한국축산식품학회지 (Food Science of Animal Resources)

  • 제36권6호
  • /
  • Pages.819-828
  • /
  • 2016
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  • 2636-0772(pISSN)
  • /
  • 2636-0780(eISSN)
한국축산식품학회 (Korean Society for Food Science of Animal Resources)
권호 표지
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Comparison of Characteristics of Myosin Heavy Chain-based Fiber and Meat Quality among Four Bovine Skeletal Muscles

  • Kim, Gap-Don (Institute of Agriculture and Life Science, Gyeongsang National University) ;
  • Yang, Han-Sul (Institute of Agriculture and Life Science, Gyeongsang National University) ;
  • Jeong, Jin-Yeon (Institute of Agriculture and Life Science, Gyeongsang National University)
  • 투고 : 2016.09.16
  • 심사 : 2016.12.05
  • 발행 : 2016.12.31
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초록

Muscle fiber characteristics account for meat quality and muscle fibers are mainly classified into three or more types according to their contractile and metabolic properties. However, the majority of previous studies on bovine skeletal muscle are based on myosin ATPase activity. In the present study, the differences in the characteristics of muscle fibers classified by the expression of myosin heavy chain (MHC) among four bovine skeletal muscles such as longissimus thoracis (LT), psoas major (PM), semimembranosus (SM) and semi-tendinosus (ST) and their relationships to beef quality were investigated. MHCs 2x, 2a and slow were identified by LC-MS/MS and IIX, IIA and I fiber types were classified. PM, which had the smallest size and highest density of fibers regardless of type, showed the highest myoglobin content, CIE $L^*$, $a^*$, $b^*$ and sarcomere length (p<0.05), whereas ST with the highest composition of IIX, showed high shear force and low sarcomere length (p<0.05). The correlation coefficients between muscle fiber characteristics and meat quality showed that type IIX is closely related to poor beef quality and that a high density of small-sized fibers is related to redness and tenderness. Therefore, the differences in meat quality between muscles can be explained by the differences in muscle fiber characteristics, and especially, the muscles with good quality are composed of more small-sized fibers regardless of fiber type.

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참고문헌

  1. Abreu, E., Quirox-Rothe, E., Mayoral, A. I., Vivo, J. M., Robina, Á., Guillén, M. T., Agüera, E., and Rivero, J. L. (2006) Myosin heavy chain fibre types and fibre sizes in nulliparous and primiparous ovariectomized Iberian sows: Interaction with two alternative rearing systems during the fattening period. Meat Sci. 74, 359-372. https://doi.org/10.1016/j.meatsci.2006.04.002
  2. Acevedo, L. M. and Rivero, J. L. L. (2006) New insights into skeletal muscle fibre types in the dog with particular focus towards hybrid myosin phenotypes. Cell Tissue Res. 323, 283-303. https://doi.org/10.1007/s00441-005-0057-4
  3. AOAC. (2000) Official methods of analysis (17th ed.). Gaithersburg, MD: Association of Official Analytical Chemists.
  4. Arbanas, J., Klasan, G. S., Nikolic, M., Jerkovic, R., Miljanovic, I., and Malner, D. (2009) Fibre type composition of the human psoas major muscle with regard to the level of its orgin. J. Anat. 215, 636-641. https://doi.org/10.1111/j.1469-7580.2009.01155.x
  5. Bexa, T. J., Hutcheson, J. P., Miller, M. F., Brooks, J. C., Nichols, W. T., Streeter, M. N., Yates, D. A., and Johnson, B. J. (2010) Additive effects of a steroidal implant and zilpaterol hydrochloride on feedlot performance, carcass characteristics, and skeletal muscle messenger ribonucleic acid abundance in finishing steers. J. Anim. Sci. 88, 330-337. https://doi.org/10.2527/jas.2009-1797
  6. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72, 248-254. https://doi.org/10.1016/0003-2697(76)90527-3
  7. Brooke, M. H. and Kaiser, K. K. (1970) Three myosin adenosine triphosphatase system: The nature of their pH liability and sulphydryl dependence. J. Histochem. Cytochem. 18, 670-672. https://doi.org/10.1177/18.9.670
  8. Chang, K. C., Costa, N., Blackley, R., Southwood, O., Evans, G., Plastow, G., Wood, J. D., and Richardson, R. I. (2003) Relationships of myosin heavy chain fibre types to meat quality traits in traditional and modern pigs. Meat Sci. 64, 93-103. https://doi.org/10.1016/S0309-1740(02)00208-5
  9. Chikuni, K., Muroya, S., and Nakajima, I. (2004) Myosin heavy chains expressed in bovine skeletal muscles. Meat Sci. 67, 87-94. https://doi.org/10.1016/j.meatsci.2003.09.011
  10. Cross, H. R., West, R. L., and Dutson, T. R. (1981) Comparison of methods for measuring sarcomere length in beef semitendinosus muscle. Meat Sci. 5, 261-266. https://doi.org/10.1016/0309-1740(81)90016-4
  11. Folch, J., Lees, M., and Sloane-Stanley, G. H. (1957) A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226, 497-509.
  12. Gonzalez, J. M., Johnson, S. E., Thrift, T. A., Sevell, J. D., Ouellette, S. E., and Johnson, D. D. (2009) Effect of ractopamine-hydrochloride on the fiber type distribution and shelf-life of six muscles of steers. J. Anim. Sci. 87, 1764-1771. https://doi.org/10.2527/jas.2008-1469
  13. Greenwood, P. L., Tomkins, N. W., Hunter, R. A., Allingham, P. G., Harden, S., and Harper, G. S. (2009) Bovine myofiber characteristics are influenced by postweaning nutrition. J. Anim. Sci. 87, 3114-3132. https://doi.org/10.2527/jas.2009-1936
  14. Guth, L. and Samaha, F. J. (1969) Qualitative differences between actomyosin ATPase of slow and fast mammalian muscle. Exp. Neurol. 25, 138-152. https://doi.org/10.1016/0014-4886(69)90077-6
  15. Herpin, P. and Lefaucheur, L. (1992) Adaptive changes in oxidative metabolism in skeletal muscle of cold-acclimated piglets. J. Therm. Biol. 17, 277-285. https://doi.org/10.1016/0306-4565(92)90067-P
  16. Honikel, K. O. (1987) How to measure the water-holding capacity of meat? In P. V. Tarrant, G. Eikelenboom, and G. Monin (Eds.), Recommendation of standardized methods. Evaluation and control of meat quality in pigs. (pp. 129-142). Dordecht, The Netherlands: Martinus Nijhoff.
  17. Hwang, Y. H., Kim, G. D., Jeong, J. Y., Hur, S. J., and 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, 456-461. https://doi.org/10.1016/j.meatsci.2010.05.034
  18. Jurie, C., Picard, B., and Geay, Y. (1998) Influences of the method of housing bulls on their body composition and muscle fibre types. Meat Sci. 50, 457-469. https://doi.org/10.1016/S0309-1740(98)00059-X
  19. Karlsson, A., Enfalt, A. C., Essen-Gustavsson, B., Lundstrom, K., Rydhmer, L., and 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, 930-938. https://doi.org/10.2527/1993.714930x
  20. Kim, G. D. (2014) Analysis of myosin heavy chain isoforms from longissimus thoracis muscle of Hanwoo steer by electrophoresis and LC-MS/MS. Korean J. Food Sci. An. 34, 656-664. https://doi.org/10.5851/kosfa.2014.34.5.656
  21. Kim, G. D., Ryu, Y. C., Jeong, J. Y., Yang, H. S., and Joo, S. T. (2013) Relationship between pork quality and characteristics of muscle fibers classified by the distribution of myosin heavy chain isoforms. J. Anim. Sci. 91, 5525-5534. https://doi.org/10.2527/jas.2013-6614
  22. Kim, G. D., Ryu, Y. C., Jo, C. Lee, J. K., Yang, H. S., Jeong, J. Y., and Joo, S. T. (2014) The characteristics of myosin heavy chain-based fiber types in porcine longissimus dorsi muscle. Meat Sci. 96, 712-718. https://doi.org/10.1016/j.meatsci.2013.09.028
  23. Kirchofer, K. S., Calkins, C. R., and Gwartney, B. L. (2002) Fiber-type composition of muscles of the beef chuck and round. J. Anim. Sci. 80, 2872-2878. https://doi.org/10.2527/2002.80112872x
  24. Kolczak, T., Pospiech, E., Palka, K., and Lacki, J. (2003) Changes in structure of psoas major and minor and semitendinosus muscles of calves, heifers and cows during post-mortem ageing. Meat Sci. 64, 77-83. https://doi.org/10.1016/S0309-1740(02)00164-X
  25. Larzul, C., Lefaucheur, L., Ecolan, P., Gogue, J., Talmant, A., and Sellier, P. (1997) Phenotypic and genetic parameters for longissimus muscle fiber characteristics in relation to growth, carcass, and meat quality traits in large white pigs. J. Anim. Sci. 75, 3126-3137. https://doi.org/10.2527/1997.75123126x
  26. Lefaucheur, L. (2010) A second look into fibre typing - Relation to meat quality. Meat Sci. 84, 257-270. https://doi.org/10.1016/j.meatsci.2009.05.004
  27. Lefaucheur, L., Ecolan, P., Plantard, L., and Gueguen, N. (2002) New insights into muscle fiber types in the pig. J. Histochem. Cytochem. 50, 719-730. https://doi.org/10.1177/002215540205000513
  28. Levitsky, D. I. (2004). Actomyosin systems of biological motility. Biochemistry (Moscow) 69, 1177-1189. https://doi.org/10.1007/s10541-005-0063-x
  29. Maccatrozzo, L., Patruno, M., Toniolo, L., Reggiani, C., and Mascarello, F. (2004) Myosin heavy chain 2B isoform is expressed in specialized eye muscles but not in trunk and limb muscles of cattle. Eur. J. Histochem. 48, 357-366.
  30. McKenna, D. R., Mies, P. D., Baird, B. E., Pfeiffer, K. D., Ellebracht, J. W., and Savell, J. W. (2005) Biochemical and physical factors affecting discoloration characteristics of 19 bovine muscles. Meat Sci. 70, 665-682. https://doi.org/10.1016/j.meatsci.2005.02.016
  31. Ordway, G. A. and Garry, D. J. (2004) Myoglobin: An essential hemoprotein in striated muscle. J. Exp. Biol. 207, 3441-3446. https://doi.org/10.1242/jeb.01172
  32. Ozawa, S., Mitsuhashi, T., Mitsumoto, M., Matsumoto, S., Itoh, N., and Itagaki, K. (2000) The characteristics of muscle fiber types of longissimus thoracis muscle and their influences on the quantity and quality of meat from Japanese Black steers. Meat Sci. 54, 65-70. https://doi.org/10.1016/S0309-1740(99)00072-8
  33. Renand, G., Picard, B., Touraille, C., Berge, P., and Lepetit, J. (2001) Relationships between muscle characteristics and meat quality traits of young Charolais bulls. Meat Sci. 59, 49-60. https://doi.org/10.1016/S0309-1740(01)00051-1
  34. Rodriguez, J., Unruh, J., Villarreal, M., Murillo, O., Rojas, S., Camacho, J., Jaeger, J., and Reinhardt, C. (2014) Carcass and meat quality characteristics of Brahman cross bulls and steers finished on tropical pastures in Costa Rica. Meat Sci. 96, 1340-1344. https://doi.org/10.1016/j.meatsci.2013.10.024
  35. Ryu, Y. C., Choi, Y. M., Lee, S. H., Shin, H. G., Choe, J. H., and Kim, B. C. (2008) Comparing the histochemical characteristics and meat quality traits of different pig breeds. Meat Sci. 80, 363-369. https://doi.org/10.1016/j.meatsci.2007.12.020
  36. Ryu, Y. C. and Kim, B. C. (2005) The relationship between muscle fiber characteristics, postmortem metabolic rate, and meat quality of pig longissimus dorsi muscle. Meat Sci. 71, 351-357. https://doi.org/10.1016/j.meatsci.2005.04.015
  37. Solomon, M. B. and Lynch, G. P. (1988) Biochemical, histochemical and palatability characteristics of young ram lambs as affected by diet and electrical stimulation. J. Anim. Sci. 66, 1955-1962. https://doi.org/10.2527/jas1988.6681955x
  38. Talmadge, R. J. and Roy, R. R. (1993). Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms. J. Appl. Physiol. 75, 2337-2340. https://doi.org/10.1152/jappl.1993.75.5.2337

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