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Covalent bonds formed in proteins during milk sterilization: studies on caseins and casein peptides

Published online by Cambridge University Press:  01 June 2009

Denis Lorient
Affiliation:
Service de Biochimie Appliquée, Université de Nancy I, C.O. 140-F. 54037 Nancy, France

Summary

Formation of covalent bonds at milk sterilization temperatures was studied using caseins and casein peptides. At 120°C lysinoalanyl residues produced even at pH 7·0 were derived from intra-molecular interactions between phospho-serine and lysine; the conditions of formation were determined. It was also found that the formation of isopeptidic cross-links was significant with conditions more severe than those used for milk sterilization.

Type
Section E. Applied aspects of milk protein research
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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References

BEFERENCES

Aymard, C., Cuq, J. L. & Cheftel, J. C. (1977). Food Chemistry (in the Press).Google Scholar
Bjarnason, J. & Carpenter, K. J. (1970). British Journal of Nutrition 24, 313.CrossRefGoogle Scholar
Carpenter, K. J. (1960). Biochemical Journal 77, 604.CrossRefGoogle Scholar
De Groot, A. P. & Slump, P. (1969). Journal of Nutrition 98, 45.CrossRefGoogle Scholar
Kimmel, J. R. (1967). In Methods in Enzymology, vol. xi, p. 584. London: Academic Press.Google Scholar
Klostermeyer, H. & Reimerdes, E. H. (1976). American Chemical Society Centennial Meeting, San Francisco, Abstract of Paper, AGFD 56.Google Scholar
Lorient, D. & Linden, G. (1976). Journal of Dairy Research 43, 19.CrossRefGoogle Scholar
Manson, W. & Carolan, T. (1972). Journal of Dairy Research 39, 189.CrossRefGoogle Scholar
Mercier, J. C., Maubois, J. L., Poznanski, S. & Ribadeau Dumas, B. (1968). Bulletin de la Société de Chimie Biologique 50, 521.Google Scholar
Pisano, J. J., Finlayson, J. S. & Peyton, M. P. (1968). Science 160, 892.CrossRefGoogle Scholar
Schroeder, W. A., Jones, R. I., Cormick, J. & McCalla, K. (1962). Analytical Chemistry 34, 1570.CrossRefGoogle Scholar
Sternberg, M. & Kim, C. Y. (1977). In Protein Crosslinking, Nutritional and Medical Consequences, p. 73. (Ed. Friedman, M.). Plenum Press.CrossRefGoogle Scholar
Sternberg, M., Kim, C. Y. & Schwende, F. J. (1975). Science 190, 992.CrossRefGoogle Scholar
Woods, K. R. & Wang, K. T. (1967). Biochimica et Biophysica Acta 133, 369.CrossRefGoogle Scholar