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Relation between micelle size and formation of soluble casein on heating concentrated milk

Published online by Cambridge University Press:  01 June 2009

Takayoshi Aoki and
Yoshitaka Kako
Takayoshi Aoki
Affiliation:
Animal Products Processing Research Laboratory, Faculty of Agriculture, Kagoshima University, Kagoshima 890, Japan
Yoshitaka Kako
Affiliation:
Animal Products Processing Research Laboratory, Faculty of Agriculture, Kagoshima University, Kagoshima 890, Japan
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Summary

In order to examine the influence of micelle size on the formation of soluble casein brought about by heating concentrated milk, casein micelles were separated into 3 fractions by differential centrifugation. The micelles were dispersed in the ultrafiltrate of skim-milk and the preparations were concentrated to 1/2·5 of the original volume. When the concentrated milk samples were heated at 135–140 °C, a larger amount of soluble casein was formed from smaller micelles than from larger micelles. Only a slight effect on the formation of soluble casein on heating was observed when colloidal calcium phosphate (CCP) was removed from the large micelles to a level lower than that associated with the small micelles or when the CCP in the small micelles was increased to a level higher than that of the large micelles. The soluble caseins formed on heating from different sizes of micelles were similar in composition. The fact that the formation of soluble casein on heating was affected by micelle size may be ascribed to variation in the κ-casein content of micelles rather than to variation in CCP content.

Information

Type
Original Articles
Information
Journal of Dairy Research , Volume 50 , Issue 2 , May 1983, pp. 207 - 213
Copyright
Copyright © Proprietors of Journal of Dairy Research 1983

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References

REFERENCES

Allen, R. J. L. 1940 The estimation of phosphorus. Biochemical Journal 34 858–865CrossRefGoogle ScholarPubMed
Aoki, T., Hatanaka, C. & Imamura, T. 1977 Large casein micelles and soluble casein in heated concentrated whey protein-free milk. Agricultural and Biological Chemistry 41 2349–2355Google Scholar
Aoki, T. & Imamura, T. 1974 Changes of the casein complex in sterilized concentrated skim milk during storage. Agricultural and Biological Chemistry 38 309–314Google Scholar
Aoki, T.& Imamura, T. 1975 Cold-disaggregationofthe casein micelles in heated concentrated whey protein-free milk. Agricultural and Biological Chemistry 39 2107–2113Google Scholar
Aoki, T.& Imamura, T. 1976 [Effects of urea. EDTA, and pH on the disaggregation of casein micelles in heated concentrated whey protein-free milk. ] Journal of the Agricultural Chemical Society of Japan 50 99–104Google Scholar
Aoki, T., Suzuki, H. & Imamura, T. 1974 Formation of soluble casein in whey protein-free milk heated at high temperature. Milchwissenschaft 29 589–594Google Scholar
Aoki, T., Suzuki, H. & Imamvra, T. 1975 Some properties of soluble casein in heated concentrated whey protein-free milk. Milchwissenschaft 30 30–35Google Scholar
Carroll, R. J., Thompson, M. P. & Nuttino, G. C. 1968 Glutaraldehyde fixation of casein micelles for electron microscopy. Journal of Dairy Science 51 1903–1908CrossRefGoogle Scholar
Ekstrand, B. & Larsson-Raźnikiewicz, M. 1978 The monomeric casein composition of different size bovine casein micelles. Biochimica et Biophysica Acta 536 1–9Google Scholar
Fox, K. K., Harper, M. K., Holsinger, V. H. & Pallansch, M. J. 1967 Effects of high-heat treatment on stability of calcium caseinate aggregates in milk. Journal of Dairy Science 50 443–450CrossRefGoogle Scholar
Kenkare, D. B. & Hansen, P. M. T. 1967 Reversible heat-induced dissociation of the alpha-casein complex. Journal of Dairy Science 50 135–141CrossRefGoogle ScholarPubMed
McGann, T. C. A., Donnelly, W. J., Kearney, R. D.& Buchheim, W. 1980 Composition and size distribution of bovine casein micelles. Biochimica et Biophysica Ada 630 261–270CrossRefGoogle ScholarPubMed
Morr, C. V. 1969 Protein aggregation in conventional and ultra high-temperature heated skimmilk. Journal of Dairy Science 52 1174–1180CrossRefGoogle Scholar
Ono, T., Hayakawa, Y. & Odaoiri, S. 1975 [The changes of the constituents of bovine casein micelles by calcium complexing agents.] Journal of the Agricultural Chemical Society of Japan 49 417–424Google Scholar
Rose, D. & Colvin, J. R. 1966 Appearance and size of micelles from bovine milk. Journal of Dairy Science 49 1091–1097CrossRefGoogle ScholarPubMed
Rose, D., Davies, D. T. & Yaouchi, M. 1969 Quantitative determination of the major components of casein mixtures by column chromatography on DEAE-cellulose. Journal of Dairy Science 52 8–11Google Scholar
Sabarwal, P. K.Oommen, S. & Ganguli, N. C. 1972 Inorganic constituents of casein micelles from cow and buffalo milk. Journal of Food Science and Technology (Mysore) 9 144–146Google Scholar
Schmidt, D. G. 1980 Colloidal aspects of casein. Netherlands Milk and Dairy Journal 34 42–64Google Scholar
Schmidt, D. G., Walstra, P. & Buchheim, W. 1973 The size distribution of casein micelles in cow's milk. Netherlands Milk and Dairy Journal 27 128–142Google Scholar
Slattery, C. W. 1976 Review: casein micelle structure; an examination of models. Journal of Dairy Science 59 1547–1556CrossRefGoogle ScholarPubMed
Vreeman, H. J. 1979 The association of bovine SH-κ-casein at pH 7·0. Journal of Dairy Research 46 271–276CrossRefGoogle ScholarPubMed