Hostname: page-component-78c5997874-dh8gc Total loading time: 0 Render date: 2024-11-04T21:44:33.901Z Has data issue: false hasContentIssue false
  • English
  • Français

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

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

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

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