Effect of heat treatment on denaturation of bovine α-lactalbumin: Determination of kinetic and thermodynamic parameters

Journal of Agricultural and Food Chemistry

Volumn 53, Issue 25, 2005, Pages 9730-9736

  Wehbi, Zeina ^a   Pérez, María Dolores ^a   Sánchez, Lourdes ^a   Pocoví, Coloma ^a   Barbana, Chokry ^a   Calvo, Miguel ^a  

^a UNIVERSIDAD DE ZARAGOZA   (Spain)

Author keywords

Apo lactalbumin; Bovine milk; Heat denaturation; Kinetics; Native lactalbumin; Thermodynamics

Indexed keywords

LACTALBUMIN;

ANIMAL; ARTICLE; CATTLE; CHEMISTRY; HEAT; KINETICS; PROTEIN DENATURATION; THERMODYNAMICS;

ANIMALS; CATTLE; HEAT; KINETICS; LACTALBUMIN; PROTEIN DENATURATION; THERMODYNAMICS;

BOVINAE;

EID: 29744433465     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf050825y     Document Type: Article

References (34)

1. Pérez, M. D.; Sánchez, L.; Aranda, P.; Calvo, M. Synthesis and evolution of concentration of β-lactoglobulin and α-lactalbumin from cow and sheep colostrums and milk throughout early lactation. Cell. Mol. Biol. 1990, 36, 205-212.
2. Brew, K. α-Lactalbumin. In Advanced Dairy Chemistry - 1 Proteins, 3rd ed.; Fox, P. F., McSweeney, P. L. H., Eds.; Kluwer Academic/Plenum Press: New York, 2003; pp 387-421.
3. Noyelle, K.; Van Dael, H. Kinetics of conformational changes induced by the binding of various metal ions to bovine α-lactalbumin. J. Inorg. Biochem. 2002, 88, 69-76.
4. Permyakov, E. A.; Berliner, L. J. α-lactalbumin: structure and function. FEBS Lett. 2000, 473, 269-274.
5. Kronman, M. J. Metal-ion binding and the molecular conformational properties of α-lactalbumin. Crit. Rev. Biochem. Mol. Biol. 1989, 24, 565-667.
6. Segawa, T.; Sugai, S. Interactions of divalent metal ions with bovine, human, and goat α-lactalbumin. J. Biochem. 1983, 93, 1321-1328.
7. Barbana, C.; Pérez, M. D.; Sánchez, L.; Dalgalarrondo, M.; Chobert, J. M.; Haertlé, T.; Calvo, M. Interaction of bovine α-lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy. Int. Dairy J. 2006, 16, 18-25.
8. Cawthern, K. M.; Permyakov, E. A.; Berliner, L. J. Membrane-bound states of α-lactalbumin: implications for the protein stability and conformation. Protein Sci 1996, 5, 1394-1405.
9. Cawthern, K. M.; Narayan, M.; Chaudhuri, C.; Permyakov, E. A.; Berliner, L. J. Interactions of α-lactalbumin with fatty acids and spin label analogs. J. Biol. Chem. 1997, 272, 30812-30816.
10. Svensson, M.; Mossberg, A. K.; Pettersson, J.; Linse, S.; Svanborg, C. Lipids as cofactors in protein folding: stereospecific lipid-protein interactions are required to form HAMLET (human α-lactalbumin made lethal to tumor cells). Protein Sci. 2003, 12, 2805-2814.
11. Svanborg, C.; Agerstam, H.; Aronson, A.; Bjerkvig, R.; Düringer, C.; Fischer, W.; Gustafsson, L.; Hallgren, O.; Leijonhuvud, I.; Linse, S.; Mossberg, A. K.; Nilsson, H.; Pettersson, J.; Svensson, M. Hamlet kills tumor cells by an apoptosis-like mechanism cellular: molecular, and therapeutic aspects. Adv. Cancer Res. 2003, 88, 1-29.
12. Svensson, M.; Sabharwal, H.; Hakansson, A.; Mossberg, A. K.; Lipniunas, P.; Leffler, H.; Svanborg, C.; Linse, S. Molecular characterization of α-lactalbumin folding variants that induce apoptosis in tumor cells. J. Biol. Chem. 1999, 274, 6388-6396.
13. Svensson, M.; Fast, J.; Mossberg, A. K.; Duringer, C.; Gustafsson, L.; Hallgren, O.; Brooks, C. L.; Berliner, L.; Linse, S.; Svanborg, C. α-Lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human α-lactalbumin made lethal to tumor cells). Protein Sci. 2003, 12, 2794-2804.
14. Holt, C.; McPhail, D.; Nylander, T.; Otte, J.; Ipsen, R. H.; Bauer, R., et al. Some physico-chemical properties of nine semi-commercial whey protein concentrates, isolates and fractions. Int. J. Food Sci. Technol. 1999, 34, 587-601.
15. Owusu, R. K. Thermodynamic analysis of the effect of calcium on bovine α-lactalbumin conformational stability. Food Chem. 1992, 44, 189-194.
16. Chaplin, L. C.; Lyster, R. L. Irreversible heat denaturation of bovine α-lactalbumin. J. Dairy Res. 1985, 53, 249-258.
17. Mierzejewska, D.; Panasiuk, R.; Jedrychowski, J. Capillary electrophoresis determination of denaturation degree of cow milk α-lactalbumin during heat treatment of whey. Milchwissenschaft 2002, 57, 9-13.
18. Lyster, R. L. The denaturation of α-lactalbumin and β-lactoglobulin in heated milk. J. Dairy Res. 1970, 37, 233-243.
19. Jeanson, S.; Dupont, D.; Grattard, N.; Répécaud, R. Characterization of the heat treatment undergone by milk using two inhibition ELISAs for quantification of native and heat denatured α-lactalbumin. J. Agric. Food Chem. 1999, 47, 2249-2254.
20. Relkin, P. Thermal unfolding of β-lactoglobulin, α-lactalbumin, and bovine serum albumin, a thermodynamic approach. Crit. Rev. Food Sci. Nutr. 1996, 36, 565-601.
21. Relkin, P.; Launay, B.; Eynard, I. Effect of sodium and calcium addition on thermal denaturation of apo α-lactalbumin: a differential scanning calorimetric study. J. Dairy Sci. 1993, 76, 36-47.
22. Murakami, K.; Andree, P. J.; Berliner, L. J. Metal ion binding to α-lactalbumin species. Biochemistry 1982, 21, 5494-5502.
23. Grabar, P.; Willians, C. A. Methode permettant l'etude conjuge des properties electrophoretiques et immunochimies d'un mélange des proteins: application au serum sanguine. Biochim. Biophys. Acta 1953, 193-194.
24. Mancini, G.; Carbonara, A. O.; Heremans, J. F. Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry 1965, 2, 235-254.
25. Levieux, D. Heat denaturation of whey proteins comparative studies with physical and immunological methods. Ann. Rech. Vet. 1980, 11, 89-97.
26. Mainer, G.; Sánchez, L.; Ena, J. M.; Calvo, M. Kinetic and thermodynamic parameters for heat denaturation of bovine milk IgG, IgA, and IgM. J. Food Sci. 1997, 62, 1034-1038.
27. Sánchez, L.; Peiró, J. M.; Castillo, H.; Pérez, M. D.; Ena, J. M.; Calvo, M. Kinetic parameters for denaturation of bovine milk lactoferrin. J. Food Sci. 1992, 57, 873-879.
28. Paulsson, M.; Dejmek, P. Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry. J. Dairy Sci. 1990, 73, 590-600.
29. Hillier, R. M.; Lyster, R. L. Whey protein denaturation in heated milk and cheese whey. J. Dairy Res. 1979, 46, 95-102.
30. Polverino de Laureto, P.; Frare, E.; Gottardo, R.; Fontana, A. 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. Protein Struct., Funct. Genet. 2002, 49, 385-397.
31. Puyol, P.; Pérez, M. D.; Peiro, J. M.; Calvo, M. Effect of binding of retinol and palmitic acid to bovine β-lactoglobulin on its resistance to thermal denaturation. J. Dairy Sci. 1994, 1494-1502.
32. Manji, B.; Kakuda, Y. Thermal denaturation of whey proteins in skim milk. Int. Food Sci. Technol. J. 1986, 4, 163-166.
33. Eynard, L.; Iameti, S.; Relkin, P. Bonomi, F. Surface hydrophobicity changes and heat-induced modifications of α-lactalbumin. J. Agric. Food Chem. 1992, 40, 1732-1742.
34. Hendrix, T.; Griko, Y. V.; Privalov, P. A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin. Biophys. Chem. 2000, 84, 27-34.