Asian-Australasian Journal of Animal Sciences

Asian Australasian Association of Animal Production Societies (아세아태평양축산학회)
권호 표지
DOI QR코드

DOI QR Code

Studies on meat color, myoglobin content, enzyme activities, and genes associated with oxidative potential of pigs slaughtered at different growth stages

  • Yu, Qin Ping (College of Animal Science, South China Agricultural University) ;
  • Feng, Ding Yuan (College of Animal Science, South China Agricultural University) ;
  • Xiao, Juan (College of Animal Science, South China Agricultural University) ;
  • Wu, Fan (College of Animal Science, South China Agricultural University) ;
  • He, Xiao Jun (College of Animal Science, South China Agricultural University) ;
  • Xia, Min Hao (College of Animal Science, South China Agricultural University) ;
  • Dong, Tao (College of Animal Science, South China Agricultural University) ;
  • Liu, Yi Hua (College of Animal Science, South China Agricultural University) ;
  • Tan, Hui Ze (Guangdong Wen's Foodstuffs Group Co., Ltd.) ;
  • Zou, Shi Geng (Guangdong Wen's Foodstuffs Group Co., Ltd.) ;
  • Zheng, Tao (Nong Zhi Dao Co., Ltd.) ;
  • Ou, Xian Hua (Nong Zhi Dao Co., Ltd.) ;
  • Zuo, Jian Jun (College of Animal Science, South China Agricultural University)
  • Received : 2017.01.04
  • Accepted : 2017.04.25
  • Published : 2017.12.01
Download PDF
⟨ Previous Next ⟩

Abstract

Objective: This experiment investigated meat color, myoglobin content, enzyme activities, and expression of genes associated with oxidative potential of pigs slaughtered at different growth stages. Methods: Sixty 4-week-old $Duroc{\times}Landrace{\times}Yorkshire$ pigs were assigned to 6 replicate groups, each containing 10 pigs. One pig from each group was sacrificed at day 35, 63, 98, and 161 to isolate longissimus dorsi and triceps muscles. Results: Meat color scores were higher in pigs at 35 d than those at 63 d and 98 d (p<0.05), and those at 98 d were lower than those at 161 d (p<0.05). The total myoglobin was higher on 161 d compared with those at 63 d and 98 d (p<0.05). Increase in the proportions of metmyoglobin and deoxymyoglobin and a decrease in oxymyoglobin were observed between days 35 and 161 (p<0.05). Meat color scores were correlated to the proportion of oxymyoglobin (r = 0.59, p<0.01), and negatively correlated with deoxymyoglobin and metmyoglobin content (r = -0.48 and -0.62, p<0.05). Malate dehydrogenase (MDH) activity at 35 d and 98 d was higher than that at 161 d (p<0.05). The highest lactate dehydrogenase/MDH ratio was achieved at 161 d (p<0.05). Calcineurin mRNA expression decreased at 35 d compared to that at 63 d and 98 d (p<0.05). Myocyte enhancer factor 2 mRNA results indicated a higher expression at 161 d than that at 63 d and 98 d (p<0.05). Conclusion: Porcine meat color, myoglobin content, enzyme activities, and genes associated with oxidative potential varied at different stages.

Keywords

References

  1. Miller KD, Ellis M, Mckeith FK, et al. Frequency of the Rendement Napole RN-allele in a population of American Hampshire pigs. J Anim Sci 2000;78:1811-5. https://doi.org/10.2527/2000.7871811x
  2. Mancini RA, Kropf DH, Hunt MC, Johnson DE. Effects of endpoint temperature, pH, and storage time on cooked internal color reversion of pork longissimus chops. J Muscle Foods 2005;16:16-26. https://doi.org/10.1111/j.1745-4573.2004.07103.x
  3. Ki CN. Mechanisms of color change and the prevention of off-color and off-flavor in irradiated meat [Ph. D Dissertation]. Ames, IA, USA: Iowa State University; 2002.
  4. Ngapo TM, Gariepy C. Factors affecting the eating quality of pork. Crit Rev Food Sci Nutr 2008;48:599-633. https://doi.org/10.1080/10408390701558126
  5. Bekhit A, Faustman C. Metmyoglobin reducing activity. Meat Sci 2005;71:407-39. https://doi.org/10.1016/j.meatsci.2005.04.032
  6. Viriyarattanasak C, Hamada-Sato N, Watanabe M, et al. Equations for spectrophotometric determination of relative concentrations of myoglobin derivatives in aqueous tuna meat extracts. Food Chem 2011;127:656-61. https://doi.org/10.1016/j.foodchem.2011.01.001
  7. Tang J, Faustman C, Hoagland TA, et al. Postmortem oxygen consumption by mitochondria and its effects on myoglobin form and stability. J Agric Food Chem 2005;53:1223-30. https://doi.org/10.1021/jf048646o
  8. Bekhit AED, Cassidy L, Hurst RD, Farouk MM. Post-mortem metmyoglobin reduction in fresh venison. Meat Sci 2007;75:53-60. https://doi.org/10.1016/j.meatsci.2006.06.015
  9. Olsson V, Pickova J. The influence of production systems on meat quality, with emphasis on pork. AMBIO 2005;34:338-43. https://doi.org/10.1579/0044-7447(2005)034[0338:TIOPSO]2.0.CO;2
  10. Kim G, Jeong J, Hur S, et al. The relationship between meat color (CIE L* and a*), myoglobin content, and their influence on muscle fiber characteristics and pork quality. Korean J Food Sci Anim Res 2010;30:626-33. https://doi.org/10.5851/kosfa.2010.30.4.626
  11. Yamada T, Furuichi Y, Takakura H, et al. Interaction between myoglobin and mitochondria in rat skeletal muscle. J Appl Physiol 2013;114:490-7. https://doi.org/10.1152/japplphysiol.00789.2012
  12. Mckeith RO, King DA, Grayson AL, et al. Mitochondrial abundance and efficiency contribute to lean color of dark cutting beef. Meat Sci 2016;116:165-73. https://doi.org/10.1016/j.meatsci.2016.01.016
  13. Gaspar P, Neves AR, Shearman CA, et al. The lactate dehydrogenases encoded by the ldh and ldhB genes in Lactococcus lactis exhibit distinct regulation and catalytic properties-comparative modeling to probe the molecular basis. FEBS J 2007;274:5924-36. https://doi.org/10.1111/j.1742-4658.2007.06115.x
  14. Mohan A, Hunt MC, Muthukrishnan S, et al. Myoglobin redox form stabilization by compartmentalized lactate and malate dehydrogenases. J Agric Food Chem 2010;58:7021-9. https://doi.org/10.1021/jf100714g
  15. Weller P, A Price M, Isenberg H, et al. Myoglobin expression: early induction and subsequent modulation of myoglobin and myoglobin mRNA during myogenesis. Mol Cell Biol 1986;6:4539-47. https://doi.org/10.1128/MCB.6.12.4539
  16. Bigard X, Sanchez H, Zoll J, et al. Calcineurin co-regulates contractile and metabolic components of slow muscle phenotype. J Biol Chem 2000;275:19653-60. https://doi.org/10.1074/jbc.M000430200
  17. Bassel-Duby R, Olson EN. Role of calcineurin in striated muscle: development, adaptation, and disease. Biochem Biophys Res Commun 2003;311:1133-41. https://doi.org/10.1016/j.bbrc.2003.09.020
  18. Lin J, Handschin C, Spiegelman BM. Metabolic control through the PGC-1 family of transcription coactivators. Cell Metabol 2005;1:361-70. https://doi.org/10.1016/j.cmet.2005.05.004
  19. NRC. Committee on Nutrient Requirements of Swine, National Research Council. Nutrient requirements of swine. 11th ed. Washington, DC: National Academy Press; 2012.
  20. NPPC. Color measurement on pork carcasses. Color quality meeting. Ames, IA: Iowa State Univercity; 1996. pp. 8-9.
  21. Li YS, Zhu NH, Niu PP, et al. Effects of dietary chromium methionine on growth performance, carcass composition, meat colour and expression of the colour-related gene myoglobin of growing-finishing pigs. Asian-Australas J Anim Sci 2013;26:1021-9. https://doi.org/10.5713/ajas.2013.13012
  22. Krzywicki K. The determination of haem pigments in meat. Meat Sci 1982;7:29-36. https://doi.org/10.1016/0309-1740(82)90095-X
  23. Tang J, Faustman C, Hoagland TA. Krzywicki revisited: Equations for spectrophotometric determination of myoglobin redox forms in aqueous meat extracts. J Food Sci 2004;69: C717-C20.
  24. Bornez R, Linares MB, Vergara H. Systems stunning with $CO_2$ gas on Manchego light lambs: Physiologic responses and stunning effectiveness. Meat Sci 2009;82:133-8. https://doi.org/10.1016/j.meatsci.2009.01.003
  25. Nava G, Laclette JP, Bobes R, et al. Cloning, sequencing and functional expression of cytosolic malate dehydrogenase from Taenia solium: Purification and characterization of the recombinant enzyme. Exp Parasitol 2011;128:217-24. https://doi.org/10.1016/j.exppara.2011.03.008
  26. Ryu YC, Choi YM, Kim BC. Variations in metabolite contents and protein denaturation of the longissimus dorsi muscle in various porcine quality classifications and metabolic rates. Meat Sci 2005;71:522-9. https://doi.org/10.1016/j.meatsci.2005.04.034
  27. Ma L, Shao X, Wang Y, et al. Molecular cloning, characterization and expression of myoglobin in Tibetan antelope (Pantholops hodgsonii), a species with hypoxic tolerance. Gene 2014;533:532-7. https://doi.org/10.1016/j.gene.2013.09.030
  28. Karamucki T, Jakubowska M, Rybarczyk A, Gardzielewska J. The influence of myoglobin on the colour of minced pork loin. Meat Sci 2013; 94:234-8. https://doi.org/10.1016/j.meatsci.2013.01.014
  29. Sutha M, Gawdaman G, Abraham RJJ, Thirumurugan K. Influence of age on the carcass characteristics of three way synthetic pigs raised under swill feed regime. Indian J Anim Res 2015;49:114-7. https://doi.org/10.5958/0976-0555.2015.00023.0
  30. Gao XG, Xie L, Wang ZY, et al. Effect of postmortem time on the metmyoglobin reductase activity, oxygen consumption, and colour stability of different lamb muscles. Eur Food Res Technol 2013;236:579-87. https://doi.org/10.1007/s00217-012-1903-8
  31. Li G, Lee P, Mori N, et al. Long term intensive exercise training leads to a higher plasma malate/lactate dehydrogenase (M/L) ratio and increased level of lipid mobilization in horses. Vet Res Commun 2012;36:149-55. https://doi.org/10.1007/s11259-012-9515-0
  32. Rogatzki MJ, Ferguson BS, Goodwin ML, Gladden LB. Lactate is always the end product of glycolysis. Front Neurosci 2015;9:22.
  33. Galeffi F, Shetty PK, Sadgrove MP, et al. Age-related metabolic fatigue during low glucose conditions in rat hippocampus. Neurobiol Aging 2015;36:982-92. https://doi.org/10.1016/j.neurobiolaging.2014.09.016
  34. Li B, Dong C, Li P, et al. Identification of candidate genes associated with porcine meat color traits by genome-wide transcriptome analysis. Sci Rep 2016;6:35224. https://doi.org/10.1038/srep35224
  35. Kanatous SB, Mammen PPA. Regulation of myoglobin expression. J Exp Biol 2010;213:2741-7. https://doi.org/10.1242/jeb.041442
  36. Nicholson CK, Lambert, JP, Chow CW, et al. Chronic exercise downregulates myocardial myoglobin and attenuates nitrite reductase capacity during ischemia-reperfusion. J Mol Cell Cardiol 2013;64:1-10. https://doi.org/10.1016/j.yjmcc.2013.08.002
  37. Finley LWS, Lee J, Souza A, et al. Skeletal muscle transcriptional coactivator PGC-1 alpha mediates mitochondrial, but not metabolic, changes during calorie restriction. Proc Natl Acad Sci USA 2012;109:2931-6. https://doi.org/10.1073/pnas.1115813109
  38. Khan M, Couturier A, Kubens JF, et al. Niacin supplementation induces type II to type I muscle fiber transition in skeletal muscle of sheep. Acta Vet Scand 2013;55:e85. https://doi.org/10.1186/1751-0147-55-85
  39. Shen LY, Luo J, Lei HG, et al. Effects of muscle fiber type on glycolytic potential and meat quality traits in different Tibetan pig muscles and their association with glycolysis-related gene expression. Genet Mol Res 2015;14:14366-78. https://doi.org/10.4238/2015.November.13.22
  40. King DA, Shackelford SD, Wheeler TL. Relative contributions of animal and muscle effects to variation in beef lean color stability. J Anim Sci 2011;89:1434-51. https://doi.org/10.2527/jas.2010-3595
  41. Alvarez GI, Diaz AO, Longo MV, et al. Histochemical and morphometric analyses of the musculature of the forelimb of the subterranean rodent Ctenomys talarum (octodontoidea). Anat Histol Embryol 2012;41:317-25. https://doi.org/10.1111/j.1439-0264.2012.01137.x
  42. Kadim IT. Influence of feeding intake and type of muscle on quality and histochemical characteristics of dromedary camel (Camelus dromedarius) meat. J Camel Pract Res 2014;21:9-20. https://doi.org/10.5958/2277-8934.2014.00003.4

Cited by

  1. Effect of genotypes on macronutrients and antioxidant capacity of chicken breast meat vol.33, pp.11, 2020, https://doi.org/10.5713/ajas.19.0736
  2. The individual and combined effects of hypoxia and high-fat diet feeding on nutrient composition and flesh quality in Nile tilapia (Oreochromis niloticus) vol.343, pp.None, 2017, https://doi.org/10.1016/j.foodchem.2020.128479
  3. Effect of Betaine Diet on Growth Performance, Carcass Quality and Fat Deposition in Finishing Ningxiang Pigs vol.11, pp.12, 2021, https://doi.org/10.3390/ani11123408
  4. Impact of Heat Stress on Meat Quality and Antioxidant Markers in Iberian Pigs vol.10, pp.12, 2021, https://doi.org/10.3390/antiox10121911
  5. Inherent factors influence color variations in semimembranosus muscle of pigs vol.185, pp.None, 2017, https://doi.org/10.1016/j.meatsci.2021.108721