Hostname: page-component-586b7cd67f-rdxmf Total loading time: 0 Render date: 2024-11-26T14:34:25.399Z Has data issue: false hasContentIssue false
  • English
  • Français

Surface properties of the bovine casein components: relationships between structure and foaming properties

Published online by Cambridge University Press:  01 June 2009

Denis Lorient ,
Brigitte Closs  and
Jean Luc Courthaudon
Denis Lorient
Affiliation:
Laboratoire de Biochimie et Toxicologie Alimentaires ENS BANA, 21000 Dijon, France
Brigitte Closs
Affiliation:
Laboratoire de Biochimie et Toxicologie Alimentaires ENS BANA, 21000 Dijon, France
Jean Luc Courthaudon
Affiliation:
Laboratoire de Biochimie et Toxicologie Alimentaires ENS BANA, 21000 Dijon, France
Get access Rights & Permissions [Opens in a new window]

Summary

In order to optimize the use of caseins as surfactants, the surface tension, foaming capacity and stability were measured as a function of pH, ionic strength, protein concentration and polarity (modified by covalent binding of carbohydrates). We found that the caseins differ in their behaviour at the air/water interface with β-casein showing the greatest ability to decrease surface tension and to produce foams, due probably to its amphipathic structure. In experiments carried out at pH values close to pI, with low ionic strength and constant solubility (optimal conditions for foam formation), we observed a high surface hydrophobicity, a good accessibility and flexibility of peptidic side chains (evaluated by proteolysis), and a high foaming capacity parallelled by increased surface pressure. Foam stability of caseins was low compared to those of globular proteins such as β lactoglobulin.

Type
Original Articles
Information
Journal of Dairy Research , Volume 56 , Issue 3: Special Issue: Proceedings of the Hannah Research Institute Casein Conference , May 1989 , pp. 495 - 502
Copyright
Copyright © Proprietors of Journal of Dairy Research 1989

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Canton, M. C. & Mulvihill, D. M. 1983 Functional properties of caseinates chemically modified by reductive alkylation of lysines with reducing sugars. In Proceedings of International Dairy Federation, Symposium on Physico-chemical Aspects of Dehydrated Protein-rich Milk Products, Helsingor, Denmark, 17–19 May pp. 339–353Google Scholar
Colas, B., Gobin, C. & Lorient, D. 1988 Viscosity and voluminosity of caseins chemically modified by reductive alkylation with reducing sugars. Journal of Dairy Research 55 539–546CrossRefGoogle Scholar
Courthaudon, J. L., Colas, B. & Lorient, D. 1989 Covalent binding of glycosyl residues to bovine casein: effects on solubility and viscosity. Journal of Agricultural and Food Chemistry 37 32–36CrossRefGoogle Scholar
Dickinson, E. & Stainsby, G. 1982 In Colloids in Food pp. 285–330. London: Applied Science PublishersGoogle Scholar
Fox, P. F. & Mulvihill, D. M. 1983 Functional properties of caseins, caseinates and casein co-precipitates. In Proceedings of International Dairy Federation, Symposium on Physico-Chemical Aspects of Dehydrated Protein-Rich Milk Products, Helsingor, Denmark, 17–19 May pp. 188–259Google Scholar
Habeeb, A. F. 1966 Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Analytical Biochemistry 14 328–336CrossRefGoogle ScholarPubMed
Kakade, M. L. & Liener, I. E. 1969 Determination of available lysine in proteins. Analytical Biochemistry 27 273–280CrossRefGoogle ScholarPubMed
Kim, S. H. & Kinsella, J. E. 1985 Surface activity of food proteins: relationships between surface pressure development, viscoelasticity of interface films and foam stability of Bovine Serum Albumin. Journal of Food Science 50 1526–1530CrossRefGoogle Scholar
Lee, H. S., Sen, L. C., Clifford, A. J., Whitaker, J. R. & Feeney, R. E. 1979 Preparation and nutritional properties of caseins covalently modified with sugars. Reductive alkylation of lysines with glucose, fructose or lactose. Journal of Agricultural and Food Chemistry 27 1094–1098CrossRefGoogle ScholarPubMed
Le Meste, M., Colas, B., Blond, G. & Simatos, D. 1989 Influence of glycosylation on the hydration properties of caseinates. Journal of Dairy Research 56 479–486CrossRefGoogle Scholar
MacRitchie, F. 1978 Proteins at interfaces. Advances in Protein Chemistry 32 283–326CrossRefGoogle ScholarPubMed
Mitchell, J., Irons, L. & Palmer, G. J. 1970 A study of the spread and adsorbed films of milk proteins. Biochimica et Biophysica Acta 200 138–150CrossRefGoogle ScholarPubMed
Mitchell, J. R. 1986 In Developments in Food Proteins – 3 pp. 291–338. (Ed. Hudson, B. J. F.). London and New York: Applied Science PublishersGoogle Scholar
Poole, S., West, S. I. & Walters, C. L. 1984 Protein-protein interactions: their importance in the foaming of heterogeneous protein systems. Journal of the Science of Food and Agriculture 35 701–704CrossRefGoogle Scholar
Rothenbuhler, A. I. & Kinsella, J. E. 1985 The pH-stat method for assessing protein digestibility: an evaluation. Journal of Agricultural and Food Chemistry 33 433–438CrossRefGoogle Scholar
Song, K. & Damodaran, S. 1987 Structure-function relationship of proteins: adsorption of structural intermediates of bovine serum albumin at the air-water interface. Journal of Agricultural and Food Chemistry 35 236–241CrossRefGoogle Scholar
Stainsby, G. 1986 In Functional Properties of Food Macromolecules pp. 315–353. (Eds Mitchell, J. R. & Ledward, D. A.). London: Elsevier Applied Science PublishersGoogle Scholar
Townsend, A. & Nakai, S. 1983 Relationships between hydrophobicity and foaming characteristics of food Proteins. Journal of Food Science 48 589–595CrossRefGoogle Scholar
Waniska, R. & Kinsella, J. E. 1979 Foaming properties of proteins: column aeration apparatus using ovalbumin. Journal of Food Science 44 1398–1402, 1411CrossRefGoogle Scholar