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The structure of casein micelles between pH 5·5 and 6·7 as determined by light-scattering, electron microscopy and voluminosity experiments

Published online by Cambridge University Press:  01 June 2009

Henk J. Vreeman ,
Bas W. van Markwijk  and
Paula Both
Henk J. Vreeman
Affiliation:
Netherlands Inside for Dairy Research (NIZO), P.O. Box 20, 6710 BA Ede, The Netherlands
Bas W. van Markwijk
Affiliation:
Netherlands Inside for Dairy Research (NIZO), P.O. Box 20, 6710 BA Ede, The Netherlands
Paula Both
Affiliation:
Netherlands Inside for Dairy Research (NIZO), P.O. Box 20, 6710 BA Ede, The Netherlands
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Summary

Hydrodynamic radii from inelastic light-scattering experiments and radii of gyration from Zimm plots give an indication of the change of average casein micelle size when the pH is changed. Combination of the results of both types of measurements gives information on changes in the micelle protein matrix, i.e. changes in the voluminosity.

The voluminosity was also determined by the pellet method and by electron microscopy which also provided comparative data on size parameters.

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. 463 - 470
Copyright
Copyright © Proprietors of Journal of Dairy Research 1989

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References

REFERENCES

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