Aggregation of bovine β-Lactoglobulins A and B on heating at 75°C

International Dairy Journal

Volumn 6, Issue 5, 1996, Pages 519-527

  Nielsen, Bente T ^a   Singh, Harjinder ^a   Latham, June M ^a  

^a MASSEY UNIVERSITY   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

BOVINAE;

EID: 0030137918     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/0958-6946(95)00022-4     Document Type: Article

References (22)

1. Dalgleish, D.G. (1990), Denaturation and aggregation of serum proteins and caseins in heated milk. J. Agric. Food Chem., 38, 1995-1999.
2. Dannenberg, F. & Kessler, H.G. (1988). Reaction kinetics of the denaturation of whey proteins in milk. J. Food Sci., 53, 258-263.
3. de Wit, J. N. & Swinkels, G.A.M. (1980). A differential scanning calorimetric study of the thermal denaturation of bovine β-lactoglobulin. Thermal behaviour at temperatures up to 100°C. Biochim. Biophys. Acta, 624, 40-50.
4. Gordon, W.G., Basch, J.J. & Kalan, E.B. (1960). Differences in amino acid composition of β-lactoglobulin A and B. Biochem. Biophys. Res. Commun., 3, 672-674.
5. Gough, P. & Jenness, R. (1962). Heat denaturation of β-lactoglobulins A and B. J. Dairy Sci., 45, 1033-1039.
6. Harwalkar, V.R. & Kalab, M. (1985). Thermal denaturation and aggregation of β-lactoglobulin at pH 2.5. Effect of ionic strength and protein concentration. Milchwissenschaft, 40, 31-34.
7. Millier, R.M. & Lyster, R.L.J. (1979). Whey protein denaturation in heated milk and cheese whey. J. Dairy Res., 46, 95-102.
8. Huang, X.L., Catignani, G.L. & Swaisgood, H.E. (1994). Relative structural stabilities of β-lactoglobulins A and B as determined by proteolytic susceptibility and differential scanning calorimetry. J. Agric. Food Chem., 42, 1276-1280.
9. Imafidon, G.I., Ng-Kwai-Hang, K.F., Harwalkar, V.R. & Ma, C.Y. (1991). Differential scanning calorimetric study of different genetic variants of β-lactoglobulin. J. Dairy Sci., 74, 2416-2422.
10. Mailliart, P. & Ribadeau-Dumas, B. (1988). Preparation of β-lactoglobulin and β-lactoglobulin-free proteins from whey retentate by NaCl salting out at low pH. J. Food Sci., 53, 743-745, 752.
11. Manji, B. & Kakuda, Y. (1986). Thermal denaturation of whey proteins in skim milk. Can. Inst. Food Sci. Technol. J., 19, 163-166.
12. McKenzie, H.A. (1971). β-Lactoglobulins. In Milk Proteins. Chemistry and Molecular Biology, Vol. II, H. A. McKenzie, ed. Academic Press, New York, pp. 257-30.
13. Monaco, H.L., Zanotti, G., Spadon, P., Bolognesi, M., Sawyer, L. & Eliopoulos, E.E. (1987). Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J. Mol. Biol., 197, 695-706.
14. Mulvihill, D.M. & Donovan, M. (1987). Whey proteins and their thermal denaturation. A review. Irish J. Food Sci. Technol., 11, 43-75.
15. Mulvihill, D.M. & Kinsella, J.E. (1987). Gelation characteristics of whey proteins and β-lactoglobulin. Food Technol., 41(9), 102-111.
16. McSwiney, M., Singh H., Campanella, O. & Creamer, L.K. (1994). Thermal gelation and denaturation of bovine β-lactoglobulins A and B. J. Dairy Res., 61, 221-232.
17. Parris, N., Anema, S.G., Singh, H. & Creamer, L.K. (1993). Aggregation of whey proteins in heated sweet whey. J. Agric. Food Chem., 41, 460-464.
18. Relkin, P. & Launay, B. (1990). Concentration effects on the kinetics of β-lactoglobulin heat denaturation: a differential scanning calorimetric study. Food Hydrocoll., 4, 19-32.
19. Sawyer, W.H. (1968). Heat denaturation of bovine β-lactoglobulins and relevance of disulfide aggregation. J. Dairy Sci., 51, 323-329.
20. Sawyer, W.H., Norton, R.S. Nichol, L.W. & McKenzie, G.H. (1971). Thermodenaturation of bovine β-lactoglobulin: kinetics and the introduction of β structure. Biochim. Biophys. Acta, 243, 19-30.
21. Townend, R., Kumosinski, T.F. & Timasheff, S.N. (1967). The circular dichroism of variants of β-lactoglobulin. J. Biol. Chem., 242, 4538-4545.
22. Treece, J.M., Sheinson, R.S. & McMeekin, T.L. (1974). The solubilities of β-lactoglobulins A, B, and AB. Arch. Biochem. Biophys., 108, 99-108.