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Structure of β-casein

Published online by Cambridge University Press:  01 June 2009

Shunrokuro Arima ,
Ryoya Niki  and
Kenji Takase
Shunrokuro Arima
Affiliation:
University of Hokkaido, Sapporo, Japan
Ryoya Niki
Affiliation:
University of Hokkaido, Sapporo, Japan
Kenji Takase
Affiliation:
University of Hokkaido, Sapporo, Japan
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Summary

The temperature and concentration dependent association of β-casein was studied by means of viscometry, gel filtration chromatography, electron microscopy, analytical ultracentrifugation and UV difference spectrophotometry. Degrees of polymerization of 12, 22 and 49 and free energies of association of –21, –23 and – 25 kJ/mole monomer were found at temperatures of 10, 15 and 20 °C respectively in 0·2 M Na phosphate buffer pH 6·7.

Monomeric β-casein was not a completely random coil but became more compact with increasing temperature, due to hydrophobic interactions.

Type
Section C. Association of Proteins
Information
Journal of Dairy Research , Volume 46 , Issue 2: Symposium on the Physics and Chemistry of Milk Proteins , April 1979 , pp. 281 - 282
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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References

REFERENCE

Hipp, N. J., Groves, M. L., Custer, J. H. & McMeekin, T. L. (1952). Journal oj Dairy Science 35, 272.CrossRefGoogle Scholar