1932

Abstract

Fresh meat quality is greatly determined through biochemical changes occurring in the muscle during its conversion to meat. These changes are key to imparting a unique set of characteristics on fresh meat, including its appearance, ability to retain moisture, and texture. Skeletal muscle is an extremely heterogeneous tissue composed of different types of fibers that have distinct contractile and metabolic properties. Fiber type composition determines the overall biochemical and functional properties of the muscle tissue and, subsequently, its quality as fresh meat. Therefore, changing muscle fiber profile in living animals through genetic selection or environmental factors has the potential to modulate fresh meat quality. We provide an overview of the biochemical processes responsible for the development of meat quality attributes and an overall understanding of the strong relationship between muscle fiber profile and meat quality in different meat species.

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2021-02-15
2024-12-04
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Literature Cited

  1. 1. 
    Ruusunen M, Puolanne E. 2004. Histochemical properties of fibre types in muscles of wild and domestic pigs and the effect of growth rate on muscle fibre properties. Meat Sci 67:533–39
    [Google Scholar]
  2. 2. 
    Lepetit J. 2007. A theoretical approach of the relationships between collagen content, collagen cross-links and meat tenderness. Meat Sci 76:147–59
    [Google Scholar]
  3. 3. 
    Kemp CM, Sensky PL, Bardsley RG, Buttery PJ, Parr T 2010. Tenderness—an enzymatic view. Meat Sci 84:248–56
    [Google Scholar]
  4. 4. 
    Luther PK. 2009. The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling. J. Muscle Res. Cell Motil. 30:171–85
    [Google Scholar]
  5. 5. 
    Koohmaraie M, Geesink GH. 2006. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Sci 74:34–43
    [Google Scholar]
  6. 6. 
    England EM, Matarneh SK, Mitacek RM, Abraham A, Ramanathan R et al. 2018. Presence of oxygen and mitochondria in skeletal muscle early postmortem. Meat Sci 139:97–106
    [Google Scholar]
  7. 7. 
    Pösö AR, Puolanne E. 2005. Carbohydrate metabolism in meat animals. Meat Sci 70:423–34
    [Google Scholar]
  8. 8. 
    England EM, Matarneh SK, Scheffler TL, Gerrard DE 2017. Perimortal muscle metabolism and its effects on meat quality. New Aspects of Meat Quality PP Purslow 63–89 Cambridge, UK: Woodhead Publ.
    [Google Scholar]
  9. 9. 
    Matarneh SK, England EM, Scheffler TL, Gerrard DE 2017. The conversion of muscle to meat. Lawrie's Meat Science F Toldrá 159–85 Cambridge, UK: Woodhead Publ.
    [Google Scholar]
  10. 10. 
    Briskey EJ, Wismer‐Pedersen J. 1961. Biochemistry of pork muscle structure. 1. Rate of anaerobic glycolysis and temperature change versus the apparent structure of muscle tissue. J. Food Sci. 26:297–305
    [Google Scholar]
  11. 11. 
    Scopes RK. 1974. Studies with a reconstituted muscle glycolytic system. The rate and extent of glycolysis in simulated post-mortem conditions. Biochem. J. 142:79–86
    [Google Scholar]
  12. 12. 
    Hamm R, Dalrymple R, Honikel K 1973. On the post-mortem breakdown of glycogen and ATP in skeletal muscle. Proceedings of the 19th European Meeting of Meat Research Workers, Paris73–86 Champaign, IL: Am. Meat Sci. Assoc.
    [Google Scholar]
  13. 13. 
    Newbold RP, Scopes RK. 1967. Post-mortem glycolysis in ox skeletal muscle. Effect of temperature on the concentrations of glycolytic intermediates and cofactors. Biochem. J. 105:127–36
    [Google Scholar]
  14. 14. 
    Bowker BC, Grant AL, Swartz DR, Gerrard DE 2004. Myosin heavy chain isoforms influence myofibrillar ATPase activity under simulated postmortem pH, calcium, and temperature conditions. Meat Sci 67:139–47
    [Google Scholar]
  15. 15. 
    Scheffler TL, Gerrard DE. 2007. Mechanisms controlling pork quality development: the biochemistry controlling postmortem energy metabolism. Meat Sci 77:7–16
    [Google Scholar]
  16. 16. 
    Cohen P. 1978. The role of cyclic-AMP-dependent protein kinase in the regulation of glycogen metabolism in mammalian skeletal muscle. Current Topics in Cellular Regulation, Vol. 14 BL Horecker, ER Stadtman 117–96 London: Academic
    [Google Scholar]
  17. 17. 
    Hughes JM, Oiseth SK, Purslow PP, Warner RD 2014. A structural approach to understanding the interactions between colour, water-holding capacity and tenderness. Meat Sci 98:520–32
    [Google Scholar]
  18. 18. 
    Honikel K, Kim C. 1986. Causes of the development of PSE pork. Fleischwirtschaft 66:349–53
    [Google Scholar]
  19. 19. 
    Fujii J, Otsu K, Zorzato F, de Leon S, Khanna VK et al. 1991. Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia. Science 253:448–51
    [Google Scholar]
  20. 20. 
    O'Brien PJ. 1986. Porcine malignant hyperthermia susceptibility: hypersensitive calcium-release mechanism of skeletal muscle sarcoplasmic reticulum. Can. J. Vet. Res. 50:318–28
    [Google Scholar]
  21. 21. 
    Andersson DC, Betzenhauser MJ, Reiken S, Umanskaya A, Shiomi T, Marks AR 2012. Stress‐induced increase in skeletal muscle force requires protein kinase A phosphorylation of the ryanodine receptor. J. Physiol. 590:6381–87
    [Google Scholar]
  22. 22. 
    Petracci M, Bianchi M, Cavani C 2009. The European perspective on pale, soft, exudative conditions in poultry. Poult. Sci. 88:1518–23
    [Google Scholar]
  23. 23. 
    Savell JW, Mueller SL, Baird BE 2005. The chilling of carcasses. Meat Sci 70:449–59
    [Google Scholar]
  24. 24. 
    van Laack RLJM, Yang J, Spencer E 2001. Determinants of ultimate pH of pork Paper presented at the 2001 IFT Annual Meeting New Orleans, LA:
    [Google Scholar]
  25. 25. 
    Henckel P, Karlsson A, Jensen MT, Oksbjerg N, Petersen JS 2002. Metabolic conditions in porcine longissimus muscle immediately pre-slaughter and its influence on peri- and post mortem energy metabolism. Meat Sci 62:145–55
    [Google Scholar]
  26. 26. 
    England EM, Matarneh SK, Oliver EM, Apaoblaza A, Scheffler TL et al. 2016. Excess glycogen does not resolve high ultimate pH of oxidative muscle. Meat Sci 114:95–102
    [Google Scholar]
  27. 27. 
    England EM, Matarneh SK, Scheffler TL, Wachet C, Gerrard DE 2014. pH inactivation of phosphofructokinase arrests postmortem glycolysis. Meat Sci 98:850–57
    [Google Scholar]
  28. 28. 
    England EM, Matarneh SK, Scheffler TL, Wachet C, Gerrard DE 2015. Altered AMP deaminase activity may extend postmortem glycolysis. Meat Sci 102:8–14
    [Google Scholar]
  29. 29. 
    Matarneh SK, Beline M, de Luz e Silva S, Shi H, Gerrard DE 2018. Mitochondrial F1-ATPase extends glycolysis and pH decline in an in vitro model. Meat Sci 137:85–91
    [Google Scholar]
  30. 30. 
    Milan D, Jeon JT, Looft C, Amarger V, Robic A et al. 2000. A mutation in PRKAG3 associated with excess glycogen content in pig skeletal muscle. Science 288:1248–51
    [Google Scholar]
  31. 31. 
    Scheffler TL, Scheffler JM, Park S, Kasten SC, Wu Y et al. 2014. Fiber hypertrophy and increased oxidative capacity can occur simultaneously in pig glycolytic skeletal muscle. Am. J. Physiol. Cell Physiol. 306:C354–63
    [Google Scholar]
  32. 32. 
    Matarneh SK, England EM, Scheffler TL, Oliver EM, Gerrard DE 2015. Net lactate accumulation and low buffering capacity explain low ultimate pH in the longissimus lumborum of AMPKγ3R200Q mutant pigs. Meat Sci 110:189–95
    [Google Scholar]
  33. 33. 
    Copenhafer TL, Richert BT, Schinckel AP, Grant AL, Gerrard DE 2006. Augmented postmortem glycolysis does not occur early postmortem in AMPKγ3-mutated porcine muscle of halothane positive pigs. Meat Sci 73:590–99
    [Google Scholar]
  34. 34. 
    Monin G, Sellier P. 1985. Pork of low technological quality with a normal rate of muscle pH fall in the immediate post-mortem period: the case of the Hampshire breed. Meat Sci 13:49–63
    [Google Scholar]
  35. 35. 
    Joo ST, Kauffman RG, Kim BC, Park GB 1999. The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle. Meat Sci 52:291–97
    [Google Scholar]
  36. 36. 
    Apaoblaza A, Gerrard SD, Matarneh SK, Wicks JC, Kirkpatrick L et al. 2020. Muscle from grass- and grain-fed cattle differs energetically. Meat Sci 161:107996
    [Google Scholar]
  37. 37. 
    Huff-Lonergan E, Lonergan SM. 2005. Mechanisms of water-holding capacity of meat: the role of postmortem biochemical and structural changes. Meat Sci 71:194–204
    [Google Scholar]
  38. 38. 
    Qiao M, Fletcher DL, Smith DP, Northcutt JK 2001. The effect of broiler breast meat color on pH, moisture, water-holding capacity, and emulsification capacity. Poult. Sci. 80:676–80
    [Google Scholar]
  39. 39. 
    Pearce KL, Rosenvold K, Andersen HJ, Hopkins DL 2011. Water distribution and mobility in meat during the conversion of muscle to meat and ageing and the impacts on fresh meat quality attributes—a review. Meat Sci 89:111–24
    [Google Scholar]
  40. 40. 
    Honikel KO, Kim CJ, Hamm R, Roncales P 1986. Sarcomere shortening of prerigor muscles and its influence on drip loss. Meat Sci 16:267–82
    [Google Scholar]
  41. 41. 
    Guignot F, Vignon X, Monin G 1993. Post mortem evolution of myofilament spacing and extracellular space in veal muscle. Meat Sci 33:333–47
    [Google Scholar]
  42. 42. 
    Offer G, Knight P, Jeacocke R, Almond R, Cousins T et al. 1989. The structural basis of the water-holding, appearance and toughness of meat and meat products. Food Microstruct 8:151–70
    [Google Scholar]
  43. 43. 
    Kristensen L, Purslow PP. 2001. The effect of ageing on the water-holding capacity of pork: role of cytoskeletal proteins. Meat Sci 58:17–23
    [Google Scholar]
  44. 44. 
    Mancini RA, Hunt MC. 2005. Current research in meat color. Meat Sci 71:100–21
    [Google Scholar]
  45. 45. 
    Franco D, Rodríguez E, Purriños L, Crecente S, Bermúdez R, Lorenzo JM 2011. Meat quality of “Galician Mountain” foals breed. Effect of sex, slaughter age and livestock production system. Meat Sci 88:292–98
    [Google Scholar]
  46. 46. 
    Węglarz A. 2010. Meat quality defined based on pH and colour depending on cattle category and slaughter season. Czech J. Anim. Sci. 55:548–56
    [Google Scholar]
  47. 47. 
    Cho S, Kang G, Seong P-N, Park B, Kang SM 2015. Effect of slaughter age on the antioxidant enzyme activity, color, and oxidative stability of Korean Hanwoo (Bos taurus coreanae) cow beef. Meat Sci 108:44–49
    [Google Scholar]
  48. 48. 
    Kim YHB, Stuart A, Black C, Rosenvold K 2012. Effect of lamb age and retail packaging types on the quality of long-term chilled lamb loins. Meat Sci 90:962–66
    [Google Scholar]
  49. 49. 
    Seideman SC, Cross HR, Smith GC, Durland PR 1984. Factors associated with fresh meat color: a review. J. Food Qual. 6:211–37
    [Google Scholar]
  50. 50. 
    Kranen RW, van Kuppevelt TH, Goedhart HA, Veerkamp CH, Lambooy E, Veerkamp JH 1999. Hemoglobin and myoglobin content in muscles of broiler chickens. Poult. Sci. 78:467–76
    [Google Scholar]
  51. 51. 
    Nishida J, Nishida T. 1985. Relationship between the concentration of myoglobin and parvalbumin in various types of muscle tissues from chickens. Br. Poult. Sci. 26:105–15
    [Google Scholar]
  52. 52. 
    van Laack RLJM, Kauffman RG 1999. Glycolytic potential of red, soft, exudative pork longissimus muscle. J. Anim. Sci. 77:2971–73
    [Google Scholar]
  53. 53. 
    Warner RD, Kauffman RG, Greaser ML 1997. Muscle protein changes post mortem in relation to pork quality traits. Meat Sci 45:339–52
    [Google Scholar]
  54. 54. 
    Bekhit AED, Faustman C. 2005. Metmyoglobin reducing activity. Meat Sci 71:407–39
    [Google Scholar]
  55. 55. 
    Bourne M. 2002. Food texture and viscosity: concept and measurement. Principles of Objective Texture Measurement M Bourne 107–88 London: Academic
    [Google Scholar]
  56. 56. 
    Wheeler TL, Shackelford SD, Koohmaraie M 2000. Variation in proteolysis, sarcomere length, collagen content, and tenderness among major pork muscles. J. Anim. Sci. 78:958–65
    [Google Scholar]
  57. 57. 
    Hopkins DL, Geesink GH. 2009. Protein degradation postmortem and tenderisation. Applied Muscle Biology and Meat Science M Du, RJ McCormick 149–73 Boca Raton, FL: CRC Press
    [Google Scholar]
  58. 58. 
    Bekhit AED, Carne A, Ha M, Franks P 2014. Physical interventions to manipulate texture and tenderness of fresh meat: a review. Int. J. Food Prop. 17:433–53
    [Google Scholar]
  59. 59. 
    Shorthose WR, Harris PV. 1990. Effect of animal age on the tenderness of selected beef muscles. J. Food Sci. 55:1–8
    [Google Scholar]
  60. 60. 
    Hopkins DL. 2017. The eating quality of meat: II—tenderness. Lawrie's Meat Science F Toldrá 357–81 Cambridge, UK: Woodhead Publ.
    [Google Scholar]
  61. 61. 
    Young OA, Hogg BW, Mortimer BJ, Waller JE 1993. Collagen in two muscles of sheep selected for weight as yearlings. N.Z. J. Agric. Res. 36:143–50
    [Google Scholar]
  62. 62. 
    Nishimura T, Hattori A, Takahashi K 1995. Structural weakening of intramuscular connective tissue during conditioning of beef. Meat Sci 39:127–33
    [Google Scholar]
  63. 63. 
    Wheeler TL, Koohmaraie M. 1994. Prerigor and postrigor changes in tenderness of ovine longissimus muscle. J. Anim. Sci. 72:1232–38
    [Google Scholar]
  64. 64. 
    Biffin TE, Smith MA, Bush RD, Collins D, Hopkins DL 2018. The effect of combining tenderstretching and electrical stimulation on alpaca (Vicugna pacos) meat tenderness and eating quality. Meat Sci 145:127–36
    [Google Scholar]
  65. 65. 
    Pomponio L, Lametsch R, Karlsson AH, Costa LN, Grossi A, Ertbjerg P 2008. Evidence for post-mortem m-calpain autolysis in porcine muscle. Meat Sci 80:761–64
    [Google Scholar]
  66. 66. 
    Huff-Lonergan E, Mitsuhashi T, Beekman DD, Parrish FC, Olson DG, Robson RM 1996. Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. J. Anim. Sci. 74:993–1008
    [Google Scholar]
  67. 67. 
    Weaver AD, Bowker BC, Gerrard DE 2009. Sarcomere length influences μ-calpain-mediated proteolysis of bovine myofibrils. J. Anim. Sci. 87:2096–103
    [Google Scholar]
  68. 68. 
    England EM, Fisher KD, Wells SJ, Mohrhauser DA, Gerrard DE, Weaver AD 2012. Postmortem titin proteolysis is influenced by sarcomere length in bovine muscle. J. Anim. Sci. 90:989–95
    [Google Scholar]
  69. 69. 
    Wheeler TL, Koohmaraie M. 1999. The extent of proteolysis is independent of sarcomere length in lamb longissimus and psoas major. J. Anim. Sci. 77:2444–51
    [Google Scholar]
  70. 70. 
    Lomiwes D, Farouk MM, Wu G, Young OA 2014. The development of meat tenderness is likely to be compartmentalised by ultimate pH. Meat Sci 96:646–51
    [Google Scholar]
  71. 71. 
    Brooke MH, Kaiser KK. 1970. Muscle fiber types: How many and what kind. Arch. Neurol. 23:369–79
    [Google Scholar]
  72. 72. 
    Schiaffino S, Gorza L, Sartore S, Saggin L, Ausoni S et al. 1989. Three myosin heavy chain isoforms in type 2 skeletal muscle fibres. J. Muscle Res. Cell Motil. 10:197–205
    [Google Scholar]
  73. 73. 
    Bárány M. 1967. ATPase activity of myosin correlated with speed of muscle shortening. J. Gen. Physiol. 50:197–218
    [Google Scholar]
  74. 74. 
    Stienen GJM, Kiers JL, Bottinelli R, Reggiani C 1996. Myofibrillar ATPase activity in skinned human skeletal muscle fibres: fibre type and temperature dependence. J. Physiol. 493:299–307
    [Google Scholar]
  75. 75. 
    Peter JB, Barnard RJ, Edgerton VR, Gillespie CA, Stempel KE 1972. Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits. Biochemistry 11:2627–33
    [Google Scholar]
  76. 76. 
    Gauthier GF. 1969. On the relationship of ultrastructural and cytochemical features to color in mammalian skeletal muscle. Z. Zellforsch. Mikrosk. Anat. 95:462–82
    [Google Scholar]
  77. 77. 
    Schiaffino S, Reggiani C. 1996. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol. Rev. 76:371–423
    [Google Scholar]
  78. 78. 
    Pette D, Staron RS. 2001. Transitions of muscle fiber phenotypic profiles. Histochem. Cell Biol. 115:359–72
    [Google Scholar]
  79. 79. 
    Lee SH, Joo ST, Ryu YC 2010. Skeletal muscle fiber type and myofibrillar proteins in relation to meat quality. Meat Sci 86:166–70
    [Google Scholar]
  80. 80. 
    Ryu YC, Choi YM, Lee SH, Shin HG, Choe JH et al. 2008. Comparing the histochemical characteristics and meat quality traits of different pig breeds. Meat Sci 80:363–69
    [Google Scholar]
  81. 81. 
    Wright SA, Ramos P, Johnson DD, Scheffler JM, Elzo MA et al. 2018. Brahman genetics influence muscle fiber properties, protein degradation, and tenderness in an Angus-Brahman multibreed herd. Meat Sci 135:84–93
    [Google Scholar]
  82. 82. 
    Jurie C, Picard B, Geay Y 1999. Changes in the metabolic and contractile characteristics of muscle in male cattle between 10 and 16 months of age. Histochem. J. 31:117–22
    [Google Scholar]
  83. 83. 
    Hawkins RR, Moody WG, Kemp JD 1985. Influence of genetic type, slaughter weight and sex on ovine muscle fiber and fat-cell development. J. Anim. Sci. 61:1154–63
    [Google Scholar]
  84. 84. 
    Jeong J-Y, Kim G-D, Ha DM, Park MJ, Park BC et al. 2012. Relationships of muscle fiber characteristics to dietary energy density, slaughter weight, and muscle quality traits in finishing pigs. J. Anim. Sci. Technol. 54:175–83
    [Google Scholar]
  85. 85. 
    Petersen JS, Henckel P, Oksbjerg N, Sørensen MT 1998. Adaptations in muscle fibre characteristics induced by physical activity in pigs. Anim. Sci. 66:733–40
    [Google Scholar]
  86. 86. 
    Kim G-D, Kim B-W, Jeong J-Y, Hur S-J, Cho I-C et al. 2013. Relationship of carcass weight to muscle fiber characteristics and pork quality of crossbred (Korean native black pig × Landrace) F2 pigs. Food Bioprocess Technol 6:522–29
    [Google Scholar]
  87. 87. 
    Kirchofer KS, Calkins CR, Gwartney BL 2002. Fiber-type composition of muscles of the beef chuck and round. J. Anim. Sci. 80:2872–78
    [Google Scholar]
  88. 88. 
    Stufft K, Elgin J, Patterson B, Matarneh SK, Preisser R et al. 2017. Muscle characteristics only partially explain color variations in fresh hams. Meat Sci 128:88–96
    [Google Scholar]
  89. 89. 
    Rahelic S, Puac S. 1981. Fibre types in Longissimus dorsi from wild and highly selected pig breeds. Meat Sci 5:439–50
    [Google Scholar]
  90. 90. 
    Karlsson A, Enfäl A-C, Essén-Gustavsson B, Lundström K, Rydhmer L, Stern S 1993. Muscle histochemical and biochemical properties in relation to meat quality during selection for increased lean tissue growth rate in pigs. J. Anim. Sci. 71:930–38
    [Google Scholar]
  91. 91. 
    Depreux FFS, Okamura CS, Swart DR, Grant AL, Brandstetter AM, Gerrard DE 2000. Quantification of myosin heavy chain isoform in porcine muscle using an enzyme-linked immunosorbent assay. Meat Sci 56:261–69
    [Google Scholar]
  92. 92. 
    Lefaucheur L, Gerrard D. 2000. Muscle fiber plasticity in farm mammals. J. Anim. Sci. 77:1–19
    [Google Scholar]
  93. 93. 
    Carr SN, Hamilton DN, Miller KD, Schroeder AL, Fernández-Dueñas D et al. 2009. The effect of ractopamine hydrochloride (Paylean®) on lean carcass yields and pork quality characteristics of heavy pigs fed normal and amino acid fortified diets. Meat Sci 81:533–39
    [Google Scholar]
  94. 94. 
    Grant AL, Skjaerlund DM, Helferich WG, Bergen WG, Merkel RA 1993. Skeletal muscle growth and expression of skeletal muscle αs-actin mRNA and insulin-like growth factor I mRNA in pigs during feeding and withdrawal of ractopamine. J. Anim. Sci. 71:3319–26
    [Google Scholar]
  95. 95. 
    Helferich WG, Jump DB, Anderson DB, Skjaerlund DM, Merkel RA, Bergen WG 1990. Skeletal muscle α-actin synthesis is increased pretranslationally in pigs fed the phenethanolamine ractopamine. Endocrinology 126:3096–100
    [Google Scholar]
  96. 96. 
    Kim YS, Lee YB, Dalrymple RH 1987. Effect of the repartitioning agent cimaterol on growth, carcass and skeletal muscle characteristics in lambs. J. Anim. Sci. 65:1392–99
    [Google Scholar]
  97. 97. 
    Wheeler TL, Koohmaraie M. 1992. Effects of the β-adrenergic agonist L644,969 on muscle protein turnover, endogenous proteinase activities, and meat tenderness in steers. J. Anim. Sci. 70:3035–43
    [Google Scholar]
  98. 98. 
    Polla B, Cappelli V, Morello F, Pellegrino MA, Boschi F et al. 2001. Effects of the β2-agonist clenbuterol on respiratory and limb muscles of weaning rats. Am. J. Physiol. Integr. Comp. Physiol. 280:R862–69
    [Google Scholar]
  99. 99. 
    Eggert JM, Depreux FFS, Schinckel AP, Grant AL, Gerrard DE 2002. Myosin heavy chain isoforms account for variation in pork quality. Meat Sci 61:117–26
    [Google Scholar]
  100. 100. 
    Gunawan AM, Richert BT, Schinckel AP, Grant AL, Gerrard DE 2007. Ractopamine induces differential gene expression in porcine skeletal muscles. J. Anim. Sci. 85:2115–24
    [Google Scholar]
  101. 101. 
    Dadoune JP, Terquem A, Alfonsi MF 1978. High resolution radioautographic study of newly formed protein in striated muscle with emphasis on red and white fibres. Cell Tissue Res 193:269–82
    [Google Scholar]
  102. 102. 
    Lefaucheur L. 2010. A second look into fibre typing—relation to meat quality. Meat Sci 84:257–70
    [Google Scholar]
  103. 103. 
    Lefaucheur L, Hoffman RK, Gerrard DE, Okamura CS, Rubinstein N, Kelly A 1998. Evidence for three adult fast myosin heavy chain isoforms in type II skeletal muscle fibers in pigs. J. Anim. Sci. 76:1584–93
    [Google Scholar]
  104. 104. 
    Listrat A, Lebret B, Louveau I, Astruc T, Bonnet M et al. 2016. How muscle structure and composition influence meat and flesh quality. Sci. World J. 2016:3182746
    [Google Scholar]
  105. 105. 
    Ryu YC, Kim BC. 2005. The relationship between muscle fiber characteristics, postmortem metabolic rate, and meat quality of pig longissimus dorsi muscle. Meat Sci 71:351–57
    [Google Scholar]
  106. 106. 
    Kim GD, Jeong JY, Moon SH, Hwang YH, Park GB, Joo ST 2008. Effects of muscle fibre type on meat characteristics of chicken and duck breast muscle Paper presented at the 54th International Congress of Meat Science and Technology, Cape Town, S. Afr .
    [Google Scholar]
  107. 107. 
    Kim G-D, Jeong T-C, Cho KM, Jeong J-Y 2017. Identification and quantification of myosin heavy chain isoforms in bovine and porcine longissimus muscles by LC-MS/MS analysis. Meat Sci 125:143–51
    [Google Scholar]
  108. 108. 
    Hochachka PW, Emmett B, Suarez RK 1988. Limits and constraints in the scaling of oxidative and glycolytic enzymes in homeotherms. Can. J. Zool. 66:1128–38
    [Google Scholar]
  109. 109. 
    Baylor SM, Hollingworth S. 2012. Intracellular calcium movements during excitation-contraction coupling in mammalian slow-twitch and fast-twitch muscle fibers. J. Gen. Physiol. 139:261–72
    [Google Scholar]
  110. 110. 
    Baughman JM, Perocchi F, Girgis HS, Plovanich M, Belcher-Timme CA et al. 2011. Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter. Nature 476:341–45
    [Google Scholar]
  111. 111. 
    Dang DS, Buhler JF, Davis HT, Thornton KJ, Scheffler TL, Matarneh SK 2020. Inhibition of mitochondrial calcium uniporter enhances postmortem proteolysis and tenderness in beef cattle. Meat Sci 162:108039
    [Google Scholar]
  112. 112. 
    Tang J, Faustman C, Hoagland TA, Mancini RA, Seyfert M, Hunt MC 2005. Postmortem oxygen consumption by mitochondria and its effects on myoglobin form and stability. J. Agric. Food Chem. 53:1223–30
    [Google Scholar]
  113. 113. 
    Matarneh SK, England EM, Scheffler TL, Yen C-N, Wicks JC et al. 2017. A mitochondrial protein increases glycolytic flux. Meat Sci 133:119–25
    [Google Scholar]
  114. 114. 
    Matarneh SK, Yen C-N, Elgin JM, Beline M, da Luz e Silva S et al. 2018. Phosphofructokinase and mitochondria partially explain the high ultimate pH of broiler pectoralis major muscle. Poult. Sci. 97:1808–17
    [Google Scholar]
  115. 115. 
    Bloemink MJ, Adamek N, Reggiani C, Geeves MA 2007. Kinetic analysis of the slow skeletal myosin MHC-1 isoform from bovine masseter muscle. J. Mol. Biol. 373:1184–97
    [Google Scholar]
  116. 116. 
    Scheffler TL, Matarneh SK, England EM, Gerrard DE 2015. Mitochondria influence postmortem metabolism and pH in an in vitro model. Meat Sci 110:118–25
    [Google Scholar]
  117. 117. 
    Puolanne E, Kivikari R. 2000. Determination of the buffering capacity of postrigor meat. Meat Sci 56:7–13
    [Google Scholar]
  118. 118. 
    Zheng A, Rahkila P, Vuori J, Rasi S, Takala T, Väänänen HK 1992. Quantification of carbonic anhydrase III and myoglobin in different fiber types of human psoas muscle. Histochemistry 97:77–81
    [Google Scholar]
  119. 119. 
    Ramanathan R, Suman SP, Faustman C 2020. Biomolecular interactions governing fresh meat color in post-mortem skeletal muscle: a review. J. Agric. Food Chem. 68:12779–87
    [Google Scholar]
  120. 120. 
    Tichivangana JZ, Morrissey PA. 1985. Metmyoglobin and inorganic metals as pro-oxidants in raw and cooked muscle systems. Meat Sci 15:107–16
    [Google Scholar]
  121. 121. 
    Suman SP, Faustman C, Stamer SL, Liebler DC 2007. Proteomics of lipid oxidation‐induced oxidation of porcine and bovine oxymyoglobins. Proteomics 7:628–40
    [Google Scholar]
  122. 122. 
    Schaefer DM, Liu Q, Faustman C, Yin M-C 1995. Supranutritional administration of vitamins E and C improves oxidative stability of beef. J. Nutr. 125:1792S–98S
    [Google Scholar]
  123. 123. 
    Suman SP, Joseph P. 2013. Myoglobin chemistry and meat color. Annu. Rev. Food Sci. Technol. 4:79–99
    [Google Scholar]
  124. 124. 
    Belskie KM, Ramanathan R, Suman SP, Mancini RA 2015. Effects of muscle type and display time on beef mitochondria. Meat Sci 101:157–58
    [Google Scholar]
  125. 125. 
    McKenna DR, Mies PD, Baird BE, Pfeiffer KD, Ellebracht JW, Savell JW 2005. Biochemical and physical factors affecting discoloration characteristics of 19 bovine muscles. Meat Sci 70:665–82
    [Google Scholar]
  126. 126. 
    Seyfert M, Mancini RA, Hunt MC, Tang J, Faustman C 2007. Influence of carbon monoxide in package atmospheres containing oxygen on colour, reducing activity, and oxygen consumption of five bovine muscles. Meat Sci 75:432–42
    [Google Scholar]
  127. 127. 
    Joseph P, Suman SP, Rentfrow G, Li S, Beach CM 2012. Proteomics of muscle-specific beef color stability. J. Agric. Food Chem. 60:3196–203
    [Google Scholar]
  128. 128. 
    Ramanathan R, Nair MN, Hunt MC, Suman SP 2019. Mitochondrial functionality and beef colour: a review of recent research. S. Afr. J. Anim. Sci. 49:9–19
    [Google Scholar]
  129. 129. 
    Ramanathan R, Mancini RA, Konda MR 2009. Effects of lactate on beef heart mitochondrial oxygen consumption and muscle darkening. J. Agric. Food Chem. 57:1550–55
    [Google Scholar]
  130. 130. 
    Kim YH, Hunt MC, Mancini RA, Seyfert M, Loughin TM et al. 2006. Mechanism for lactate-color stabilization in injection-enhanced beef. J. Agric. Food Chem. 54:7856–62
    [Google Scholar]
  131. 131. 
    Ramanathan R, Mancini RA, Dady GA 2011. Effects of pyruvate, succinate, and lactate enhancement on beef longissimus raw color. Meat Sci 88:424–28
    [Google Scholar]
  132. 132. 
    Mohan A, Hunt MC, Barstow TJ, Houser TA, Muthukrishnan S 2010. Effects of malate, lactate, and pyruvate on myoglobin redox stability in homogenates of three bovine muscles. Meat Sci 86:304–10
    [Google Scholar]
  133. 133. 
    Faustman C, Liebler DC, McClure TD, Sun Q 1999. α,β-Unsaturated aldehydes accelerate oxymyoglobin oxidation. J. Agric. Food Chem. 47:3140–44
    [Google Scholar]
  134. 134. 
    Reuter BJ, Wulf DM, Maddock RJ 2002. Mapping intramuscular tenderness variation in four major muscles of the beef round. J. Anim. Sci. 80:2594–99
    [Google Scholar]
  135. 135. 
    Hwang Y-H, Kim G-D, Jeong J-Y, Hur S-J, Joo S-T 2010. The relationship between muscle fiber characteristics and meat quality traits of highly marbled Hanwoo (Korean native cattle) steers. Meat Sci 86:456–61
    [Google Scholar]
  136. 136. 
    Calkins CR, Dutson TR, Smith GC, Carpenter ZL, Davis GW 1981. Relationship of fiber type composition to marbling and tenderness of bovine muscle. J. Food Sci. 46:708–10
    [Google Scholar]
  137. 137. 
    Picard B, Gagaoua M, Micol D, Cassar-Malek I, Hocquette J-F, Terlouw CEM 2014. Inverse relationships between biomarkers and beef tenderness according to contractile and metabolic properties of the muscle. J. Agric. Food Chem. 62:9808–18
    [Google Scholar]
  138. 138. 
    Totland GK, Kryvi H, Slinde E 1988. Composition of muscle fibre types and connective tissue in bovine M. semitendinosus and its relation to tenderness. Meat Sci 23:303–15
    [Google Scholar]
  139. 139. 
    Seideman SC, Crouse JD, Cross HR 1986. The effect of sex condition and growth implants on bovine muscle fiber characteristics. Meat Sci 17:79–95
    [Google Scholar]
  140. 140. 
    Karlsson AH, Klont RE, Fernandez X 1999. Skeletal muscle fibres as factors for pork quality. Livest. Prod. Sci. 60:255–69
    [Google Scholar]
  141. 141. 
    Jeong DW, Choi YM, Lee SH, Choe JH, Hong KC et al. 2010. Correlations of trained panel sensory values of cooked pork with fatty acid composition, muscle fiber type, and pork quality characteristics in Berkshire pigs. Meat Sci 86:607–15
    [Google Scholar]
  142. 142. 
    Renand G, Picard B, Touraille C, Berge P, Lepetit J 2001. Relationships between muscle characteristics and meat quality traits of young Charolais bulls. Meat Sci 59:49–60
    [Google Scholar]
  143. 143. 
    Muroya S, Ertbjerg P, Pomponio L, Christensen M 2010. Desmin and troponin T are degraded faster in type IIb muscle fibers than in type I fibers during postmortem aging of porcine muscle. Meat Sci 86:764–69
    [Google Scholar]
  144. 144. 
    Ouali A, Talmant A. 1990. Calpains and calpastatin distribution in bovine, porcine and ovine skeletal muscles. Meat Sci 28:331–48
    [Google Scholar]
  145. 145. 
    Kumamoto T, Kleese WC, Cong J, Goll DE, Pierce PR, Allen RE 1992. Localization of the Ca2+-dependent proteinases and their inhibitor in normal, fasted, and denervated rat skeletal muscle. Anat. Rec. 232:60–77
    [Google Scholar]
  146. 146. 
    Koohmaraie M. 1996. Biochemical factors regulating the toughening and tenderization processes of meat. Meat Sci 43:193–201
    [Google Scholar]
  147. 147. 
    Huang F, Huang M, Zhang H, Zhang C, Zhang D, Zhou G 2016. Changes in apoptotic factors and caspase activation pathways during the postmortem aging of beef muscle. Food Chem 190:110–14
    [Google Scholar]
  148. 148. 
    Tsujimoto Y, Shimizu S. 2007. Role of the mitochondrial membrane permeability transition in cell death. Apoptosis 12:835–40
    [Google Scholar]
  149. 149. 
    Kemp CM, Parr T. 2008. The effect of recombinant caspase 3 on myofibrillar proteins in porcine skeletal muscle. Animal 2:1254–64
    [Google Scholar]
  150. 150. 
    Huang M, Huang F, Xu X, Zhou G 2009. Influence of caspase3 selective inhibitor on proteolysis of chicken skeletal muscle proteins during post mortem aging. Food Chem 115:181–86
    [Google Scholar]
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