Method for the isolation of bovine β-lactoglobulin from a cheese whey protein fraction and physicochemical characterization of the purified product

International Dairy Journal

Volumn 7, Issue 4, 1997, Pages 229-235

  Caessens, Petra W J R ^a,b   Visser, Servaas ^a   Gruppen, Harry ^b  

^a NIZO FOOD RESEARCH   (Netherlands)

^b WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

Lactoglobulin; Physicochemical properties; Purification

Indexed keywords

EID: 0030853218     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-6946(97)00004-6     Document Type: Article

References (29)

1. Aschaffenburg, R. and Drewry, J. (1957) Improved method for the preparation of crystalline β-lactoglobulin and α-lactalbumin from cow's milk. Biochemical Journal 65, 273-277.
2. de Jong, N., Visser, S. and Olieman, C. (1993) Determination of milk proteins by capillary electrophoresis. Journal of Chromatography 652, 207-213.
3. de Wit, J. N. and Bronts, H. (1992) Process for the recovery of α-lactalbumin and β-lactoglobulin from a whey protein product. European Patent Application 0 604 684, 7 pp.
4. de Wit, J. N., Klarenbeek, G. and Hontelez-Backx, E. (1983) Evaluation of functional properties of whey protein concentrates and whey protein isolates 1. Isolation and characterization. Netherlands Milk and Dairy Journal 37, 37-49.
5. Dunnill, D. and Green, D. W. (1965) Sulphydryl groups and the N↔ conformational change in β-lactoglobulin. Journal of Molecular Biology 15, 147-151.
6. Ebeler, S. E., Phillips, L. G. and Kinsella, J. E. (1990) Purification of β-lactoglobulin: Isolation of genetic variants and influence of purification method on secondary structure. Milchwissenschaft 45, 694-698.
7. Fox, K. K., Holsinger, V. H., Posati, L. P. and Pallansch, M. J. (1967) Separation of β-lactoglobulin from other milk serum proteins by trichloroacetic acid. Journal of Dairy Science 50, 1363-1367.
8. Geeraert, E. and Sandra, P. (1985) Capillary GC of triglycerides in fats and oils using a high temperature phenylmethylsilicone stationary phase, part 1. Journal of High Resolution Chromatography and Chromatography Communications 8, 415-422.
9. Hambling, S. G., Mc Alpine, A. S. and Sawyer, L. (1992) β-Lactoglobulin, In Advanced Dairy Chemistry, Proteins, ed. P. F. Fox. Vol. 1, pp. 141-190, Elsevier Applied Science, London.
10. Hoffmann, M. A. M., Roefs, S. P. F. M., Verheul, M., van Mil, P. J. J. M. and de Kruif, C. G. (1996) Aggregation of β-lactoglobulin studied by in situ light scattering. Journal of Dairy Research 63, 423-440.
11. International Organization for Standardization (1995) Milk and milk products - determination of nitrogen content -method by combustion according to the Dumas principle. ISO/WD, 14891, 13 pp.
12. Kella, N. K. D. and Kinsella, J. E. (1988) Enhanced thermodynamic stability of β-lactoglobulin at low pH; A possible mechanism. Biochemical Journal 255, 113-118.
13. Kinekawa, Y.-I. and Kitabatake, N. (1996) Purification of β-lactoglobulin from whey protein concentrate by pepsin treatment. Journal of Dairy Science 79, 350-356.
14. Kinsella, J. E. and Whitehead, D. M. (1989) Proteins in whey: chemical, physical and functional properties. Advances in Food and Nutrition Research 33, 343-438.
15. Koops, J., Klomp, H. and Elgersma, R. H.C. (1975) Rapid determination of nitrogen in milk and dairy products by colorimetric estimation of ammonia following an accelerated procedure. Netherlands Milk and Dairy Journal 29, 169-180.
16. Larson, B. L. and Jenness, R. (1955) β-Lactoglobulin. In Biochemical Preparations, ed. W. W. Westerfeld, pp. 23-29. John Wiley and Sons, New York.
17. Maté, J. I. and Krochta, J. M. (1994) β-Lactoglobulin separation from whey protein isolate on a large scale. Journal of Food Science 59, 1111-1114.
18. McKenzie, H. A. (1971) β-Lactoglobulin. In Milk Proteins Chemistry and Molecular Biology, ed. H. A. McKenzie, Vol. II, pp. 257-325. Academic Press, New York.
19. Pearce, R. J. (1983) Thermal separation of β-lactoglobulin and α-lactalbumin in bovine Cheddar cheese whey. Australian Journal of Dairy Technology 38, 144-149.
20. Swaisgood, H. E. (1982) Chemistry of milk protein. In Developments in Dairy Chemistry-I, Proteins, ed. P. F. Fox, pp. 1-60. Applied Science Publishers, London.
21. Tanimoto, M., Kawasaki, Y. Y., Shinmoto, H., Dosaka, S. and Tomizawa, A. (1990) Process for producing kappa-casein glycomacropeptides. European Patent Application 393-850, 5 pp.
22. Tanford, C., Bunville, L. G. and Nozaki, Y. (1959) The reversible transformation of β-lactoglobulin at pH 7.5. Journal of the American Chemical Society 81, 4032-4036.
23. Townend, R. and Timasheff, S. N. (1960) Molecular interactions in β-lactoglobulin. III. Light scattering investigation of the stoichiometry of the association between pH 3.7 and 5.2. Journal of the American Chemical Society 82, 3168-3174.
24. Townend, R., Weinberger, L. and Timasheff, S. N. (1960a) Molecular interactions in β-lactoglobulin. IV. The dissociation of β-lactoglobulin below pH 3.5. Journal of the American Chemical Society 82, 3175-3179.
25. Townend, R., Winterbottom, R. J. and Timasheff, S. N. (1960b) Molecular interactions in β-lactoglobulin. II. Ultracentrifugal and electrophoretic studies of the association of β-lactoglobulin below its isoelectrical point. Journal of the American Chemical Society 82, 3161-3168.
26. van Riel, J. and Olieman, C. (1995) Determination of caseinomacropeptide with capillary zone electrophoresis and its application to the detection and estimation of rennet whey solids in milk and buttermilk. Electrophoresis 16, 529-533.
27. Verhoef, J. C. and Barendrecht, E. (1977) Mechanism and reaction rate of the Karl Fischer filtration reaction. Part V. Analytical implications. Analytica Chimica Acta 94, 395-403.
28. Visser, S., Slangen, K. J. and Rollema, H. S. (1991) Phenotyping of bovine milk proteins by reversed-phase high-performance liquid chromatography. Journal of Chromatography 548, 361-370.
29. Visser, S. and Slangen, K. J. (1992) Reversed-phase HPLC separation of bovine milk protein genetic variants. Journal of Chromatographic Science 30, 466.