Heat-induced redistribution of disulfide bonds in milk proteins. 1. Bovine β-lactoglobulin

Journal of Agricultural and Food Chemistry

Volumn 52, Issue 25, 2004, Pages 7660-7668

  Creamer, Lawrence K ^a   Bienvenue, Annie ^c   Nilsson, Hanna ^b   Paulsson, Marie ^b   Van Wanroij, Miriam ^d   Lowe, Edwin K ^a   Anema, Skelte G ^a   Boland, Michael J ^a   Jiménez Flores, Rafael ^c  

^a FONTERRA RESEARCH CENTRE   (New Zealand)

^b LUND UNIVERSITY   (Sweden)

^c CALIFORNIA POLYTECHNIC STATE UNIVERSITY   (United States)

^d WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

Lactoglobulin; Disulfide bonding; Heat induced change; Mass spectroscopy

Indexed keywords

BETA LACTOGLOBULIN; CYSTEINE; DITHIOTHREITOL; MILK PROTEIN; PEPTIDE; TRYPSIN;

ARTICLE; CHEMICAL STRUCTURE; CONTROLLED STUDY; DISULFIDE BOND; ELECTROSPRAY MASS SPECTROMETRY; HEATING; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; NONHUMAN; PROTEIN ANALYSIS; PROTEIN DOMAIN; REDUCTION;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DISULFIDES; HEAT; HYDROLYSIS; LACTOGLOBULINS; MILK PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; TRYPSIN;

BOVINAE;

EID: 10644243447     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf049388y     Document Type: Article

References (33)

1. Sawyer, W. H. Complex between β-lactoglobulin and κ-casein. A review. J. Dairy Sci. 1969, 52, 1347-1355.
2. Elfagm, A. A.; Wheelock, J. V. Interaction of bovine α-lactalbumin and β-lactoglobulin in heated milk. J. Dairy Sci. 1978, 61, 28-32.
3. Lalande, M.; Tissier, J. P.; Corrieu, G. Fouling of a plate heat exchanger used in ultra-high-temperature sterilization of milk. J. Dairy Res. 1984, 57, 557-568.
4. Havea, P.; Singh, H.; Creamer, L. K.; Campanella, O. H. Electrophoretic characterization of the protein products formed during heat treatment of whey protein concentrate solutions. J. Dairy Res. 1998, 65, 79-91.
5. McKenzie, H. A. β-Lactoglobulins. In Milk Proteins: Chemistry and Molecular Biology; McKenzie, H. A., Ed.; Academic Press: New York, 1971; pp 257-330.
6. Havea, P.; Carr, A. J.; Creamer, L. K. The roles of disulphide and non-covalent bonding in the functional properties of heat-induced whey protein gels. J. Dairy Res. 2004, 71, 330-339.
7. Creamer, L. K.; Sawyer, L. β-Lactoglobulin. In Encyclopedia of Dairy Sciences; Roginski, H., Fuquay, J. W., Fox, P. F., Eds.; Academic Press: San Diego, CA, 2003; pp 1932-1939.
8. Brownlow, S.; Morais Cabral, J. H.; Cooper, R.; Flower, D. R.; Yewdall, S. J.; Polikarpov, I.; North, A. C. T.; Sawyer, L. Bovine β-lactoglobulin at 1.8 Å resolution - still an enigmatic lipocalin. Structure 1997, 5, 481-495.
9. Qin, B. Y.; Bewley, M. C.; Creamer, L. K.; Baker, E. N.; Jameson, G. B. Functional implications of structural differences between variants A and B of bovine β-lactoglobulin. Protein Sci. 1999, 8, 75-83.
10. 15N chemical shifts for bovine β-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form. J. Biomol. NMR 1998, 12, 89-107.
11. Kuwata, K.; Hoshino, M.; Forge, V.; Era, S.; Batt, C. A.; Goto, Y. Solution structure and dynamics of bovine β-lactoglobulin A. Protein Sci. 1999, 8, 2541-2545.
12. Fogolari, F.; Ragona, L.; Zetta, L.; Romagnoli, S.; De Kruif, K. G.; Molinari, H. Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH 2. FEBS Lett. 1998, 436, 149-154.
13. Mulvihill, D. M.; Donovan, M. Whey proteins and their thermal denaturation - a review. Irish J. Food Sci. Technol. 1987, 11, 43-75.
14. Qi, X. L.; Holt, C.; McNulty, D.; Clarke, D. T.; Brownlow, S.; Jones, G. R. Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. Biochem. J. 1997, 324, 341-346.
15. Prabakaran, S.; Damodaran, S. Thermal unfolding of β-lactoglobulin: characterization of initial unfolding events responsible for heat-induced aggregation. J. Agric. Food Chem. 1997, 45, 4303-4308.
16. Croguennec, T.; Bouhallab, S.; Mollé, D.; O'Kennedy, B. T.; Mehra, R. Stable monomeric intermediate with exposed Cys119 is formed during heat denaturation of β-lactoglobulin. Biochem. Biophys. Res. Commun. 2003, 301, 465-471.
17. Surroca, Y.; Haverkamp, J.; Heck, A. J. R. Towards the understanding of molecular mechanisms in the early stages of heat-induced aggregation of β-lactoglobulin AB. J. Chromatogr. A 2002, 970, 275-285.
18. Livney, Y. D.; Verespej, E.; Dalgleish, D. G. Steric effects governing disulfide bond interchange during thermal aggregation in solutions of β-lactoglobulin B and α-lactalbumin. J. Agric. Food Chem. 2003, 51, 8098-8106.
19. Manderson, G. A.; Hardman, M. J.; Creamer, L. K. Effect of heat treatment on the conformation and aggregation of β-lactoglobulin A, B, and C. J. Agric. Food Chem. 1998, 46, 5052-5061.
20. Iametti, S.; De Gregori, B.; Vecchio, G.; Bonomi, F. Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin. Eur. J. Biochem. 1996, 237, 106-112.
21. Schokker, E. P.; Singh, H.; Pinder, D. N.; Norris, G. E.; Creamer, L. K. Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH. Int. Dairy J. 1999, 9, 791-800.
22. Cho, Y.; Singh, H.; Creamer, L. K. Heat-induced interactions of β-lactoglobulin A and κ-casein B in a model system. J. Dairy Res. 2003, 70, 61-71.
23. Bienvenue, A.; Norris, C. S.; Boland, M. J.; Creamer, L. K.; Jimenez-Flores, R. Disulfide bonding patterns between β-lactoglobulin and κ-casein in a heated and spray-dried milk model. J. Dairy Sci. 2002, 85 (Suppl. 1), 340.
24. Mailliart, P.; Ribadeau-Dumas, B. Preparation of β-lactoglobulin and β-lactoglobulin-free proteins from whey retentate by NaCl salting out at low pH. J. Food Sci. 1988, 53, 743-747.
25. Nilsson, H. Hydrolysis of β-lactoglobulin A, B and C with trypsin. Master's thesis, Lund University, 2000.
26. Dalgalarrondo, M.; Chobert, J. M.; Dufour, E.; Bertrandharb, C.; Dumont, J. P.; Haertle, T. Characterization of bovine β-lactoglobulin B tryptic peptides by reversed-phase high-performance liquid chromatography. Milchwissenschaft 1990, 45, 212-216.
27. Chobert, J.-M.; Dalgalarrondo, M.; Dufour, E.; Bertrand-Harb, C.; Haertlé, T. Influence of pH on the structural changes of β-lactoglobulin studied by tryptic hydrolysis. Biochim. Biophys. Acta 1991, 1077, 31-34.
28. Morgan, F.; Léonil, J.; Mollé, D.; Bouhallab, S. Nonenzymatic lactosylation of bovine β-lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms. Biochem. Biophys. Res. Commun. 1997, 236, 413-417.
29. Dufour, E.; Dalgalarrondo, M.; Adam, L. Conformation of β-lactoglobulin at an oil/water interface as determined from proteolysis and spectroscopic methods. J. Colloid Interface Sci. 1998, 207, 264-272.
30. 1H NMR study. J. Agric. Food Chem. 1998, 46, 1805-1813.
31. Edwards, P. J. B.; Jameson, G. B.; Palmano, K. P.; Creamer, L. K. Heat-resistant structural features of bovine β-lactoglobulin A revealed by NMR H/D exchange observations. Int. Dairy J. 2002, 12, 331-344.
32. Yagi, M.; Sakurai, K.; Kalidas, C.; Batt, C. A.; Goto, Y. Reversible unfolding of bovine β-lactoglobulin mutants without a free thiol group. J. Biol. Chem. 2003, 278, 47009-47015.
33. Creamer, L. K.; Nilsson, H. C.; Paulsson, M. A.; Coker, C. J.; Hill, J. P.; Jiménez-Flores, R.. Effect of genetic variation on the tryptic hydrolysis of bovine β-lactoglobulin A, B, and C. J. Dairy Sci. 2004, 87, in press.