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The participation of methionine and cysteine in the formation of bonds resistant to the action of proteolytic enzymes in heated casein

Published online by Cambridge University Press:  09 March 2007

Danuta Pieniaźek ,
Maria Rakowska  and
Hanna Kunachowicz
Danuta Pieniaźek
Affiliation:
Institute of Food and Nutrition, Warszawa, Powsińka 61/63, Poland
Maria Rakowska
Affiliation:
Institute of Food and Nutrition, Warszawa, Powsińka 61/63, Poland
Hanna Kunachowicz
Affiliation:
Institute of Food and Nutrition, Warszawa, Powsińka 61/63, Poland
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Abstract

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1. The influence of temperature, moisture content and the presence of glucose on the level of available methionine and cysteine in casein was studied.

2. Differences between total and available methionine and cysteine contents of heated casein (90° for 24 h) were determined by an in vitro method. The maximum losses in total and available methionine content were 22 and 51% respectively. The losses in total and available cysteine content were 24 and 100% respectively.

3. The results indicated that for heated casein the release of amino acids by proteolytic enzymes was less complete than for native casein.

4. The results of rat growth assays suggested that diets containing oxidized casein are less well utilized by rats than those containing native casein. The decrease in body-weight of rats receiving the diets containing oxidized casein could be counteracted by the addition of methionine and 20 g unoxidized casein/kg diet.

5. There was a lower level of some available amino acids (determined after enzymic hydrolysis using pancreatopeptidase E (EC 3.4.4.7), leucine aminopeptidase (EC 3.4.1.1) and prolidase (EC 3.4.3.7)), including those essential for the rat, in oxidized casein as compared with native casein.

6. Cysteic acid, in oxidized casein, probably makes impossible the utilization of the amino acids in its neighbourhood.

7. From the differences in the available amino acid contents of the native, oxidized and heated casein it was concluded that the oxidation of casein causes the formation of complexes in the polypeptide chain, resistant to enzymic hydrolysis, but to a much lesser extent than does heating.

Type
Papers of direct relevance to Clinical and Human Nutrition
Information
British Journal of Nutrition , Volume 34 , Issue 2 , September 1975 , pp. 163 - 173
Copyright
Copyright © The Nutrition Society 1975

References

Bjarnason, J. & Carpenter, K. J. (1969). Br. J. Nutr. 23, 859.CrossRefGoogle Scholar
Bjarnason, J. & Carpenter, K. J. (1970). Br. J. Nutr. 24, 313.CrossRefGoogle Scholar
Carpenter, K. J. & Bjarnason, J. (1968). Proc. I.B.P. Symp., Stockholm p. 319.Google Scholar
Dawson, R. & Woodham, A. A. (1966). Proc. Nutr. Soc. 25, ix.Google Scholar
Ellinger, G. M. & Boyne, E. B. (1965). Br. J. Nutr. 19, 587.CrossRefGoogle Scholar
Ellinger, G. M. & Palmer, R. (1969). Proc. Nutr. Soc. 28, 42A.Google Scholar
El-Maraghi, N. R. H., Platt, B. S. & Stewart, R. J. C. (1965). Br. J. Nutr. 19, 491.CrossRefGoogle Scholar
Hawk, P. B., Oser, B. L. & Summerson, W. H. (1947). Practical Physiological Chemistry, p. 1163. Philadelphia: W. B. Saunders Co.Google Scholar
Kunachowicz, H. (1970). Investigation on net protein utilization coefficient (NPU) in relation to the growth rate of experimental animals. PhD Thesis, Institute of Food and Nutrition, Warsaw, Poland.Google Scholar
Miller, D. S. & Samuel, P. (1968). Proc. Nutr. Soc. 27, 21A.Google Scholar
Miller, E. L., Hartley, A. W. & Thomas, D. C. (1965). Br. J. Nutr. 19, 565.CrossRefGoogle Scholar
Moore, S., Spackman, D. H. & Stein, W. H. (1958). Analyt. Chem. 30, 1185.CrossRefGoogle Scholar
Njaa, L. R. (1962). Br. J. Nutr. 16, 571.CrossRefGoogle Scholar
Pieniaźek, D., Rakowska, M., Szkillpdziowa, W. & Grabarek, Z. (1975). Br. J. Nutr. 34, 175.CrossRefGoogle Scholar
Schweigert, B. S. & Guthneck, B. T. (1954). J. Nutr. 54, 333.CrossRefGoogle Scholar
Smith, E. L. (1955). Meth. Enzym. 2, 93.CrossRefGoogle Scholar
Toennies, G. (1942). J. biol. Chem. 145, 667.CrossRefGoogle Scholar
Waibel, P. E. & Carpenter, K. J. (1972). Br. J. Nutr. 27, 509.CrossRefGoogle Scholar
Wilkes, S. H., Bayliss, M. E. & Prescott, J. M. (1973). Eur. J. Biochem. 34, 459.CrossRefGoogle Scholar