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CPG-chromatography studies on the stability of casein micelles

Published online by Cambridge University Press:  01 June 2009

Märtha Larsson-Raźnikiewicz ,
Elisabeth Almlöf  and
Bo Ekstrand
Märtha Larsson-Raźnikiewicz
Affiliation:
Department of Chemistry, Swedish University of Agricultural Sciences, S-750 07 Uppsala, Sweden
Elisabeth Almlöf
Affiliation:
Department of Chemistry, Swedish University of Agricultural Sciences, S-750 07 Uppsala, Sweden
Bo Ekstrand
Affiliation:
Department of Chemistry, Swedish University of Agricultural Sciences, S-750 07 Uppsala, Sweden
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Summary

Casein micelles fractionated on controlled pore glass (CPG-10/3000) were shown to be stable by recycling experiments. Only minor effects on the size distribution of the casein micelles were found after heating skim-milk to 100 °C for 10 min, or freeze-drying skim-milk at – 70 °C followed by resuspension in the synthetic milk serum of Jenness & Koops (1962). The heating caused some whey proteins (β-lactoglobulin) to enter the micelle fractions while the freeze-drying caused some of the largest micelles to disrupt. In colloidal calcium phosphate-free skim-milk prepared according to Pyne & McGann (1960) all the micelles appeared to dissociate into monomeric caseins.

Type
Section D. Casein Micelles
Information
Journal of Dairy Research , Volume 46 , Issue 2: Symposium on the Physics and Chemistry of Milk Proteins , April 1979 , pp. 313 - 316
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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References

REFERENCES

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