Animal Bioscience

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

DOI QR Code

The relationship between myofiber characteristics and meat quality of Chinese Qinchuan and Luxi cattle

  • Lu, Xiao (College of Food Science and Engineering, Shandong Agricultural University) ;
  • Yang, Yuying (College of Food Science and Engineering, Shandong Agricultural University) ;
  • Zhang, Yimin (College of Food Science and Engineering, Shandong Agricultural University) ;
  • Mao, Yanwei (College of Food Science and Engineering, Shandong Agricultural University) ;
  • Liang, Rongrong (College of Food Science and Engineering, Shandong Agricultural University) ;
  • Zhu, Lixian (College of Food Science and Engineering, Shandong Agricultural University) ;
  • Luo, Xin (College of Food Science and Engineering, Shandong Agricultural University)
  • Received : 2020.02.06
  • Accepted : 2020.06.20
  • Published : 2021.04.01
Download PDF
⟨ Previous Next ⟩

Abstract

Objective: The objectives of this study were to explore the expression patterns of myosin heavy chain (MyHC) genes of different skeletal muscles from Chinese cattle, and to investigate the relationship between myofiber characteristics and meat quality of M. longissimus lumborum (LL), M. psoas major (PM), and M. semimembranosus (SM) from Chinese Luxi and Qinchuan cattle. Methods: Three major muscles including LL, PM, and SM from Chinese Luxi cattle and Chinese Qinchuan cattle were used in this study. The myofiber characteristics were measured by histochemical analysis. The MyHC isoforms expression was evaluated by real-time quantitative polymerase chain reaction. Quality traits including pH value, meat color, cooking loss, Warner-Bratzler shear force (WBSF) and sarcomere length were determined at day 5 postmortem. Results: PM muscle had higher pH value, a* value, sarcomere length and lower WBSF value compared to LL and SM muscles (p<0.05). Numbers of type I myofiber and the relative expression of MyHC I mRNA in PM muscle were higher than those of LL and SM muscles (p<0.05). Myofiber diameter of PM muscle was lower than that of LL and SM muscles, regardless of myofiber types (p<0.05). Conclusion: According to the stepwise linear regression analyses, tenderness was influenced by myofiber characteristics in all three examined muscles. Tenderness of beef muscles from Qinchuan and Luxi cattle could be improved by increasing numbers of type I myofiber.

Keywords

References

  1. Joo ST, Kim GD, Hwang YH, Ryu YC. Control of fresh meat quality through manipulation of muscle fiber characteristics. Meat Sci 2013;95:828-36. https://doi.org/10.1016/j.meatsci.2013.04.044
  2. McKenna DR, Mies PD, Baird BE, Pfeiffer KD, Ellebracht JW, Savell JW. Biochemical and physical factors affecting discoloration characteristics of 19 bovine muscles. Meat Sci 2005;70:665-82. https://doi.org/10.1016/j.meatsci.2005.02.016
  3. Stolowski GD, Baird BE, Miller RK, et al. Factors influencing the variation in tenderness of seven major beef muscles from three Angus and Brahman breed crosses. Meat Sci 2006;73:475-83. https://doi.org/10.1016/j.meatsci.2006.01.006
  4. Joo SH, Lee KW, Hwang YH, Joo ST. Histochemical characteristics in relation to meat quality traits of eight major muscles from Hanwoo steers. Korean J Food Sci Anim Resour 2017;37:716-25. https://doi.org/10.5851/kosfa.2017.37.5.716
  5. Nair MN, Canto AC, Rentfrow G, Suman SP. Muscle-specific effect of aging on beef tenderness. LWT 2019;100:250-2. https://doi.org/10.1016/j.lwt.2018.10.038
  6. Lee SH, Joo ST, Ryu YC. Skeletal muscle fiber type and myofibrillar proteins in relation to meat quality. Meat Sci 2010;86:166-70. https://doi.org/10.1016/j.meatsci.2010.04.040
  7. Choi YM, Kim BC. Muscle fiber characteristics, myofibrillar protein isoforms, and meat quality. Livest Sci 2009;122:10518. https://doi.org/10.1016/j.livsci.2008.08.015
  8. Kim GD, Yang HS, Jeong JY. Comparison of characteristics of myosin heavy chain-based fiber and meat quality among four bovine skeletal muscles. Korean J Food Sci Anim Resour 2016;36:819-28. https://doi.org/10.5851/kosfa.2016.36.6.819
  9. Zhang M, Liu Y, Fu C, et al. Expression of MyHC genes, composition of muscle fiber type and their association with intramuscular fat, tenderness in skeletal muscle of Simmental hybrids. Mol Biol Rep 2014;41:833-40. https://doi.org/10.1007/s11033-013-2923-6
  10. Chikuni K, Muroya S, Nakajima I. Myosin heavy chain isoforms expressed in bovine skeletal muscles. Meat Sci 2004; 67:87-94. https://doi.org/10.1016/j.meatsci.2003.09.011
  11. Picard B, Cassar-Malek I. Evidence for expression of IIb myosin heavy chain isoform in some skeletal muscles of Blonde d'Aquitaine bulls. Meat Sci 2009;82:30-6. https://doi.org/10.1016/j.meatsci.2008.11.022
  12. Tanabe R, Muroya S, Chikuni K. Sequencing of the 2a, 2x, and slow isoforms of the bovine myosin heavy chain and the different expression among muscles. Mamm Genom 1998;9:1056-8. https://doi.org/10.1007/s003359900924
  13. Hwang YH, Kim GD, Jeong JY, Hur SJ, Joo ST. The relationship between muscle fiber characteristics and meat quality traits of highly marbled Hanwoo (Korean native cattle) steers. Meat Sci 2010;86:456-61. https://doi.org/10.1016/j.meatsci.2010.05.034
  14. Lang YM, Wang YF, Sun BZ, et al. Myofiber characteristics and eating quality of three major muscles from Chinese Simmental cattle. Can J Anim Sci 2017;97:101-8. https://doi.org/10.1139/cjas-2015-0182
  15. Brooke MH, Kaiser KK. Muscle fiber types: how many and what kind? Arch Neurol 1970;23:369-79. https://doi.org/10.1001/archneur.1970.00480280083010
  16. Lu X, Zhang Y, Zhu L, Luo X, Hopkins DL. Effect of superchilled storage on shelf life and quality characteristics of M. longissimus lumborum from Chinese Yellow cattle. Meat Sci 2019;149:79-84. https://doi.org/10.1016/j.meatsci.2018.11.014
  17. Li K, Zhang Y, Mao Y, et al. Effect of very fast chilling and aging time on ultra-structure and meat quality characteristics of Chinese Yellow cattle M. Longissimus lumborum. Meat Sci 2012;92:795-804. https://doi.org/10.1016/j.meatsci.2012.07.003
  18. Ryu YC, Choi YM, Lee SH, et al. Comparing the histochemical characteristics and meat quality traits of different pig breeds. Meat Sci 2008;80:363-9. https://doi.org/10.1016/j.meatsci.2007.12.020
  19. Oe M, Ojima K, Nakajima I, Chikuni K, Shibata M, Muroya S. Distribution of tropomyosin isoforms in different types of single fibers isolated from bovine skeletal muscles. Meat Sci 2016;118:129-32. https://doi.org/10.1016/j.meatsci.2016.04.013
  20. Schiaffino S, Reggiani C. Fiber types in mammalian skeletal muscles. Physiol Rev 2011;91:1447-531. https://doi.org/10.1152/physrev.00031.2010
  21. Liu C, Zhang Y, Yang X, et al. Potential mechanisms of carbon monoxide and high oxygen packaging in maintaining color stability of different bovine muscles. Meat Sci 2014;97:18996. https://doi.org/10.1016/j.meatsci.2014.01.027
  22. Suman SP, Hunt MC, Nair MN, Rentfrow G. Improving beef color stability: practical strategies and underlying mechanisms. Meat Sci 2014;98:490-504. https://doi.org/10.1016/j.meatsci.2014.06.032
  23. Kim YH, Keeton JT, Smith SB, Berghman LR, Savell JW. Role of lactate dehydrogenase in metmyoglobin reduction and color stability of different bovine muscles. Meat Sci 2009;83:376-82. https://doi.org/10.1016/j.meatsci.2009.06.009
  24. Kemp CM, Sensky PL, Bardsley RG, Buttery PJ, Parr T. Tenderness-an enzymatic view. Meat Sci 2010;84:248-56. https://doi.org/10.1016/j.meatsci.2009.06.008
  25. Hildrum KI, Rodbotten R, Hoy M, Berg J, Narum B, Wold JP. Classification of different bovine muscles according to sensory characteristics and Warner Bratzler shear force. Meat Sci 2009;83:302-7. https://doi.org/10.1016/j.meatsci.2009.05.016
  26. Veiseth-Kent E, Pedersen ME, Ronning SB, Rodbotten R. Can postmortem proteolysis explain tenderness differences in various bovine muscles? Meat Sci 2018;137:114-22. https://doi.org/10.1016/j.meatsci.2017.11.011
  27. Ozawa S, Mitsuhashi T, Mitsumoto M, et al. 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 2000;54:65-70. https://doi.org/10.1016/S0309-1740(99)00072-8
  28. Choe JH, Choi YM, Lee SH, et al. The relation between glycogen, lactate content and muscle fiber type composition, and their influence on postmortem glycolytic rate and pork quality. Meat Sci 2008;80:355-62. https://doi.org/10.1016/j.meatsci.2007.12.019
  29. Ryu YC, Kim BC. The relationship between muscle fiber characteristics, postmortem metabolic rate, and meat quality of pig longissimus dorsi muscle. Meat Sci 2005;71:351-7. https://doi.org/10.1016/j.meatsci.2005.04.015
  30. Francisco CL, Jorge AM, Dal-Pai-Silva M, Carani FR, Cabeco LC, Silva SR. Muscle fiber type characterization and myosin heavy chain (MyHC) isoform expression in Mediterranean buffaloes. Meat Sci 2011;88:535-41. https://doi.org/10.1016/j.meatsci.2011.02.007