Browse > Article
http://dx.doi.org/10.7744/kjoas.20180012

Overview of muscle metabolism, muscle fiber characteristics, and meat quality  

Choe, Jeehwan (Department of Animal Science and Biotechnology, Chungnam National University)
Publication Information
Korean Journal of Agricultural Science / v.45, no.1, 2018 , pp. 50-57 More about this Journal
Abstract
Meat comes from the skeletal muscles of farm animals, such as pigs, chickens, and cows. Skeletal muscles are composed of many muscle fibers. Muscle fibers are categorized into three types, fiber type I, IIA, and IIB, based on their contractile speed and metabolic properties. Different muscle fiber types have different biochemical, physiological, and biophysical characteristics. Especially, the characteristics of muscle fiber type I and IIB are opposite to each other. Muscle fiber type I has a relatively strong oxidative metabolic trait and a higher content of lipids. In contrast to fiber type I, muscle fiber type IIB has a strong glycolytic metabolic trait and a relatively lower content of lipids and a higher content of glycogen. Muscle fiber type IIA has intermediate properties between fiber type I and IIB. Thus, muscles with different fiber type compositions exhibit different ante- and post-mortem muscle characteristics. In particular, the different metabolic traits of muscles due to the different compositions of the fiber types strongly affect the biochemical and physiological processes during the conversion of muscle to meat and subsequently influence the quality of the meat. Therefore, understating muscle metabolism and muscle fiber characteristics is very important when discussing the traits of meat quality. This review is an overview on basic muscle metabolism, muscle fiber characteristics, and their influence on meat quality and finally provides a comprehensive understanding about the fundamental traits of muscles and meat quality.
Keywords
meat quality; metabolites; muscle fiber; muscle metabolism;
Citations & Related Records
Times Cited By KSCI : 1  (Citation Analysis)
연도 인용수 순위
1 Morita S, Iwamoto H, Fukumitsu Y, Gotoh T, Nishimura S, Ono, Y. 2000. Heterogeneous composition of histochemical fibre types in the different parts of M. longissimus thoracis from Mishima (Japanese native) steers. Meat Science 54:59-63.   DOI
2 Offer G, Knight PK, Jeacocke R, Almond R, Cousins T, Elsey J, Parsons N, Sharp A, Starr R, Purslow P. 1989. The structural basis of the water-holding, appearance and toughness of meat and meat products. Food Microstructure 8:151-170.
3 Park SH, Kim YH, Lee HJ, Baek YC, Kim MS, Jeong JY, Oh YK, Park SK. 2017. Inhibition of mitochondrial activity induces muscle fiber type change from slow to fast in $C_{2}C_{12}$ myotubes. Korean Journal of Agricultural Science 44:586-594.
4 Peter JB, Barnard RJ, Edgerton VR, Gillespie CA, Stempel CE. 1972. Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits. Biochemistry 11:2627-2633.   DOI
5 Poso AR, Puolanne E. 2005. Carbohydrate metabolism in meat animals. Meat Science 70:423-434.   DOI
6 Rasmussen UF, Rasmussen HN, Andersen AJ, Jorgensen PF, Quistorff B. 1996. Characterization of mitochondria from pig muscle: Higher activity of exo-NADH oxidase in animals suffering from malignant hyperthermia. The Biochemical Journal 315:659-663.   DOI
7 Ryu YC, Kim BC. 2005. The relationship between muscle fiber characteristics, postmortem metabolic rate, and meat quality of pig longissimus dorsi muscle. Meat Science 71:351-357.   DOI
8 Ryu YC, Kim BC. 2006. Comparison of histochemical characteristics in various pork groups categorized by postmortem metabolic rate and pork quality. Journal of Animal Science 84:894-901.   DOI
9 Ryu YC, Lee SH, Rhee MS, Imm JY, Kim BC. 2002. Prediction of pork quality attributes using metabolic rate and muscle fiber characteristics. The 48th International Congress of Meat Science & Technology pp. 286-287, Rome, Italy.
10 Scheffler TL, Gerrard DE. 2007. Mechanisms controlling pork quality development: The biochemistry controlling postmortem energy metabolism. Meat Science 77:7-16.   DOI
11 Schiaffino S, Reggiani C. 1996. Molecular diversity of myofibrillar proteins: Gene regulation and functional significance. Physiological Reviews 76:371-423.   DOI
12 Solomon MB, Campbell RG, Steele NC. 1990. Effect of sex and exogenous porcine somatotropin on longissimus muscle fiber characteristics of growing pigs. Journal of Animal Science 68:1176-1181.   DOI
13 Staun H. 1963. Various factors affecting number and size of muscle fibers in the pig. Acta Agriculture Scandinavica 13:293-322.   DOI
14 Vann RC, Althen TG, Smith WK, Veenhuizen JJ, Smith SB. 1998. Recombinant bovine somatotropin (rbST) administration to creep-fed beef calves increases muscle mass but does not affect satellite cell number or concentration of myosin light chain-1f mRNA. Journal of Animal Science 76:1371-1379.   DOI
15 Warriss PD. 2010. Meat science-an introductory text (2nd ed.). CABI, MA, USA.
16 Honikel KO, Kim CJ. 1986. Causes of the development of PSE pork. Fleischwirtsch 66:349-353.
17 Yla-Ajos MSK. 2006. Glycogen debranching enzyme activity in the muscles of meat producing animals. Ph.D. dissertation, University of Helsinki., Helsinki, Finland.
18 Henckel P, Oksbjerg N, Erlandsen E, Barton-Gade P, Bejerholm C. 1997. Histo- and biochemical characteristics of the longissimus dorsi muscle in pigs and their relationships to performance and meat quality. Meat Science 47:311-321.   DOI
19 Highley JR, Esiri MM, McDonald B, Roberts HC, Walker MA, Crow TJ. 1999. The size and fiber composition of the anterior commissure with respect to gender and schizophrenia. Biological Psychiatry 45:1120-1127.   DOI
20 Hintz CS, Coyle EF, Kaiser KK, Chi MMY, Lowry OH. 1984. Comparison of muscle fiber typing by quantitative enzyme assays and by myosin ATPase staining. Journal of Histochemistry and Cytochemistry 32:655-660.   DOI
21 Klont RE, Brocks L, Eikelenboom B. 1998. Muscle fibre type and meat quality. Meat Science 49(S1):S219-S229.   DOI
22 Irving TC, Swatland HJ, Millman BM. 1989. X-ray diffraction measurements of myofilament lattice spacing and optical measurements of reflectance and sarcomere length in commercial pork loins. Journal of Animal Science 67:152-156.   DOI
23 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 Science 52:291-297.   DOI
24 Karlsson AH, Klont RE, Fernandez X. 1999. Skeletal muscle fibres as factors for pork quality. Livestock Production Science 60:255-269.   DOI
25 Lengerken G, Wicke M, Maak S. 1997. Stress susceptibility and meat quality-situation and prospects in animal breeding and research. Archives of Animal Breeding 40:163-171.
26 Bendall JR. 1973. Post mortem changes in muscle. In Structure and Function of Muscle (2nd) edited by Bourne GH. Academic Press, NY, USA.
27 Aberle ED, Forrest JC, Gerrard DE, Mills EW. 2001. Principles of Meat Science. Kendall/Hunt Publishing Company, Iowa, USA.
28 Allen E, Forrest JC, Chapman AB, First N, Bray RW, Briskey EJ. 1966. Phenotypic and genetic associations between porcine muscle properties. Journal of Animal Science 25:962-968.   DOI
29 Bendall JR. 1951. The shortening of rabbit muscles during rigor mortis: Its relation to the breakdown of adenosine triphosphate and creatine phosphate and to muscular contraction. Journal of Physiology 144:71-88.
30 Briskey EJ, Wismer-Pedersen J. 1961. Biochemistry of pork muscle structure. I. Rate of anaerobic glycolysis and temperature change versus the apparent structure of muscle tissue. Journal of Food Science 26:297-305.   DOI
31 Brocks L, Klont RE, Buist W, de Greef K, Tieman M, Engel B. 2000. The effects of selection of pigs on growth rate vs leanness on histochemical characteristics of different muscles. Journal of Animal Science 78:1247-1254.   DOI
32 Brook MH, Kaiser KK. 1970. Three myosin adenosine triphosphatase systems: The nature of their pH liability and sulfhydryl dependence. Journal of Histochemistry and Cytochemistry 18:670-672.   DOI
33 Candek-Potokar M, Lefaucheur L, Zlender B, Bonneau M. 1999. Effect of slaughter weight and/or age on histological characteristics of pig longissimus dorsi muscle as related to meat quality. Meat Science 52:195-203.   DOI
34 Choe JH, Kim BC. 2014. Association of blood glucose, blood lactate, serum cortisol levels, muscle metabolites, muscle fiber type composition, and pork quality traits. Meat Science 97:137-142.   DOI
35 Carpenter ZL, Kauffman RG, Bray RW, Briskey EJ, Weckel KG. 1963. Factors influencing quality in pork. A. histological observation. Journal of Food Science 28:467-471.   DOI
36 Choe JH, Choi YM, Lee SH, Nam YJ, Jung YC, Park HC, Kim YY, Kim BC. 2009. The relation of blood glucose level to muscle fiber characteristics and pork quality traits. Meat Science 83:62-67.   DOI
37 Choe JH, Choi YM, Lee SH, Shin HG, Ryu YC, Hong KC, Kim BC. 2008. The relation between glycogen, lactate content and muscle fiber type composition, and their influence on postmortem glycolytic rate and pork quality. Meat Science 80:355-362.   DOI
38 Fiedler I, Ender K, Kuchenmeister U, Wicke M, Lengerken G. 2003. Phenotypic variations of muscle fibre and intramuscular fat traits in longissimus muscle of $F_2$ population Duroc $\times$ Berlin miniature pig and relationships to meat quality. Meat Science 63:131-139.   DOI
39 Fiedler I, Ender K, Wicke M, Lengerken G. 1993. Relationships between micro-structure of muscle tissue and stress susceptibility in Landrace pigs (halothane sensitivity). Archives of Animal Breeding 36:525-538.
40 Fiedler I, Ender K, Wicke M, Maak S, Lengerken G, Meyer W. 1999. Structural and functional characteristics of muscle fibres in pigs with different malignant hyperthermia susceptibility (MHS) and different meat quality. Meat Science 53:9-15.   DOI
41 Gentry JG, McGlone JJ, Blanton Jr JR, Miller MG. 2002. Impact of spontaneous exercise on performance, meat quality, and muscle fiber characteristics of growing/finishing pigs. Journal of Animal Science 80:2833-2839.   DOI