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The effect of dietary homoarginine derived from guanidination of synthetic lysine on endogenous amino acid loss and apparent and true ileal amino acid digestibility in the pig

Published online by Cambridge University Press:  09 March 2007

H. L. Zhang ,
D. F. Li ,
S. Y. Qiao ,
F. L. Wang ,
X. J. Chen  and
P. A. Thacker
H. L. Zhang
Affiliation:
National Key Laboratory in Animal Nutrition, China Agricultural University, Beijing, No. 2. Yuanmingyuan West Road, Beijing, 100094, People's Republic of China
D. F. Li*
Affiliation:
National Key Laboratory in Animal Nutrition, China Agricultural University, Beijing, No. 2. Yuanmingyuan West Road, Beijing, 100094, People's Republic of China
S. Y. Qiao
Affiliation:
National Key Laboratory in Animal Nutrition, China Agricultural University, Beijing, No. 2. Yuanmingyuan West Road, Beijing, 100094, People's Republic of China
F. L. Wang
Affiliation:
National Key Laboratory in Animal Nutrition, China Agricultural University, Beijing, No. 2. Yuanmingyuan West Road, Beijing, 100094, People's Republic of China
X. J. Chen
Affiliation:
National Key Laboratory in Animal Nutrition, China Agricultural University, Beijing, No. 2. Yuanmingyuan West Road, Beijing, 100094, People's Republic of China
P. A. Thacker
Affiliation:
Department of Animal Science, 51 Campus Drive, University of Saskatchewan, Saskatoon, Saskatchewan, S7N 5A8, Canada
*
†E-mail: defali@public2.bta.net.cn/qiaoshy@mafic.ac.cn
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Abstract

These studies were conducted to determine whether dietary homoarginine, derived from guanidination of synthetic lysine, affects the measurement of apparent and true ileal amino acid digestibility in the pig and to determine the optimal ratio of o-methylisourea (OMIU) to free synthetic lysine in the guanidination reaction that produces homoarginine. In two preliminary experiments, specific amounts of lysine were weighed and added to a solution of 0·6 mol/l OMIU to produce OMIU to free synthetic lysine ratios of 2:1, 1·5:1, 1·4:1, 1·3:1, 1·2:1, 1·1:1 and 1·0:1. The mixture was incubated at a pH of 10·5 and a temperature of 20±1°C for 6 days. The highest yield of homoarginine (proportionately 0·995) was produced with an OMIU to free synthetic lysine ratio of 1·5:1. The serum concentrations of homoarginine and lysine were measured in two test pigs at various times after consuming a single meal containing either homoarginine or lysine. Blood samples were taken before and 0·5, 1·5, 2·5, 4·5, 6·0, 7·5, and 11·5 h after feeding. Thirty minutes after feeding the homoarginine-containing diet, the homoarginine concentration in serum was 0·013 mmol/dl, and increased to a maximum of 0·031 mmol/dl 1·5 h after feeding. Thirty minutes after feeding the lysine-containing diet, the serum lysine concentration was 0·011 mmol/dl and also reached its maximum concentration of 0·025 mmol/dl 1·5 h after feeding. The timing of the changes in concentration of homoarginine and lysine related to feeding were similar, which suggests that homoarginine is absorbed and metabolized in a similar manner to lysine. Six Large White×Landrace barrows, weighing 68·5±3·5 kg and fitted with a simple T-cannula at the distal ileum as well as a jugular vein catheter, were used to determine the effects of homoarginine on endogenous amino acid flows and apparent and true ileal amino acid digestibility. The experimental design was a doubly replicated 3×3 Latin-square design with the three treatments consisting of a lysine-free, zein-based diet and jugular infusion of a lysine solution; a lysine-free, zein-based diet supplemented with homoarginine; and a lysine-free, zein-based diet supplemented with l-lysine. There were no significant differences in endogenous ileal lysine flow for pigs receiving the different treatments (396·6, 407·6, and 360·4 mg/kg DMI, respectively, P=0·71). In addition, with the exception of phenylalanine (P=0·04), there were no significant differences (P>0·10) in the apparent and true ileal digestibility of crude protein and amino acids among the three treatments. Therefore, it would appear that the presence of dietary homoarginine, derived from guanidination of synthetic lysine, does not affect endogenous amino acid losses or the digestibility of crude protein as well as most amino acids. These results are therefore supportive of the use of the homoarginine method as a means of measuring true ileal lysine digestibility.

Keywords

digestibilityhomoarginineileumlysinepigs
Type
Research Article
Information
Animal Science , Volume 82 , Issue 1 , February 2006 , pp. 23 - 30
Copyright
Copyright © British Society of Animal Science 2006

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References

Association of Official Analytical Chemists. 1990. Official methods of analysis, 15th edition. Association of Official Analytical Chemists, Washington, DC.Google Scholar
Bergner, H., Drochner, W. and Bartel, J. 1994. Secretion of endogenous protein independent of protein and fibre intake of 15N-labelled pigs. Proceedings of the sixth international symposium on digestive physiology in pigs (ed. Souffrant, W. B. and Hagemei-ser, H.), pp. 11–13. EAAP publication, Dummerstorf.Google Scholar
Boisen, S. and Moughan, P. J. 1996. Dietary influences on endogenous ileal protein and amino acid loss in the pig: a review. Acta Agriculturæ Scandinavica Section A, Animal Science 46: 154–164.Google Scholar
Butts, C. A., Moughan, P. J., Smith, W. C. and Car, D. H. 1993. Endogenous lysine and other amino acid flows at the terminal ileum of the growing pig (20 kg bodyweight): The effect of protein-free, synthetic amino acid, peptide and protein alimentation. Journal of the Science of Food and Agriculture 61: 31–40.CrossRefGoogle Scholar
De Lange, C. F. M., Sauer, W. C., Mosenthin, R. and Souffrant, W. B. 1989a. The effect of feeding different protein-free diets on the recovery and amino acid composition of endogenous proteins collected from the distal ileum and feces in pigs. Journal of Animal Science 67: 745–754.Google ScholarPubMed
De Lange, C. F. M., Sauer, W. C. and Souffrant, W. B. 1989b. The effect of protein status of the pig on the recovery and amino acid composition of endogenous protein in digesta collected from the distal ileum. Journal of Animal Science 67: 755–762.CrossRefGoogle ScholarPubMed
Donkoh, A. and Moughan, P. J. 1999. Endogenous ileal nitrogen and amino acid flows in the growing pig receiving a protein-free diet and diets containing enzymatically hydrolyzed casein or graded levels of meat and bone meal. Animal Science 68: 511–518.CrossRefGoogle Scholar
Drescher, K., Hagemeister, H., De Vrese, M., Roos, N., Middendorf, K. and Rantamäki, P. 1994. Guanidination (homoar-ginine-labeling) of proteins does affect prececal 15N recovery in pigs. Proceedings of the sixth international symposium on digestive physiology in pigs (ed. Souffrant, W. B. and Hagemeiser, H.), pp. 64–66. EAAP publication, Dummerstorf.Google Scholar
Fan, M. Z., Sauer, W. C., Hardin, R. T. and Lien, K. A. 1994. Determination of apparent ileal amino acid digestibility in pigs: effect of dietary amino acid level. Journal of Animal Science 72: 2851–2859.CrossRefGoogle ScholarPubMed
Fan, M. Z., Sauer, W. C. and McBurney, M. I. 1995. Estimation by regression analysis of endogenous amino acid levels in digesta collected from the distal ileum of pigs. Journal of Animal Science 73: 2318–2319.CrossRefGoogle ScholarPubMed
GabertV., M., Jorgensen, H. and Nyachoti, C. M. 2001. Bioavail-ability of amino acids in feedstuffs for swine. Swine nutrition, second edition (ed. Lewis, A. J. and Southern, L. L.), pp. 151–177. CRC Press, Boca Raton, FL.Google Scholar
Hagemeister, H. and Erbersdobler, H. 1985. Chemical labeling of dietary protein by transformation of lysine to homoarginine: A new technique to follow intestinal digestion and absorption Proceeding of the Nutrition Society 44: 133A.Google Scholar
Imbeah, M., Angkanaporn, K., Ravindran, V. and Bryden, W. L. 1996. Investigations on the guanidination of lysine in proteins. Journal of the Science of Food and Agriculture 72: 213–218.3.0.CO;2-N>CrossRefGoogle Scholar
Li, S., Sauer, W. C. and Fan, M. Z. 1993. The effect of dietary crude protein level on amino acid digestibility in early-weaned pigs. Journal of Animal Physiology and Animal Nutrition 70: 26–37.CrossRefGoogle Scholar
Maga, J. A. 1981. Measurement of available lysine using the guanidination reaction. Journal of Food Science 46: 132–134.CrossRefGoogle Scholar
Marty, B. J., Chavez, E. R. and De Lange, C. F. M. 1994. Recovery of amino acids at the distal ileum for determining apparent and true ileal amino acid digestibilities in growing pigs fed various heat-processed full-fat soybean products. Journal of Animal Science 72: 2029–2037.CrossRefGoogle ScholarPubMed
Means, G. E. and Feeney, R. E. 1971. Selected techniques for modification of protein side chains. In Chemical modification of proteins. pp. 68–104. Holden-Day, San Francisco, CA.Google Scholar
Moughan, P. J. and Rutherfurd, S. M. 1990. Endogenous flow of total lysine and other amino acids at the distal ileum of the protein- or peptide-fed rat: The chemical labeling of gelatine protein by transformation of lysine to homoarginine. Journal of the Science of Food and Agriculture 52: 179–192.CrossRefGoogle Scholar
Moughan, P. J., Schuttert, G. and Leenaars, M. 1992. Endogenous amino acid flow in the stomach and small intestine of the young growing pig. Journal of the Science of Food and Agriculture 62: 437–442.CrossRefGoogle Scholar
Nyachoti, C. M., De Lange, C. F. M., McBride, B. W. and Schulze, H. 1997a. Significance of endogenous gut nitrogen losses in the nutrition of growing pigs: a review. Canadian Journal of Animal Science 77: 149–163.CrossRefGoogle Scholar
Nyachoti, C. M., De Lange, C. F. M. and Schulze, H. 1997b. Estimating endogenous amino acid flows at the terminal ileum and true ileal amino acid digestibilities in feedstuffs for growing pigs using the homoarginine method. Journal of Animal Science 75: 3206–3213.CrossRefGoogle ScholarPubMed
Nyachoti, C. M., McNeilage-Van de Wiele, E. M., De Lange, C. F. M. and Gabert, V. M. 2002b. Evaluation of the homoarginine technique for measuring true ileal amino acid digestibilities in pigs fed a barley-canola meal-based diet. Journal of Animal Science 80: 440–448.CrossRefGoogle ScholarPubMed
Ravindran, V., Hew, I. and Bryden, W. L. 1998. Influence of guanidination on apparent ileal amino acid digestibility in some protein sources for broilers. Poultry Science 77: 873–877.CrossRefGoogle ScholarPubMed
Rutherfurd, S. M. and Moughan, P. J. 1990. Guanidination of lysine in selected dietary proteins. Journal of Agricultural and Food Chemistry 38: 209–211.CrossRefGoogle Scholar
Schmitz, M., Hagemeister, H. and Erbersdobler, H. F. 1991. Homoarginine labeling is suitable for determination of protein absorption in miniature pigs. Journal of Nutrition 121: 1575–1580.CrossRefGoogle ScholarPubMed
Smith, C. A. and Ficken, M. D. 1991. Non-surgical cannulation of the vena cava for chronic blood collection in mature swine. Laboratory Animal Science 41: 274–278.Google ScholarPubMed
Statistical Analysis System Institute. 1999. SAS/STAT users guide, version 6, fourth edition. SAS Institute Inc., Cary, NC.Google Scholar
Wang, F. L. 2004 Energy and protein requirement of lactating sows. Ph.D. dissertation, China Agricultural University, Beijing.Google Scholar
Williams, C. H., David, D. J. and Lismaa, O. 1962. The determination of chromic oxide in feces samples by atomic absorption spectrophotometry. Journal of Agriculture Science 59: 381–385.CrossRefGoogle Scholar
Zhang, H. L., Qiao, S. Y., Chen, X. J., Wang, X., Xing, J. J. and Yin, Y. L. 2005. Effects of graded levels of soya-bean protein on endogenous ileal lysine loss and amino acid digestibility in growing pigs. Animal Science 81: 257–264.CrossRefGoogle Scholar
Zhu, X. P., Li, D. F., Qiao, S. Y., Xiao, C. T., Qiao, Q. Y. and Ji, C. 1998. Evaluation of HP300 soybean protein in starter pig diets. Asian-Australian Journal of Animal Science 11: 201–207.CrossRefGoogle Scholar