Modification of bovine β-lactoglobulin by glycation in a powdered state or in an aqueous solution: Effect on association behavior and protein conformation

Journal of Agricultural and Food Chemistry

Volumn 47, Issue 1, 1999, Pages 83-91

  Morgan, François ^a   Léonil, Joëlle ^a   Mollé, Daniel ^a   Bouhallab, Saïd ^a  

^a CEMAGREF   (France)

Author keywords

Lactoglobulin; Aggregation; Conformation; Denaturation; Glycation

Indexed keywords

BETA LACTOGLOBULIN; GLUCOSE; LACTOGLOBULIN; WATER;

ANIMAL; AQUEOUS SOLUTION; ARTICLE; CATTLE; CHEMICAL MODIFICATION; CHEMISTRY; CONFORMATIONAL TRANSITION; GEL CHROMATOGRAPHY; GLYCATION; GLYCOSYLATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; POWDER; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MODIFICATION; SOLUTION AND SOLUBILITY;

ANIMALS; CATTLE; CHROMATOGRAPHY, GEL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLUCOSE; LACTOGLOBULINS; POWDERS; PROTEIN CONFORMATION; SOLUTIONS; WATER;

ANIMALIA; BOS TAURUS; BOVINAE;

EID: 0345059266     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf9804387     Document Type: Article

References (33)

1. Bouhallab, S.; Morgan, F.; Henry, G.; Mollé, D.; Léonil, J. Formation of stable covalent dimer explains the high solubility at pH 4.6 of lactose-β-Lactoglobulin conjugates heated near neutral pH. J. Agric. Food Chem., submitted for publication.
2. 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.
3. Burr, R.; Moore, C. H.; Hill, J. P. Evidence of multiple glycosylation of bovine β-Lactoglobulin by electrospray ionisation mass spectrometry. Milchwissenschaft 1996, 51, 488-492.
4. Cairoli, S.; Iametti, S.; Bonomi, F. Reversible and irreversible modifications of β-Lactoglobulin upon exposure to heat. J. Protein Chem. 1994, 13, 347-354.
5. De Wit, J. N. The use of whey protein products. A review: NIZO Research Report Verslag V295; NIZO: Ede, Netherlands, 1989.
6. Eigel, W. N.; Butler, J. E.; Ernstrom, C. A.; Farrell, H. M.; Harwalkar, V. R.; Jenness, R.; Whitney, R. McL. Nomenclature of proteins of cow's milk: fifth revision. J. Dairy Sci. 1984, 67, 1599-1631.
7. Ellman, G. L. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 1959, 82, 70-77.
8. Fauquant, J.; Maubois, J.-L.; Pierre, A. Microfiltration of milk through a mineral membrane [Microfiltration du lait sur membrane minèrale]. Technol. Lait. 1988, 1028, 21-23.
9. Garcia Alvarez-Coque, M. C.; Medina Hernandez, M. J.; Villanueva Vcamanas, R. M.; Mongay Fernandez, C. Studies on the formation and stability of isoindoles derived from amino-acids, o-phthalaldehyde and N-acetyl-1-cysteine. Anal. Biochem. 1989, 180, 172-176.
10. Griffin, W. G.; Griffin, M. C. A.; Martin, S. R.; Price, J. Molecular basis of thermal aggregation of bovine β-Lactoglobulin A. J. Chem. Soc., Faraday Trans. 1993, 89, 3395-3406.
11. Hoffmann, M. A. M.; Van Mil, P. J. J. M. Heat-induced aggregation of β-Lactoglobulin: role of the free thiol group and disulfide bonds. J. Agric. Food Chem. 1997a, 45, 2942-2948.
12. Hoffmann, M. A. M.; Sala, G.; Olieman, C.; DeKruif, K. G. Molecular mass distributions of heat-induced β-Lactoglobulin aggregates. J. Agric. Food Chem. 1997b, 45, 2949-2957.
13. Iametti, S.; Cairoli, S.; DeGregori, B.; Bonomi, F. Modifications of high-order structures upon heating of β-Lactoglobulin: dependence of the protein concentration. J. Agric. Food Chem. 1995, 43, 53-58.
14. 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.
15. Kella, N. K. D.; Kinsella, J. E. Enhanced thermodynamic stability of β-Lactoglobulin at low pH. Biochem. J. 1988, 255, 113-118.
16. Kester, J. J.; Richardson, T. Modification of whey proteins to improve functionality. J. Dairy Sci. 1984, 67, 2757-2774.
17. Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 1991, 24, 946-950.
18. Laemmli, U. K. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature 1970, 227, 680-685.
19. Laligant, A.; Dumay, E.; Casas Valencia, C.; Cuq, J.-L.; Cheftel, J.-C. Surface hydrophobicity and aggregation of β-Lactoglobulin heated near neutral pH. J. Agric. Food Chem. 1991, 39, 2147-2155.
20. Law, A. J. R.; Leaver, J.; Banks, J. M.; Horne, D. S. Quantitative fractionnation of whey proteins by gel permeation FPLC. Milchwissenschaft 1993, 48, 663-666.
21. Léonil, J.; Mollé, D.; Fauquant, J.; Maubois, J.-L.; Pearce, R. J.; Bouhallab, S. Characterization by ionization mass spectrometry of lactosyl-β-Lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose binding site. J. Dairy Sci. 1997, 80, 2270-2281.
22. Matsuda, T.; Kato, Y.; Nakamura, R. Lysine loss and polymerization of bovine β-Lactoglobulin by amino-carbonyl reaction with lactulose. J. Agric. Food Chem. 1991, 39, 1201-1204.
23. Maubois, J.-L.; Léonil, J.; Bouhallab, S.; Mollé, D.; Pearce, J. R. Characterization by ionization mass spectrometry of a lactosyl-β-Lactoglobulin conjugate occurring during mild heating of whey. Abstract D116, Program and Abstracts of the American Dairy Science Association and Northeastern ADSA/ASAS Meeting, June 25-28, 1995, Cornell University, Ithaca, NY. J. Dairy Sci. 1995, 78, suppl 1.
24. Mohan Reddy, I.; Kella, N. K. D.; Kinsella, J. E. Structural and conformational basis of the resistance of β-Lactoglobulin to peptic and chymotryptic digestion. J. Agric. Food Chem. 1988, 36, 737-741.
25. Mollé, D.; Morgan, F.; Bouhallab, S.; Léonil, J. Selective detection of lactolated peptides in hydrolysates by liquid chromatography/electrospray tandem mass spectrometry. Anal. Biochem. 1998, 259, 152-161.
26. Morgan, F.; Léonil, J.; Mollé, D.; Bouhallab, S. Non enzymatic lactosylation of bovine β-Lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms. Biochem. Biophys. Res. Commun. 1997, 236, 413-417.
27. Morgan, F.; Bouhallab, S.; Mollé, D.; Henry, G.; Maubois, J.-L.; Léonil, J. Lactolation of β-Lactoglobulin monitored by electrospray ionisation mass spectrometry. Int. Dairy J. 1998, 8, 95-98.
28. O'Brien, J. Heat-induced changes in lactose: isomerization, degradation, Maillard browning. In Heat-induced changes in milk, 2nd ed.; Fox, P. F., Ed.; IDF: Brussels, 1995; pp 134-170.
29. Ogg, C. L. Determination of nitrogen by the micro-Kjeldhal method. J.-Assoc. Off. Anal. Chem. 1960, 43, 689-693.
30. 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.
31. 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.
32. Roefs, S. P. F. M.; De Kruif, K. G. A model for the denaturation and aggregation of β-Lactoglobulin. Eur. J. Biochem. 1994, 226, 883-889.
33. Scatchard, G. The attraction of proteins for small molecules and ions. Ann. N.Y. Acad. Sci. 1949, 51, 660-672.