Journal of Physical Chemistry B 114 3639–3647CrossRefGoogle ScholarPubMed
Dufour, E, Roger, P & Heartle, T 1992 Binding of benzo(α)pyrene, and cis-parinaric acid to beta-lactoglobulin: influence of protein modification. Journal of Protein Chemistry 11 645–652CrossRefGoogle Scholar
Host, A, Husby, S & Osterballe, O 1988 A prospective study of cow's milk allergy in exclusively breast-fed infants. Incidence, pathogenetic role of early inadvertent exposure to cow's milk formula, and characterization of bovine milk protein in human milk. Acta Paediatrica Scandinavica 77 663–670CrossRefGoogle ScholarPubMed
Marthasarathy, P & Johnson, WC Jr 1987 Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Analytical Biochemistry 167 76–85Google Scholar
Matulis, D, Baumann, CG, Bloomfield, VA & Lovrien, RE 1999 1-Anilino-8-naphthalene sulfonate as a protein conformational tightening agent. Biopolymers 49 451–4583.0.CO;2-6>CrossRefGoogle ScholarPubMed
Muhammad, G, Thomas, C, Julien, J, Michel, P & Saïd, B 2009 Copper modulates the heat-induced sulfhydryl/disulfide interchange reactions of β-lactoglobulin. Food Chemistry 116 884–891CrossRefGoogle Scholar
Navarra, G, Leone & Militello, V 2007 Thermal aggregation of β-lactoglobulin in presence of metal ions. Biophysical Chemistry 131 52–61CrossRefGoogle ScholarPubMed
Pescuma, M, Hébert, EM, Rabesona, H, Drouet, M, Choiset, Y, Haertlé, T, Mozzi, F, Valdez, GF & Chobert, JM 2011 Proteolytic action of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 reduces antigenic response to bovine β-lactoglobulin. Food Chemistry 15 487–492CrossRefGoogle Scholar
Shaikh, SMT, Seetharamappa, J, Kandagal, PB & Ashoka, S 2006 Binding of the bioactive component isothipendyl hydrochloride with bovine serum albumin. Journal of Molecular Structure 786 46–52CrossRefGoogle Scholar
Simons, J, Kosters, HA, Visschers, RW & Jongh, HHJ 2002 Role of calcium as trigger in thermal beta-lactoglobulin aggregation. Archives of Biochemistry and Biophysics 406 143–152CrossRefGoogle ScholarPubMed
Suutari, TJ, Valkonen, KH, Karttunen, TJ, Ehn, B-M, Ekstrand, B, Bengtsson, U, Virtanen, V, Nieminen, M & Kokkonen, J 2006 IgE cross reactivity between reindeer and bovine milk β-lactoglobulins in cow's milk allergic patients. Journal of Investigational Allergology Clinical Immunology 16 296–302Google ScholarPubMed
Vaarala, O, Saukkonen, T, Savilahti, E, Klemola, T & Akerblom, HK 1995 Development of immune response to cow's milk proteins in infants receiving cow's milk or hydrolyzed formula. Journal of Allergy and Clinical Immunology 96 917–923CrossRefGoogle ScholarPubMed
Vetri, V & Militello, V 2005 Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin. Biophysical Chemistry 113 83–91CrossRefGoogle ScholarPubMed
Viseu, MI, Carvalho, TI & Costa, SMB 2004 Conformational transitions in beta-lactoglobulin induced by cationic amphiphiles: equilibrium studies. Biophysical Journal 86 2392–2402CrossRefGoogle ScholarPubMed
Zsila, F, Imre, T, Szabo, PT, Bikadi, Z & Simonia, M 2002 Induced chirality upon binding of cis-parinaric acid to bovine β-lactoglobulin: spectroscopic characterization of the complex. FEBS Letter 520 81–87CrossRefGoogle ScholarPubMed