Hostname: page-component-586b7cd67f-t7czq Total loading time: 0 Render date: 2024-11-26T06:10:37.025Z Has data issue: false hasContentIssue false
  • English
  • Français

The amino acid composition of tissue protein is affected by the total sulfur amino acid supply in growing pigs

Published online by Cambridge University Press:  18 February 2014

J. A. Conde-Aguilera ,
C. Cobo-Ortega ,
Y. Mercier ,
S. Tesseraud  and
J. van Milgen
J. A. Conde-Aguilera
Affiliation:
INRA, UMR1348 PEGASE, F-35590 Saint-Gilles, France Agrocampus Ouest, UMR1348 PEGASE, F-35000 Rennes, France
C. Cobo-Ortega
Affiliation:
INRA, UMR1348 PEGASE, F-35590 Saint-Gilles, France Agrocampus Ouest, UMR1348 PEGASE, F-35000 Rennes, France
Y. Mercier
Affiliation:
Adisseo France SAS, F-92160 Antony, France
S. Tesseraud
Affiliation:
INRA, UR83 Recherches Avicoles, F-37380 Nouzilly, France
J. van Milgen*
Affiliation:
INRA, UMR1348 PEGASE, F-35590 Saint-Gilles, France Agrocampus Ouest, UMR1348 PEGASE, F-35000 Rennes, France
*
†E-mail: [email protected]
Get access

Abstract

The factorial approach to assess the amino acid (AA) requirements of pigs is based on the assumption that the AA composition of body protein is constant. However, there are indications that this assumption may not be valid because the AA composition of body protein can be affected by the AA supply. The extent to which different tissues are affected by an AA deficiency is unknown. The objective of this study was to investigate the effect of feeding pig diets with a deficient or sufficient total sulfur AA supply (TSAA; Met+Cys) from 6 to 23 weeks of age on tissue composition and meat quality. The deficient diet (TSAA–) provided 24% Met : Lys and 51% TSAA : Lys on a standardized ileal digestible basis, which are 19% and 16% below the recommended requirements, respectively. The sufficient diet (TSAA+) provided 33% Met : Lys and 60% TSAA : Lys. Diets were offered slightly below the ad libitum feed intake capacity of the pigs. Pigs offered diet TSAA– had a lower average daily gain, lower weights of the longissimus dorsi (LM) and rhomboideus muscles (RM), and of selected skin sections (P<0.05). The weight of different sections of the small intestine and the liver was not affected by the diet. The protein content of the LM and RM decreased in pigs offered diet TSAA– (P<0.05), whereas the protein content of other tissues was not affected. The TSAA supply affected the AA composition (g/16 g N) of protein in all tissues, but the Met content was changed only in the liver (P<0.05). Pigs receiving diet TSAA– had a lower Cys content in the RM and in the distal jejunum and ileum (P<0.01). The deficient TSAA supply resulted in a lower carcass weight and higher muscle glycogen stores (P<0.05), but did not affect other meat quality traits. The results of this study indicate that the muscles, jejunum and ileum respond more to a prolonged AA deficiency than the liver. In addition, the observed changes in AA composition of tissue protein question the use of a constant AA profile of retained protein to assess AA requirements.

Keywords

sulfur amino acidspigstissue compositiondeficiency
Type
Full Paper
Information
animal , Volume 8 , Issue 3 , March 2014 , pp. 401 - 409
Copyright
© The Animal Consortium 2014 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Bikker, P, Verstegen, MW and Bosch, MW 1994. Amino acid composition of growing pigs is affected by protein and energy intake. Journal of Nutrition 124, 1961–1969.Google Scholar
Caperna, TJ, Gavelek, D and Vossoughi, J 1994. Somatotropin alters collagen-metabolism in growing pigs. Journal of Nutrition 124, 770–778.Google Scholar
Chang, YM and Wei, HW 2005. The effects of dietary lysine deficiency on muscle protein turnover in postweanling pigs. Asian-Australasian Journal of Animal Sciences 18, 1326–1335.CrossRefGoogle Scholar
Chung, TK and Baker, DH 1992. Efficiency of dietary methionine utilization by young pigs. Journal of Nutrition 122, 1862–1869.Google Scholar
Cohen, SA, Meys, M and Tarvin, TL 1989. The pico tag method. A manual of advanced techniques for amino acid analysis. Millipore Corporation, Bedford, MA, USA.Google Scholar
Conde-Aguilera, JA, Barea, R, Le Floc'h, N, Lefaucheur, L and van Milgen, J 2010. A sulfur amino acid deficiency changes the amino acid composition of body protein in piglets. Animal 4, 1349–1358.CrossRefGoogle ScholarPubMed
Daumas, G 2008. Taux de muscle des pièces et appréciation de la composition corporelle des carcasses. Journées de la Recherche Porcine 40, 61–68.Google Scholar
Ebner, S, Schoknecht, P, Reeds, P and Burrin, D 1994. Growth and metabolism of gastrointestinal and skeletal muscle tissues in protein-malnourished neonatal pigs. American Journal of Physiology – Regulatory Integrative and Comparative Physiology 266, R1736–R1743.Google Scholar
Gahl, MJ, Finke, MD, Crenshaw, TD and Benevenga, NJ 1996. Efficiency of lysine or threonine retention in growing rats fed diets limiting in either lysine or threonine. Journal of Nutrition 126, 3090–3099.Google Scholar
Hamard, A, Seve, B and Le Floc'h, N 2007. Intestinal development and growth performance of early-weaned piglets fed a low-threonine diet. Animal 1, 1134–1142.Google Scholar
Hamard, A, Seve, B and Le Floc'h, N 2009. A moderate threonine deficiency differently affects protein metabolism in tissues of early-weaned piglets. Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology 152, 491–497.CrossRefGoogle ScholarPubMed
Henry, Y 1993. Affinement du concept de la protéine idéale pour le porc en croissance. INRA Productions Animales 6, 199–212.Google Scholar
Honikel, KO 1998. Reference methods for the assessment of physical characteristics of meat. Meat Science 49, 447–457.Google Scholar
Kim, YI 2005. Nutritional epigenetics: impact of folate deficiency on DNA methylation and colon cancer susceptibility. Journal of Nutrition 135, 2703–2709.Google Scholar
Kyriazakis, I, Emmans, GC and McDaniel, R 1993. Whole body amino acid composition of the growing pig. Journal of the Science of Food and Agriculture 62, 29–33.Google Scholar
Lebret, B, Meunier-Salaun, MC, Foury, A, Mormede, P, Dransfield, E and Dourmad, JY 2006. Influence of rearing conditions on performance, behavioral, and physiological responses of pigs to preslaughter handling, carcass traits, and meat quality. Journal of Animal Science 84, 2436–2447.Google Scholar
Mahan, DC and Shields, RG Jr 1998. Essential and nonessential amino acid composition of pigs from birth to 145 kilograms of body weight, and comparison to other studies. Journal of Animal Science 76, 513–521.Google Scholar
Martinez-Ramirez, HR, Jeaurond, EA and de Lange, CFM 2008. Dynamics of body protein deposition and changes in body composition after sudden changes in amino acid intake: I. Barrows. Journal of Animal Science 86, 2156–2167.Google Scholar
Moore, S 1963. On the determination of cystine as cysteic acid. Journal of Biological Chemistry 238, 235–237.Google Scholar
National Research Council (NRC) 1998. Nutrient requirements of swine, 10th revised edition National Academy Press, Washington, DC, USA.Google Scholar
Pearson, AM and Young, RB 1989. Muscle and meat biochemistry. Academic Press, London, UK.Google Scholar
Purchas, RW, Morel, PCH, Janz, JAM and Wilkinson, BHP 2009. Chemical composition characteristics of the longissimus and semimembranosus muscles for pigs from New Zealand and Singapore. Meat Science 81, 540–548.Google Scholar
Sauvant, D, Perez, JM and Tran, G 2004. Tables of composition and nutritional value of feed materials. Pigs, poultry, cattle, sheep, goats, rabbits, horses, fish, 2nd edition INRA Editions, Paris, France.CrossRefGoogle Scholar
Schaart, MW, Schierbeek, H, van der Schoor, SRD, Stoll, B, Burrin, DG, Reeds, PJ and van Goudoever, JB 2005. Threonine utilization is high in the intestine of piglets. Journal of Nutrition 135, 765–770.CrossRefGoogle ScholarPubMed
Sève, B and Le Floc’h, N 1998. Valorisation mutuelle du L-tryptophane et de la L-thréonine supplémentaires dans l’aliment deuxième âge du porcelet. Journées de la Recherche Porcine 30, 209–216.Google Scholar
Spangenburg, EE and Booth, FW 2003. Molecular regulation of individual skeletal muscle fibre types. Acta Physiologica Scandinavica 178, 413–424.CrossRefGoogle ScholarPubMed
Stipanuk, MH 2004. Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine. Annual Review of Nutrition 24, 539–577.Google Scholar
Stoll, B, Chang, XY, Fan, MZ, Reeds, PJ and Burrin, DG 2000. Enteral nutrient intake level determines intestinal protein synthesis and accretion rates in neonatal pigs. American Journal of Physiology – Gastrointestinal and Liver Physiology 279, G288–G294.Google Scholar
Talmant, A, Fernandez, X, Sellier, P and Monin, G 1989. Glycolytic potential in longissimus muscle of Large White pigs as measured after in vivo sampling. In Proceedings of the 35th International Congress of Meat Science and Technology, 20–25 August 1989, Copenhagen, Denmark, pp. 1129–1132.Google Scholar
Wei, HW and Fuller, M 2006. Dietary deficiencies of single amino acids: whole-body amino acid composition of adult rats. Archives of Animal Nutrition 60, 119–130.Google Scholar
Wyszcecki, G and Stiles, WS 1982. Color science. Concepts and methods, quantitative data and formula, 2nd revised edition John Wiley & Sons, New York, USA.Google Scholar
Supplementary material: PDF

Conde-Aguilera Supplementary Material

Table S1

Download Conde-Aguilera Supplementary Material(PDF)
PDF 19.8 KB