Hostname: page-component-848d4c4894-v5vhk Total loading time: 0 Render date: 2024-06-28T19:12:56.410Z Has data issue: false hasContentIssue false
  • English
  • Français

DL-methionyl-DL-methionine as an efficient methionine source for promoting zootechnical performance and methionine-related pathways in the whiteleg shrimp (Penaeus vannamei)

Published online by Cambridge University Press:  11 January 2023

Marina Machado Open the ORCID record for Marina Machado [Opens in a new window] ,
Sergio Fernández-Boo Open the ORCID record for Sergio Fernández-Boo [Opens in a new window] ,
Carla Teixeira ,
Michael Viegas ,
Renata Serradeiro ,
Jorge Dias ,
Benjamín Costas Refojos  and
Karthik Masagounder
Marina Machado*
Affiliation:
Centro Interdisciplinar de Investigação Marinha e Ambiental (CIIMAR), Universidade do Porto, Terminal de Cruzeiros do Porto de Leixões, Avenida General Norton de Matos s/n, 4450-208, Matosinhos, Portugal
Sergio Fernández-Boo
Affiliation:
Centro Interdisciplinar de Investigação Marinha e Ambiental (CIIMAR), Universidade do Porto, Terminal de Cruzeiros do Porto de Leixões, Avenida General Norton de Matos s/n, 4450-208, Matosinhos, Portugal
Carla Teixeira
Affiliation:
Centro Interdisciplinar de Investigação Marinha e Ambiental (CIIMAR), Universidade do Porto, Terminal de Cruzeiros do Porto de Leixões, Avenida General Norton de Matos s/n, 4450-208, Matosinhos, Portugal Instituto de Ciências Biomédicas Abel Salazar (ICBAS-UP), Universidade do Porto, Rua de Jorge Viterbo Ferreira 228, 4050-123, Porto, Portugal
Michael Viegas
Affiliation:
SPAROS Lda., Área Empresarial de Marim, Lote C, Olhão, Portugal
Renata Serradeiro
Affiliation:
RIASEARCH Lda, Cais da Ribeira de Pardelhas 21, Murtosa, Portugal
Jorge Dias
Affiliation:
SPAROS Lda., Área Empresarial de Marim, Lote C, Olhão, Portugal
Benjamín Costas Refojos
Affiliation:
Centro Interdisciplinar de Investigação Marinha e Ambiental (CIIMAR), Universidade do Porto, Terminal de Cruzeiros do Porto de Leixões, Avenida General Norton de Matos s/n, 4450-208, Matosinhos, Portugal Instituto de Ciências Biomédicas Abel Salazar (ICBAS-UP), Universidade do Porto, Rua de Jorge Viterbo Ferreira 228, 4050-123, Porto, Portugal
Karthik Masagounder
Affiliation:
Evonik Operations GmbH, Rodenbacher Chaussee 4, 63457 Hanau-Wolfgang, Germany
*
*Corresponding author: Marina Machado, email [email protected]
Get access Rights & Permissions [Opens in a new window]

Abstract

Methionine (MET) supplementation is a current strategy to achieve shrimp requirement. Notwithstanding, the efficiency of the precisely formulated feeds can be diminished since shrimps are slow eaters and masticate feed externally that results in nutrient leaching. In this regard, a methionine dipeptide (DL-methionyl DL-methionine) benefits the feed industry by reducing MET water solubility while increasing its bioavailability. Therefore, the effects of feeding whiteleg shrimp (Penaeus vannamei) with increasing levels of methionine dipeptide were evaluated on zootechnical performance and methionine-, immune- and antioxidant-related pathways. A 74 d growth trial was conducted by feeding a control diet and four diets supplemented with AQUAVI® Met-Met at 0·08, 0·12, 0·24 and 0·32% of DM. Diet digestibility, body amino acids (AA) composition and nitrogen metabolites, metabolic enzymes, oxidative status and gene expression were evaluated. It can be concluded that graded dietary increase of methionine dipeptide up to 0·24 % for 74 d translated in significant gains on the growth performance, feed efficiency, nutrient and nitrogen gain and shrimp survival. Moreover, it was showed that Met-Met dietary spare leads to an improvement of free-AA pool and nitrogen metabolites concentration and reduces the signs of oxidative stress. Finally, in a closer look to the MET-related pathways passive to be altered by Met-Met spare, a clear modulation of the described antioxidant and cell proliferation routes was detected.

Keywords

ImmunonutritionAntioxidant responseImmune systemGrowth
Type
Research Article
Information
British Journal of Nutrition , Volume 130 , Issue 4 , 28 August 2023 , pp. 616 - 632
Check for updates
Copyright
© Interdisciplinary Centre of Marine and Environmental Research of the University of Porto, 2023. Published by Cambridge University Press on behalf of The Nutrition Society

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

NRC (2011) Nutrient Requirements of Fish and Shrimp. Washington, DC: The National Academies Press.Google Scholar
FAO (2016) The State of World Fisheries and Aquaculture 2016 (SOFIA): Contributing to Food Security and Nutrition for All. Rome: Food and Agriculture Organization. pp. 200.Google Scholar
Lee, C & Lee, K-J (2018) Dietary protein requirement of Pacific white shrimp Litopenaeus vannamei in three different growth stages. Fisheries Aquat Sci 21, 30.CrossRefGoogle Scholar
Goff, JB & Gatlin, DM (2004) Evaluation of different sulfur amino acid compounds in the diet of red drum, Sciaenops ocellatus, and sparing value of cystine for methionine. Aquaculture 241, 465–477.CrossRefGoogle Scholar
Kaushik, SJ, Cravedi, JP, Lalles, JP, et al. (1995) Partial or total replacement of fish meal by soybean protein on growth, protein utilization, potential estrogenic or antigenic effects, cholesterolemia and flesh quality in rainbow trout, Oncorhynchus mykiss. Aquaculture 133, 257–274.CrossRefGoogle Scholar
Xie, J-J, Lemme, A, He, J-Y, et al. (2018) Fishmeal levels can be successfully reduced in white shrimp (Litopenaeus vannamei) if supplemented with DL-Methionine (DL-Met) or DL-Methionyl-DL-Methionine (Met-Met). Aquacult Nutr 24, 1144–1152.CrossRefGoogle Scholar
Li, P, Mai, KS, Trushenski, J & Wu, GY (2009) New developments in fish amino acid nutrition: towards functional and environmentally oriented aquafeeds. Amino Acids 37, 43–53.CrossRefGoogle ScholarPubMed
Le Floc’h, N, Melchior, D & Obled, C (2004) Modifications of protein and amino acid metabolism during inflammation and immune system activation. Livest Prod Sci 87, 37–45.CrossRefGoogle Scholar
Azeredo, R, Serra, CR, Oliva-Teles, A, et al. (2017) Amino acids as modulators of the European seabass, Dicentrarchus labrax, innate immune response: an in vitro approach. Sci Rep-UK 7, 18009.CrossRefGoogle ScholarPubMed
Grillo, MA & Colombatto, S (2008) S-adenosylmethionine and its products. Amino Acids 34, 187–193.CrossRefGoogle ScholarPubMed
Grimble, RF & Grimble, GK (1998) Immunonutrition: role of sulfur amino acids, related amino acids, and polyamines. Nutrition 14, 605–610.CrossRefGoogle ScholarPubMed
Laxman, S, Sutter, BM & Tu, BP (2014) Methionine is a signal of amino acid sufficiency that inhibits autophagy through the methylation of PP2A. Autophagy 10, 386–387.CrossRefGoogle ScholarPubMed
Martinez, Y, Li, X, Liu, G, et al. (2017) The role of methionine on metabolism, oxidative stress, and diseases. Amino Acids 49, 2091–2098.CrossRefGoogle ScholarPubMed
Niculescu, MD & Zeisel, SH (2002) Diet, methyl donors and DNA methylation: interactions between dietary folate, methionine and choline. J Nutr 132, 2333s–2335s.CrossRefGoogle ScholarPubMed
Van Brummelen, R & du Toit, D (2007) L-methionine as immune supportive supplement: a clinical evaluation. Amino Acids 33, 157–163.CrossRefGoogle ScholarPubMed
Williams, KT & Schalinske, KL (2010) Homocysteine metabolism and its relation to health and disease. BioFactors 36, 19–24.Google ScholarPubMed
Igarashi, K & Kashiwagi, K (2000) Polyamines: mysterious modulators of cellular functions. Biochem Bioph Res Co 271, 559–564.CrossRefGoogle ScholarPubMed
Waterland, RA (2006) Assessing the effects of high methionine intake on DNA methylation. J Nutr 136, 1706S–1710S.CrossRefGoogle ScholarPubMed
Sutter Benjamin, M, Wu, X, Laxman, S, et al. (2013) Methionine Inhibits Autophagy and Promotes Growth by Inducing the SAM-Responsive Methylation of PP2A. Cell 154, 403–415.CrossRefGoogle ScholarPubMed
Luo, S & Levine, RL (2009) Methionine in proteins defends against oxidative stress. FASEB J 23, 464–472.CrossRefGoogle ScholarPubMed
Levine, RL, Berlett, BS, Moskovitz, J, et al. (1999) Methionine residues may protect proteins from critical oxidative damage. Mech Ageing Dev 107, 323–332.CrossRefGoogle ScholarPubMed
Li, P, Yin, YL, Li, D, et al. (2007) Amino acids and immune function. Br J Nutr 98, 237–252.CrossRefGoogle ScholarPubMed
Wu, B, Cui, H, Peng, X, et al. (2012) Pathology of spleen in chickens fed on a diet deficient in methionine. Health 4, 32–38.CrossRefGoogle Scholar
Bunchasak, C (2009) Role of dietary methionine in poultry production. J Poult Sci 46, 169–179.CrossRefGoogle Scholar
Azeredo, R, Machado, M, Guardiola, FA, et al. (2017) Local immune response of two mucosal surfaces of the European seabass, Dicentrarchus labrax, fed tryptophan- or methionine-supplemented diets. Fish Shell Immun 70, 76–86.CrossRefGoogle ScholarPubMed
Machado, M, Azeredo, R, Diaz-Rosales, P, et al. (2015) Dietary tryptophan and methionine as modulators of European seabass (Dicentrarchus labrax) immune status and inflammatory response. Fish Shell Immun 42, 353–362.CrossRefGoogle ScholarPubMed
Machado, M, Azeredo, R, Fontinha, F, et al. (2018) Dietary methionine improves the European seabass (dicentrarchus labrax) immune status, inflammatory response, and disease resistance. Front Immunol 9, 2672.CrossRefGoogle ScholarPubMed
Machado, M, Engrola, S, Colen, R, et al. (2020) Dietary methionine supplementation improves the European seabass (Dicentrarchus labrax) immune status following long-term feeding on fish meal free diets. Br J Nutr 1–29.Google Scholar
Machado, M, Moura, J, Peixoto, D, et al. (2021) Dietary methionine as a strategy to improve innate immunity in rainbow trout (Oncorhynchus mykiss) juveniles. Gen Comp Endocr 302, 113690.CrossRefGoogle ScholarPubMed
Richard, L, Blanc, P-P, Rigolet, V, et al. (2010) Maintenance and growth requirements for nitrogen, lysine and methionine and their utilisation efficiencies in juvenile black tiger shrimp, Penaeus monodon, using a factorial approach. Br J Nutr 103, 984–995.CrossRefGoogle ScholarPubMed
Dabrowski, K, Zhang, Y, Kwasek, K, et al. (2010) Effects of protein-, peptide- and free amino acid-based diets in fish nutrition. Aquacult Res 41, 668–683.CrossRefGoogle Scholar
Ji, R, Wang, Z, He, J, et al. (2021) Effects of DL-methionyl-DL-methionine supplementation on growth performance, immune and antioxidative responses of white leg shrimp (Litopenaeus vannamei) fed low fishmeal diet. Aquacult Rep 21, 100785.Google Scholar
Niu, J, Lemme, A, He, J-Y, et al. (2018) Assessing the bioavailability of the Novel Met-Met product (AQUAVI® Met-Met) compared to dl-methionine (dl-Met) in white shrimp (Litopenaeus vannamei). Aquaculture 484, 322–332.CrossRefGoogle Scholar
AOAC (2006) Official Methods of Analysis of Association of Official Analytical Chemists International. Gaithersburg, MD: AOAC.Google Scholar
Bolin, DW, King, RP & Klosterman, EW (1952) A simplified method for the determination of chromic oxide (Cr2 O3) when used as an index substance. Science 116, 634–635.CrossRefGoogle ScholarPubMed
Zar, JH (1999) Biostatistical Analysis. Ilinois; Englewood Cliffs, NJ: Prentice-HaIl.Google Scholar
Mamauag, REP, Gao, J, Thanh Nguyen, B, et al. (2012) Supplementations of dl-methionine and methionine dipeptide in diets are effective for the development and growth of larvae and juvenile red sea bream, pagrus major. J World Aquacult Soc 43, 362–374.CrossRefGoogle Scholar
Tesser, MB, Terjesen, BF, Zhang, Y, et al. (2005) Free- and peptide-based dietary arginine supplementation for the South American fish pacu (Piaractus mesopotamicus). Aquacult Nutr 11, 443–453.CrossRefGoogle Scholar
Engel, PC & Paradisi, F (2010) 5.03 – Novel enzymes for biotransformation and resolution of alpha-amino acids. In Comprehensive Natural Products II, pp. 71–90 [Liu, H-W & Mander, L, editors]. Oxford: Elsevier.CrossRefGoogle Scholar
Yancey, PH, Clark, ME, Hand, SC, et al. (1982) Living with water stress: evolution of osmolyte systems. Science 217, 1214–1222.CrossRefGoogle ScholarPubMed
Yancey, PH (2001) Fish physiology, nitrogen excretion. In Nitrogen Compounds as Osmolytes, pp. 309–341 [Wright, P & Anderson, P, editors]. San Diego: Academic Press.Google Scholar
Greenaway, P (2001) The Crustacea. Oxford: Oxford Press. pp. 292–324.Google Scholar
Augusto, A, Greene, LJ, Laure, HJ, et al. (2007) The ontogeny of isosmotic intracellular regulation in the diadromous, freshwater palaemonid shrimps, Macrobrachium amazonicum and M. olfersi (Decapoda). J Crustacean Biol 27, 626–634.CrossRefGoogle Scholar
Nakamura, K, Iwaizumi, K & Yamada, S (2007) Hemolymph patterns of free amino acids in the brine shrimp Artemia franciscana after three days starvation at different salinities. Comp Biochem Physiol A: Mol Integr Physiol 147, 254–259.CrossRefGoogle ScholarPubMed
Shinji, J, Okutsu, T, Jayasankar, V, et al. (2012) Metabolism of amino acids during hyposmotic adaptation in the whiteleg shrimp, Litopenaeus vannamei. Amino Acids 43, 1945–1954.CrossRefGoogle ScholarPubMed
Halliwell, B & Gutteridge, JM (2015) Free Radicals in Biology and Medicine. Oxford: Oxford University Press.CrossRefGoogle Scholar
Brigelius-Flohé, R (2006) Glutathione peroxidases and redox-regulated transcription factors. Biol Chem 387, 1329–1335.CrossRefGoogle ScholarPubMed
Weissbach, H, Etienne, F, Hoshi, T, et al. (2002) Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function. Arch Biochem Biophys 397, 172–178.CrossRefGoogle ScholarPubMed
Pegg, AE (2009) S-Adenosylmethionine decarboxylase. Essays Biochem 46, 25–45.Google ScholarPubMed
Pegg, AE (2008) Spermidine/spermine-N(1)-acetyltransferase: a key metabolic regulator. Am J Physiol - Endocrinol Metab 294, E995–E1010.CrossRefGoogle ScholarPubMed
Zhang, N (2017) Role of methionine on epigenetic modification of DNA methylation and gene expression in animals. Anim Nutr 4, 11–16.CrossRefGoogle ScholarPubMed
Mills, CD (2001) Macrophage arginine metabolism to ornithine/urea or nitric oxide/citrulline: a life or death issue. Crit Rev Immunol 21, 399–425.CrossRefGoogle ScholarPubMed
Parkhitko, AA, Jouandin, P, Mohr, SE, et al. (2019) Methionine metabolism and methyltransferases in the regulation of aging and lifespan extension across species. Aging Cell 18, e13034-e.CrossRefGoogle ScholarPubMed
McKeever, MP, Weir, DG, Molloy, A, et al. (1991) Betaine-homocysteine methyltransferase: organ distribution in man, pig and rat and subcellular distribution in the rat. Clin Sci 81, 551–556.CrossRefGoogle ScholarPubMed
Hunter, EAL & Grimble, RF (1997) Dietary sulphur amino acid adequacy influences glutathione synthesis and glutathione dependent enzymes during the inflammatory response to endotoxin and tumour necrosis factor-α in rats. Clin Sci 92, 297–305.CrossRefGoogle ScholarPubMed