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Use of guanidinated dietary protein to measure losses of endogenous amino acids in poultry

Published online by Cambridge University Press:  09 March 2007

P. Siriwan ,
W. L. Bryden  and
E. F. Annison
P. Siriwan
Affiliation:
Department of Animal Science, University of Sydney, Camden, N.S. W., Australia
W. L. Bryden
Affiliation:
Department of Animal Science, University of Sydney, Camden, N.S. W., Australia
E. F. Annison
Affiliation:
Department of Animal Science, University of Sydney, Camden, N.S. W., Australia
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Abstract

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Guanidinated proteins when fed to non-ruminants provide values for both endogenous amino acid losses and amino acid digestibilities, provided that the homoarginine residues in the treated protein are randomly distributed. Earlier studies have established that guanidination has only minor effects on the structure of the protein and, in particular, on its susceptibility to proteolysis. Furthermore, we have confirmed that homoarginine behaves as a typical amino acid in the small intestine. Lysine residues in casein and soya-bean protein, and in the proteins of cotton-seed meal, meat meal, soya-bean meal, maize, sorghum and wheat were converted to homoarginine by guanidination, the extent of conversion ranging from 37–68%. Sequential proteolysis in vitro of these guanidinated materials showed that the ratios of homoarginine to other amino acids remained unchanged for casein and soya-bean protein, indicating random distribution of homoarginine residues, but not for all the amino acids in meals and cereals. The use of guanidinated casein as the sole protein source in diets fed to broiler chickens allowed measurement of endogenous losses of amino acids under normal feeding conditions and calculation of true digestibilities of dietary amino acids at the ileum. Endogenous amino acid losses measured by the use of guanidinated casein (15.3 g/kg dry matter (DM) intake) were significantly higher (P < 0.001) than values obtained by feeding a N-free diet (5.4 g/kg DM intake), or by regression analysis to zero N intake (72 g/kg DM intake)

Keywords

Endogenous amino acidsAmino acid digestibilityHomoarginineGuanidinationPoultry
Type
Amino acid utilization
Information
British Journal of Nutrition , Volume 71 , Issue 4 , April 1994 , pp. 515 - 529
Copyright
Copyright © The Nutrition Society 1994

References

REFERENCES

Austic, R. E. & Nesheim, M. C. (1970). Role of kidney arginase in variations of the arginine requirements of chicks. Journal of Nutrition 100, 855–869.CrossRefGoogle ScholarPubMed
Bryden, W. L. (1989). Intestinal distribution and absorption of biotin in the chicken. British Journal of Nutrition 62, 389–398.CrossRefGoogle ScholarPubMed
de Lange, C. F. M., Souffrant, W. L. & Sauer, W. C. (1990). Real ileal protein and amino acid digestibilities in feedstuffs for growing pigs as determined with the 15N-isotope dilution technique. Journal of Animal Science 68, 409–418.CrossRefGoogle ScholarPubMed
Hagemeister, H. & Erbersdobler, H. (1985). Chemical labelling of dietary protein by transformation of lysine to homoarginine: new technique to follow intestinal digestion and absorption. Proceedings of the Nutrition Society 44, 133A.Google Scholar
Maga, J. A. (1981). Measurement of available lysine using the guanidination reaction. Journal of Food Science 46, 132–134.CrossRefGoogle Scholar
Markland, F. S., Bacharach, A. D. E., Weber, B. H., O'Grady, T. C., Saunder, G. C. & Umeura, N. (1975) Chemical modification of yeast 3-phosphoglycerate kinase. Journal of Biological Chemistry 250, 1301–1310.CrossRefGoogle ScholarPubMed
Roos, N., Hagemeister, H. & Scholtissek, J. (1990). Protein digestibility measured by 15N and homoarginine. Proceedings of the Nutrition Society 49, 48A.Google Scholar
Rutherford, S. M. & Moughan, P. J. (1990). Guanidination of lysine in selected dietary proteins. Journal of Agricultural and Food Chemistry 38, 209–211.Google Scholar
Ryan, W. L., Barak, A. J. & Johnson, R. J. (1968). Lysine, homocitrulline and homoarginine metabolism by the isolated perfused rat liver. Archives of Biochemistry and Biophysics 123, 294–297.CrossRefGoogle ScholarPubMed
Schmitz, M., Hagemeister, H. & Erbersdobler, H. F. (1991). Homoarginine labelling is suitable for determination of protein absorption in miniature pigs. Journal of Nutrition 121, 1575–1580.Google Scholar
Schuttert, G., Moughan, P. J. & Jackson, F. (1991). In vitro determination of the extent of hydrolysis of homoarginine by arginase in the small intestine of the growing rat. Journal of Agricultural and Food Chemistry 39, 511–513.CrossRefGoogle Scholar
Sibbald, I. R. (1987). Estimation of bioavailable amino acids in feedstuffs for poultry and pigs: a review with emphasis on balance experiments. Canadian Journal of Animal Science 67, 221–300.Google Scholar
Siriwan, P., Bryden, W. L. & Annison, E. F. (1987). The use of homoarginine to correct ileal digestibility values for endogenous amino acids. Proceedings of the Nutrition Society of Australia 12, 103.Google Scholar
Siriwan, P., Bryden, W. L. & Annison, E. F. (1989). The use of homoarginine to determine true amino acid digestibility. Proceedings of the Nutrition Society of Australia 14, 97.Google Scholar
Siriwan, P., Bryden, W. L., Mollah, Y. & Annison, E. F. (1993). Measurement of endogenous amino acid losses in poultry. British Poultry Science (In the Press).Google Scholar
Skurray, G. R. & Cumming, R. B. (1975). Deamination of amino acids in the small intestine of chickens fed meat meal. Poultry Science 54, 1689–1692.Google Scholar
Smith, G. H. & Lewis, D. (1963). Arginine in poultry nutrition. 2. Chick arginase. British Jozirnal of Nutrition 17, 415–444.Google Scholar