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Studies in rats on the nutritional value of hydrogen peroxide-treated fish protein and the utilization of oxidized sulphur-amino acids

Published online by Cambridge University Press:  09 March 2007

L. B. SjÖberg  and
S. L. BostrÖm
L. B. SjÖberg
Affiliation:
Astra Nutrition AB, Fack, S-431 20 Mölndal, Sweden
S. L. BostrÖm
Affiliation:
Astra Nutrition AB, Fack, S-431 20 Mölndal, Sweden
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Abstract

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1. The nutritional value of fish protein oxidized with different levels of hydrogen peroxide, and the utilization of oxidized sulphur-amino acids in the rat were investigated.

2. The results showed that the biological value (bv) and protein efficiency ratio (per) of the fish protein were significantly decreased by the treatment with H2O2, and although there were no significant differences between samples treated with 20, 40 or 80 g H2O2/kg, there was a gradual decrease of BV at higher concentrations. Digestibility was not affected by the treatment.

3. Supplementation with 1 g L-methionine/kg or 1 g L-cystine/kg significantly increased the BV for all H2O2-treated samples. With the exception of the sample treated with 80 g H2O2/kg, the BV was increased by L-methionine supplementation to the level for the untreated fish protein.

4. Treatment with H2O2 led to the formation of methionine sulphoxide, methionine sulphone and cysteic acid. The availability of these compounds was studied as supplements to the untreated fish protein as well as to the H2O2-treated fish protein. The results showed that L-methionine DL-sulphoxide was as available as methionine, but that L-methionine sulphone and cysteic acid had no supplementary effect.

5. The availability of lysine in fish protein was not affected by treatment with 20 g H2O2/kg as judged by its effect as a supplement to wheat flour.

6. The plasma amino acid pattern for rats given a diet with H2O2-treated fish protein was identical to that for rats given an untreated fish protein, with the exception of the presence of the two isomers of L-methionine DL-sulphoxide and L-methionine sulphone. The oxidized S-amino acids were also found in liver, kidney and gastrocnemius muscle from the rat.

7. Only traces of L-methionine DL-sulphoxide were found in the urine. About half the ingested L-methionine sulphone was found in the urine and almost all was present as an acid-labile conjugate.

Type
Research Article
Information
British Journal of Nutrition , Volume 38 , Issue 2 , September 1977 , pp. 189 - 205
Copyright
Copyright © The Nutrition Society 1977

References

REFERENCES

Anderson, G. H., Li, G. S. K., Jones, J. D. & Bender, F. (1975). J. Nutr. 105, 317.CrossRefGoogle Scholar
Association of Official Analytical Chemists (1970). Official Methods of Analysis. Washington, DC: Association of Official Analytical Chemists.Google Scholar
Byington, M. H., Hoove, J. M. & Clark, H. E. (1972). J. Nutr. 102, 219.CrossRefGoogle Scholar
Cuq, J. L., Provansal, M., Guilleux, F. & Cheftel, C. (1973). J. Fd Sci. 38, 11.CrossRefGoogle Scholar
Eggum, B. (1973). In Protein in Human Nutrition, p. 317. [J.W.G., Porter and B., A. Rolls, editors.] London and New York: Academic Press.Google Scholar
Ellinger, G. M. & Palmer, R. (1969). Proc. Nutr. Soc. 28, 42 A.Google Scholar
Gray, W. R. & Hartley, B. S. (1963). Biochem. J. 89, 59.CrossRefGoogle Scholar
Gros, C. & Labousse, B. (1969). Eur. J. Biochem. 7, 463.CrossRefGoogle Scholar
Hills, G. L. & Thiel, G. C. (1945). J. Dairy Res. 14, 340.CrossRefGoogle Scholar
Ivanetich, K. M., Bradstrom, J. J. & Kaminsky, L. S. (1976). Biochemistry, Easton 15, 1144.CrossRefGoogle Scholar
Jeppsson, J. O. & Karlsson, I. M. (1972). J. Chromatog. 72, 93.CrossRefGoogle Scholar
Kido, K. & Kassell, B. (1975). Biochemistry, Easton 14, 631.CrossRefGoogle Scholar
Miller, D. S. & Samuel, P. (1968). Proc. Nutr. Soc. 27, 21 A.Google Scholar
Miller, S. A., Tannenbaum, S. R. & Seitz, A. W. (1970). J. Nutr. 100, 909.CrossRefGoogle Scholar
Moore, S. (1963). J. biol. Chem. 238, 235.CrossRefGoogle Scholar
Neumann, N. P. (1967). Meth. Enzym. 11, 485.CrossRefGoogle Scholar
Njaa, L. R. (1962). Br. J. Nutr. 16, 571.CrossRefGoogle Scholar
Perry, T. L. & Hansen, S. (1969). Clinica chim. Acta 25, 53.CrossRefGoogle Scholar
Rasekh, J., Stillings, B. R. & Sidwell, R. (1972). J. Fd Sci. 37, 423.CrossRefGoogle Scholar
Slump, P. & Schreuder, H. A. W. (1973). J. Sci. Fd Agric. 24, 657.CrossRefGoogle Scholar
Smith, R. C. (1972). Biochim. Biophys. Acta 261, 304.CrossRefGoogle Scholar
Spies, J. R. & Chambers, D. C. (1948). Analyt. Chem. 20, 30.CrossRefGoogle Scholar
Spies, J. R. & Chambers, D. C. (1949). Analyt. Chem. 21, 1249.CrossRefGoogle Scholar
Stein, W. H. & Moore, S. (1954). J. biol. Chem. 211, 915.CrossRefGoogle Scholar
Stillings, B. R., Hammerle, O. H. & Snyder, D. G. (1969). J. Nutr. 97, 70.CrossRefGoogle Scholar
US Pharmacopoeia, XIV (1950). p. 789.Google Scholar
Wingo, W. J., Smith, R. A. & Wood, J. (1953). Archs Biochem. Biophys. 47, 307.CrossRefGoogle Scholar
Womack, M. & Rose, W. C. (1941). J. biol. Chem. 141, 375.CrossRefGoogle Scholar