Effects of Oral Administration of Encapsulated-Leucine on Amino Acid and Plasma Metabolite Profiles in Broiler Chicks During the Starter Phase
DOI:
https://doi.org/10.3923/ijps.2020.252.256Abstract
Background and Objective: An abundant studies show that leucine (Leu) acts as an anabolic agent that stimulates skeletal muscle growth in human as well as in animals. However, the effect of encapsulated leucine (CL) supplementation on growth performance of broiler chickens has not been evaluated. Therefore, the aim of this study was to determine initial metabolic responses to CL supplementation on food intake, plasma metabolites and branched chain amino acid concentration in 7-day-old broiler chicks. Materials and Methods: A total of 24 chicks were randomly assigned to the following treatments: (1) Control 4 h (C), (2) Free leucine 4h (L) and (3) Encapsulated-leucine 4h (CL). After 6 h of fasting, chicks were given a bolus of oral injection of distilled water, free leucine (6 mmol/10 mL kg–1 BW) or encapsulated-leucine (6 mmol/10 mL kg–1 BW). Immediately after the injection, chicks were allowed free access to a commercial starter diet for 1 h. Blood collections were obtained 4 h after the oral injection. Food intake, total glucose, total cholesterol, triacylglycerol, plasma leucine levels and the activity of glutamic oxaloacetic transaminase (GOT) were measured. Results: Food intake, glucose, total cholesterol and triacylglycerol levels were not affected by Leu supplementation. At 4 h, GOT levels were greater (p<0.05) in the CL group than that of the Leu groups. At 4 h, although plasma Leu levels were similar in all groups, Valine levels were lower (p<0.005) in the C and CL groups than that of the Leu group and isoleucine levels were lower (p<0.001) in the CL group than that of the C and Leu groups. Conclusion: The results of this study suggest that an oral administration of CL caused prolonged leucine-induced anabolic effects that may be beneficial for growth. Our observations also pave the way for studying the long-term effects of CL supplementation on performance of broiler chicks.
References
Reeds, P.J., D.G. Burrin, T.A. Davis, M.L. Fiorotto, B. Stoll and J.B.v. Goudoever, 2000. Protein nutrition of the neonate. Proc. Nutr. Soc., 59: 87-97.
Davis, T.A. and M.L. Fiorotto, 2009. Regulation of muscle growth in neonates. Curr. Opin. Clin. Nutr. Metab. Care, 12: 78-85.
Columbus, D.A., M.L. Fiorotto and T.A. Davis, 2015. Leucine is a major regulator of muscle protein synthesis in neonates. Amino Acids, 47: 259-270.
Suryawan, A., R.A. Orellana, M.L. Fiorotto and T.A. Davis, 2011. Triennial growth symposium: Leucine acts as a nutrient signal to stimulate protein synthesis in neonatal pigs. J. Anim. Sci., 89: 2004-2016.
Erwan, E., A.R. Alimon, A.Q. Sazili and H. Yaakub, 2008. Effect of varying levels of leucine and energy on performance and carcass characteristics of broiler chickens. Int. J. Poult. Sci., 7: 696-699.
Layman, D.K., T.G. Anthony, B.B. Rasmussen, S.H. Adams, C.J. Lynch, G.D. Brinkworth and T.A. Davis, 2015. Defining meal requirements for protein to optimize metabolic roles of amino acids. Am. J. Clinic. Nutr., 101: 1330S-1338S.
Manjarín, R., D.A. Columbus, J. Solis, A.D. Hernandez-García and A. Suryawan et al., 2018. Short- and long-term effects of leucine and branched-chain amino acid supplementation of a protein- and energy-reduced diet on muscle protein metabolism in neonatal pigs. Amino Acids, 50: 943-959.
Wilson, G.J., C.J. Moulton, P.J. Garlick, T.G. Anthony and D.K. Layman, 2012. Post-meal responses of elongation factor 2 (eEF2) and adenosine monophosphate-activated protein kinase (AMPK) to leucine and carbohydrate supplements for regulating protein synthesis duration and energy homeostasis in rat skeletal muscle. Nutrients, 13: 1723-1739.
Koenig, K.M. and L.M. Rode, 2001. Ruminal degradability, intestinal disappearance and plasma methionine response of rumen-protected methionine in dairy cows. J. Dairy Sci., 84: 1480-1487.
Dahiya, J.P., D. Hoehler, A.G.V. Kessel and M.D. Drew, 2007. Dietary encapsulated glycine influences Clostridium perfringens and lactobacilli growth in the gastrointestinal tract of broiler chickens. J. Nutr., 137: 1408-1414.
Webb, K.E., 1990. Intestinal absorption of protein hydrolysis products: A review. J. Anim. Sci., 68: 3011-3022.
Erwan, E., V.S. Chowdhury, K. Ito and M. Furuse, 2013. Lauroyl-L-aspartate decreased food intake and body temperature in neonatal chicks. Pharmacol. Biochem. Behav., 113: 7-11.
SAS, 1998. Stat view, version 5. SAS Institute, Cary, North Carolina
Koch, C.E., S. Göddeke, M. Krüger and A. Tups, 2013. Effect of central and peripheral leucine on energy metabolism in the Djungarian hamster (Phodopus sungorus) J. Comp. Physiol., 183: 261-268.
Edmonds, M.S. and D. Baker, 1987. Comparative effects of individual amino acid excesses when added to a corn-soybean meal diet: Effects on growth and dietary choice in the chick. J. Anim. Sci., 65: 699-705.
Edmonds, M.S. and D.H. Baker, 1987. Amino acid excesses for young pigs: Effects of excess methionine, tryptophan, threonine or leucine J. Anim. Sci., 64: 1664-1671.
Penz, Jr. A.M., A.J. Clifford, Q.R. Rogers and F.H. Kratzer, 1984. Failure of dietary leucine to influence the tryptophan-niacin pathway in chicken. J. Nutr., 114: 33-41.
D`Mello, J.P.F. and D. Lewis, 1970. Amino acids interaction in chick nutrition. Interrelationships between leucine, isoleucine and valine. Br. Poult. Sci., 11: 313-323.
Williams, L.R., F.A. Martz and E.S. Hilderbrand, 1970. Feeding encapsulated methionine supplement to lactating cows. J. Dairy Sci., 53: 1709-1713.
Ospina-Rojas, I.C., A.E. Murakami, C.R.A. Duarte, G.R. Nascimento, E.R.M. Garcia, M.I. Sakamoto and R.V. Nunes, 2017. Leucine and valine supplementation of low-protein diets for broiler chickens from 21 to 42 days of age. Poult. Sci., 96: 914-922.
Zhang, Y., K. Guo, R.E. LeBlanc, D. Loh, G.J. Schwartz and Y.H. Yu, 2007. Increasing dietary leucine intake reduces diet-induced obesity and improves glucose and cholesterol metabolism in mice via multimechanisms. Diabetes, 56: 1647-1654.
Higuchi, N., M. Kato, M. Miyazaki, M. Tanaka and M. Kohjima et al., 2011. Potential role of branched‐chain amino acids in glucose metabolism through the accelerated induction of the glucose‐sensing apparatus in the liver. J. Cell. Biochem., 112: 30-38.
Xie, J., L. Tang, L. Lu, L. Zhang and X. Lin et al., 2015. Effects of acute and chronic heat stress on plasma metabolites, hormones and oxidant status in restrictedly fed broiler breeders. Poult. Sci., 94: 1635-1644.
Imaeda, N., 1999. Characterization of serum enzyme activities and electrolyte levels in broiler chickens after death from sudden death syndrome. Poult. Sci., 78: 66-69.
Valchev, I., D. Kanakov, T.S. Hristov, L. Lazarov, R. Binev, N. Grozeva and Y. Nikolov, 2014. Investigations on the liver function of broiler chickens with experimental aflatoxicosis. Bulg. J. Vet. Med., 17: 302-313.
Simth, T.K. and R.E. Austic, 1978. The branched-chain amino acid antagonism in chicks. J. Nutr., 108: 1180-1191.
Wilson, G.J., C.J. Moulton, P.J. Garlick, T.G. Anthony and D.K. Layman, 2012. Post-meal responses of elongation factor 2 (eEF2) and adenosine monophosphate-activated protein kinase (AMPK) to leucine and carbohydrate supplements for regulating protein synthesis duration and energy homeostasis in rat skeletal muscle. Nutrients, 13: 1723-1739.
Downloads
Published
Issue
Section
License
Copyright (c) 2020 The Author(s)

This work is licensed under a Creative Commons Attribution 4.0 International License.
This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution and reproduction in any medium, provided the original author and source are credited.