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Metabolism of heat-damaged proteins in the rat

Influence of heat damage on the excretion of amino acids and peptides in the urine

Published online by Cambridge University Press:  19 January 2009

J. E. Ford  and
C. Shorrock
J. E. Ford
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading RG2 9AT
C. Shorrock
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading RG2 9AT
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Abstract

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1. Freeze-dried cod muscle and casein were subjected to various conditions of heat treat-ment. Diets containing the different products, or the unheated materials, were given to a group of four adult male rats during successive 48 h periods, and urine was collected during the second 24 h of each 48 h period. A further collection of urine was made from the rats after they had been given protein isolated from heated skim-milk powder. The content and amino acid composition of the ‘peptide’ and ‘free amino acids’ in the urines were determined.

2. Heat damage to the cod-fillet protein increased the total urinary excretion of peptide-bound amino acids, from 18·6 to 48·8 µmol/rat.d. The composition of the peptide also changed, and in particular there was a marked increase in lysine, from 2·98 to 20·30 µmol %. Three amino acids - lysine, aspartic acid and glutamic acid - together comprised nearly 70 % of the total amino acid residues. There was a corresponding increase in urinary excretion of free amino acids, from 53·7 to I 14·4 µmol/rat.d. The combined losses of lysine in urinary peptide and free amino acids were 1·5 % of the total lysine ingested, as against 0·3 % for the unheated cod fillet.

3. The effects of similar heat treatment of casein on the composition of the urinary peptide and free amino acids were less marked. There was no increase in total urinary peptide excretion and there was a smaller increase in the lysine content of the peptide.

4. In urine of rats given protein isolated from heated skim-milk powder, the peptide hydro-lysate was rich in lysine and in furosine, which together comprised 41 mol % of the total amino acid composition. These compounds were presumably formed, together with a smaller quantity of pyridosine, from lysine-carbohydrate complex in the urine. It is probable that, as compared with free lysine, the lysine-carbohydrate complex was absorbed relatively in-efficiently from the rat intestine.

5. The findings are discussed in relation to the wider question of the metabolism of the ‚unavailable peptide’ that is released in the course of digestion of heat-damaged protein.

Type
General Nutrition
Information
British Journal of Nutrition , Volume 26 , Issue 2 , September 1971 , pp. 311 - 322
Copyright
Copyright © The Nutrition Society 1971

References

REFERENCES

Ackroyd, H. & Hopkins, F. G. (1916). Biochem. J. 10, 551.Google Scholar
Andrews, P. (1964). Biochem. J. 91, 222.Google Scholar
Barman, T. E. (1969). Enzyme Handbook Vol. 2, p. 644. Heidelburg: Springer Verlag.Google Scholar
Bjarnason, J. & Carpenter, K. J. M. (1970). Br. J. Nutr. 24, 313.Google Scholar
Bunyan, J. & Price, S. A. (1960). J. Sci. Fd Agric. 11, 25.CrossRefGoogle Scholar
Buraczewski, S., Buraczewska, L. & Ford, J. E. (1967). Acta biochom. pol. 14, 121.Google Scholar
Carpenter, K. J. (1960). Biochem. J. 77, 604.Google Scholar
Dawson, R. & Porter, J. W. G. (1962). Br. J. Nutr. 16, 27.Google Scholar
Donoso, G., Lewis, O. A. M., Miller, D. S. & Payne, P. R. (1962). J. Sci. Fd Agric. 13, 192.Google Scholar
Finot, P. A., Bricout, J., Viani, R. & Mauron, J. (1968). Experientia 24, 1097.CrossRefGoogle Scholar
Finot, P. A., Viani, R., Bricout, J. & Mauron, J. (1969). Experientia 25, 134.Google Scholar
Fleck, A. & Munro, H. N. (1965). Clinica chim. Acta 11, 2.Google Scholar
Ford, J. E. (1962). Br. J. Nutr. 16, 409.Google Scholar
Ford, J. E. (1965). Br. J. Nutr. 19, 277.Google Scholar
Ford, J. E. & Salter, D. N. (1966). Br. J. Nutr. 20, 843.Google Scholar
Heyns, K., Heukeshoven, J. & Brose, K. H. (1968). Angew. Chemie 80, 627.Google Scholar
Mauron, J. (1970). Int. Z. VitamForsch. 40, 209.Google Scholar
Miller, D. S. (1956). J. Sci. Fd Agric. 7, 337.CrossRefGoogle Scholar
Miller, E. L., Carpenter, K. J. & Milner, C. K. (1965). Br. J. Nutr. 19, 547.CrossRefGoogle Scholar
Sauberlich, H. E., Pearse, E. L. & Baumann, C. A. (1948). J. biol. Chem. 175, 29.CrossRefGoogle Scholar
Spackman, D. H., Stein, W. H. & Moore, S. (1958). Analyt. Chem. 30, 1190.Google Scholar
Wu, C. (1954). J. biol. Chem. 207, 775.Google Scholar