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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
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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

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References

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