A Comparison of the Functional and Interfacial Properties of β-Casein and Dephosphorylated β-Casein

The functional and interfacial properties of β-casein and dephosphorylated β-casein (DeP β-casein) were studied at pH 7.0 in 10 mM phosphate buffer. A decrease in emulsion stability and an increase in foamability was observed. Results from a variety of interfacial techniques including electrophoreti...

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Bibliographic Details
Published in:Journal of colloid and interface science 1997-11, Vol.195 (1), p.77-85
Main Authors: Husband, Fiona A., Wilde, Peter J., Mackie, Alan R., Garrood, Martin J.
Format: Article
Language:English
Subjects:
Biological and medical sciences
casein
emulsion
foam
Fundamental and applied biological sciences. Psychology
interface
Molecular biophysics
Surface properties. Adsorption
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Summary:The functional and interfacial properties of β-casein and dephosphorylated β-casein (DeP β-casein) were studied at pH 7.0 in 10 mM phosphate buffer. A decrease in emulsion stability and an increase in foamability was observed. Results from a variety of interfacial techniques including electrophoretic mobility, thin film thickness, surface and interfacial tension, surface rheology, adsorbed layer thickness, and adsorption isotherms of dephosphorylated β-casein and β-casein are reported. The results demonstrate that the phosphorylated groups of the N-terminal region of β-casein are important for stabilizing emulsions. This is either as a direct result of charge repulsion between β-casein N-terminal regions or more probably as an indirect result of the reduced N-terminal charge permitting DeP β-casein to adopt a different interfacial conformation resulting in a loss or reduction of a steric barrier.
ISSN:0021-9797
1095-7103
DOI:10.1006/jcis.1997.5137