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Cleavage of the linkage between colloidal calcium phosphate and casein on heating milk at high temperature

Published online by Cambridge University Press:  01 June 2009

Takayoshi Aoki
Affiliation:
Department of Animal Science, Faculty of Agriculture, Kagoshima University, Kagoshima 890, Japan
Taketoshi Umeda
Affiliation:
Department of Animal Science, Faculty of Agriculture, Kagoshima University, Kagoshima 890, Japan
Yoshitaka Kako
Affiliation:
Department of Animal Science, Faculty of Agriculture, Kagoshima University, Kagoshima 890, Japan

Summary

In order to examine the effect of heating on the changes in the linkage between colloidal Ca phosphate (CCP) and casein, high-performance gel chromatography of casein micelles disaggregated by 6 M-urea was carried out using 6 M-urea simulated milk ultrafiltrate as the effluent. Although the CCP content increased when whey protein-free (WPF) milk was heated at 60–90 °C for 10 min, almost no changes in the content of casein aggregates cross-linked by CCP were observed. The content of casein aggregates cross-linked by CCP decreased from 51·9 to 46·1% in WPF milk and from 52·3 to 43·6% in concentrated WPF milk on heating at 135–140 °C for 75 s, indicating the cleavage of the linkage between CCP and casein. The cleavage of the linkage between CCP and casein on heating was considered to occur without liberation of ester phosphate groups. It was suggested that the transformation of CCP to another form was responsible for the cleavage between CCP and casein on heating milk at high temperature

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1990

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References

REFERENCES

Allen, R. J. L. 1940 The estimation of phosphorus. Biochemical Journal 34 858865CrossRefGoogle ScholarPubMed
Aoki, T. & Imamura, T. 1974 Changes of the casein complex in sterilized concentrated skim milk during storage. Agricultural and Biological Chemistry 38 309314CrossRefGoogle Scholar
Aoki, T. & Imamura, T. 1975 Cold-disaggregation of the casein micelles in heated concentrated whey proteinfree milk. Agricultural and Biological Chemistry 39 21072113Google Scholar
Aoki, T. & Kako, Y. 1983 Relation between micelle size and formation of soluble casein on heating concentrated milk. Journal of Dairy Research 50 207213CrossRefGoogle Scholar
Aoki, T., Kako, Y. & Imamura, T. 1986 Separation of the casein aggregates cross-linked by colloidal calcium phosphate from bovine casein micelles by high performance gel chromatography in the presence of urea. Journal of Dairy Research 53 5359CrossRefGoogle Scholar
Aoki, T., Suzuki, H. & Imamura, T. 1974 Formation of soluble casein in whey protein-free milk heated at high temperature. Milchwissenschaft 29 589594Google Scholar
Aoki, T., Suzuki, H. & Imamura, T. 1975 Some properties of soluble casein in heated concentrated whey protein-free milk. Milchwissenschaft 30 3035Google Scholar
Aoki, T., Yamada, N., Tomita, I., Kako, Y. & Imamura, T. 1987 Caseins are cross-linked through their ester phosphate groups by colloidal calcium phosphate. Biochimica et Biophysica Acta 911 238243CrossRefGoogle ScholarPubMed
Fox, P. F. 1981 Heat-induced changes in milk preceding coagulation. Journal of Dairy Science 64 21272137CrossRefGoogle Scholar
Holt, C. 1982 Inorganic constituents of milk. III. The colloidal calcium phosphate of cow's milk. Journal of Dairy Research 49 2938CrossRefGoogle ScholarPubMed
Holt, C. 1985 The milk salts: their secretion, concentration and physical chemistry. In Developments in Dairy Chemistry-3. Lactose and minor constituents pp. 143181 (Ed. Fox, P. F.) London: Elsevier Applied Science PublishersGoogle Scholar
Holt, C., Hasnain, S. S. & Hukins, D. W. L. 1982 Structure of bovine milk calcium phosphate determined by X-ray absorption spectroscopy. Biochimica et Biophysica Acta 719 299303CrossRefGoogle ScholarPubMed
Irlam, J. C., Holt, C., Hasnain, S. S. & Hukins, D. W. L. 1985 Comparison of the structure of micellar calcium phosphate in milk from six species by extended X-ray absorption fine structure spectroscopy. Journal of Dairy Research 52 267273CrossRefGoogle Scholar
Nelson, L. S., Holt, C. & Hukins, D. W. L. 1989 The EXAFS spectra of poorly crystalline calcium phosphate preparations from heated milk. Physica B 158 103104CrossRefGoogle Scholar
Pyne, G. T. 1962 Reviews of the progress of dairy science. C. Dairy chemistry. Some aspects of the physical chemistry of the salts of milk. Journal of Dairy Research 29 101130CrossRefGoogle Scholar
Rose, D. & Colvin, J. R. 1966 Internal structure of casein micelles from bovine milk. Journal of Dairy Science 49 351355CrossRefGoogle ScholarPubMed
Schmidt, D. G. 1982 Association of caseins and casein micelle structure. In Developments in Dairy Chemistry-1. Proteins pp. 6186 (Ed. Fox, P. F.) London: Applied Science PublishersGoogle Scholar
Schmidt, D. G. & Both, P. 1987 Studies on the precipitation of calcium phosphate. I. Experiments in the pH range 5·3 to 6·8 at 25 °C and 50 °C in the absence of additives. Netherlands Milk and Dairy Journal 41 101120Google Scholar
Swaisgood, H. E. 1982 Chemistry of milk protein. In Developments in Dairy Chemistry-1. Proteins pp. 159 (Ed. Fox, P. F.) London: Applied Science PublishersGoogle Scholar
Van Kemenade, M. J. J. M. & De Bruyn, P. L. 1989 The influence of casein on the kinetics of hydroxyapatite precipitation. Journal of Colloid and Interface Science 129 114CrossRefGoogle Scholar