Animal Bioscience

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

DOI QR Code

Meat quality, post-mortem proteolytic enzymes, and myosin heavy chain isoforms of different Thai native cattle muscles

  • Chaosap, Chanporn (Department of Agricultural Education, Faculty of Industrial Education and Technology, King Mongkut's Institute of Technology Ladkrabang) ;
  • Sivapirunthep, Panneepa (Department of Agricultural Education, Faculty of Industrial Education and Technology, King Mongkut's Institute of Technology Ladkrabang) ;
  • Sitthigripong, Ronachai (Department of Animal Technology and Fishery, Faculty of Agricultural Technology, King Mongkut's Institute of Technology Ladkrabang) ;
  • Tavitchasri, Piyada (Department of Animal Science, King Mongkut's Institute of Technology Ladkrabang, Prince of Chumphon Campus) ;
  • Maduae, Sabaiporn (Department of Animal Technology and Fishery, Faculty of Agricultural Technology, King Mongkut's Institute of Technology Ladkrabang) ;
  • Kusee, Tipyaporn (Department of Animal Technology and Fishery, Faculty of Agricultural Technology, King Mongkut's Institute of Technology Ladkrabang) ;
  • Setakul, Jutarat (Department of Animal Technology and Fishery, Faculty of Agricultural Technology, King Mongkut's Institute of Technology Ladkrabang) ;
  • Adeyemi, Kazeem (Department of Animal Production, Faculty of Agriculture, University of Ilorin)
  • Received : 2020.11.24
  • Accepted : 2021.04.10
  • Published : 2021.09.01
Download PDF
⟨ Previous Next ⟩

Abstract

Objective: This study investigated the meat quality characteristics, endogenous proteolytic enzymes, collagen content, and myosin heavy chain (MyHC) isoforms of different muscles of Thai native cattle (TNC). Methods: Infraspinatus (IF), Longissimus thoracis (LT), and Supraspinatus (SS) muscles were obtained from two TNC breeds, Kho-Lan (KL, n = 7) and Kho-Isaan (KI, n = 7). The muscle and meat characteristics of TNC breeds and their relationship with MyHC expression were examined. Results: Three MyHC isoforms namely MyHC I, MyHC IIa, and MyHC IIx were detected in the muscles. The KL had higher (p<0.05) MyHC IIx than the KI. The IF muscle had higher (p<0.05) MyHC I compared to other muscles. The LT muscle had the least MyHC I. The LT had higher (p<0.05) MyHC IIx than the IF and SS muscles. The IF presented the least MyHC IIx. The KL had higher (p<0.05) lightness and moisture content and lower crude protein, redness, cooking loss, shear force, and calpastatin than the KI. The glycogen, total collagen, soluble collagen, crude protein, ash contents, and troponin T degradation product of IF and SS were lower (p<0.05) than that of LT. Ether extract in LT was lower (p<0.05) than that of IF and SS. The percentage of MyHC I, MyHC IIa, and MyHC IIx were significantly correlated with muscle and meat characteristics of TNC. Conclusion: These results suggest that the differences in the MyHC isoforms may partly account for the variation in meat quality between breeds and among muscles of TNC.

Keywords

Acknowledgement

This work was supported by a research grant from the Thailand Research Fund (TRF) under grant number RDG5320048. Our special thanks to Prof. Tim Parr and Emeritus Prof. Ronald Bardsley, Division of Nutritional Biochemistry, School of Biosciences, University of Nottingham, for valuable comments and proofreading which greatly improved the manuscript.

References

  1. Information and Communication Technology Center. National Animal Statistics. Bangkok, Thailand: Department of Livestock Development; 2018.
  2. Wangkumhang P, Wilantho A, Shaw PJ, et al. Genetic analysis of Thai cattle reveals a Southeast Asian indicine ancestry. Peer J 2015;3:e1318. https://doi.org/10.7717/peerj.1318
  3. Kahi AK, Graser HU. Indigenous Thai beef cattle breeding scheme incorporating indirect measures of adaptation: sensitivity to changes in heritabilities of and genetic correlations between adaptation traits. Asian-Australas J Anim Sci 2004; 17:1039-46. https://doi.org/10.5713/ajas.2004.1039
  4. Sethakul J, Opatpatanakit Y, Sivapirunthep P, Intrapornudom P. Beef quality under production systems in Thailand: preliminary remarks. In: Proceedings of the 13th, AAAP Animal Science Congress Hanoi; 2008 Sept 22-26: Hanoi, Vietnam.
  5. Adeyemi KD, Shittu RM, Sabow AB, et al. Comparison of myofibrillar protein degradation, antioxidant profile, fatty acids, metmyoglobin reducing activity, physicochemical properties and sensory attributes of gluteus medius and infraspinatus muscles in goats. J Anim Sci Technol 2016; 58:23. https://doi.org/10.1186/s40781-016-0105-5
  6. Lefaucheur L, Ecolan P, Plantard L, Gueguen N. New insights into muscle fiber types in the pig. J Histochem Cytochem 2002;50:719-30. https://doi.org/10.1177/002215540205000513
  7. Choi Y, Kim B-C. Muscle fiber characteristics, myofibrillar protein isoforms, and meat quality. Livest Sci 2009;122:105-18. https://doi.org/10.1016/j.livsci.2008.08.015
  8. Hwang Y-H, Kim G-D, Jeong J-Y, Hur S-J, Joo S-T. 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
  9. Koohmaraie M, Geesink GH. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Sci 2006;74:34-43. https://doi.org/10.1016/j.meatsci.2006.04.025
  10. Picard B, Barboiron C, Chadeyron D, Jurie C. Protocol for high-resolution electrophoresis separation of myosin heavy chain isoforms in bovine skeletal muscle. Electrophoresis 2011;32:1804-6. https://doi.org/10.1002/elps.201100118
  11. Arther JSC, Mykles DL. Calpain zymography with casein or fluorescein isothiocyanate casein. In: Elce JS, editor. Calpain methods and protocols. Methods in molecular biology. Humana Press; 2000. pp. 109-16.
  12. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem 1951;193:265-75. https://doi.org/10.1016/S0021-9258(19)52451-6
  13. Chaosap C, Sitthigripong R, Sivapirunthep P, Pungsuk A, Adeyemi KD, Sazili AQ. Myosin heavy chain isoforms expression, calpain system and quality characteristics of different muscles in goats. Food Chem 2020;321:126677. https://doi.org/10.1016/j.foodchem.2020.126677
  14. AOAC International. Official methods of analysis of AOAC International. 18th ed. Gaithersburg, MD, USA: AOAC International; 2005.
  15. Dreiling CE, Brown DE, Casale L, Kelly L. Muscle glycogen: comparison of iodine binding and enzyme digestion assays and application to meat samples. Meat Sci 1987;20:167-77. https://doi.org/10.1016/0309-1740(87)90009-X
  16. Hill F. The solubility of intramuscular collagen in meat animals of various ages. J Food Sci 1966;31:161-6. https://doi.org/10.1111/j.1365-2621.1966.tb00472.x
  17. 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
  18. 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 2016; 36:819-28. https://doi.org/10.5851/kosfa.2016.36.6.819
  19. Waritthitham A, Lambertz C, Langholz HJ, Wicke M, Gauly M. Muscle fiber characteristics and their relationship to water holding capacity of Longissimus dorsi muscle in Brahman and Charolais crossbred bulls. Asian-Australas J Anim Sci 2010;23:665-71. https://doi.org/10.5713/ajas.2010.90482
  20. Kirchofer K, Calkins CR, Gwartney BL. Fiber-type composition of muscles of the beef chuck and round. J Anim Sci 2002;80:2872-8. https://doi.org/10.2527/2002.80112872x
  21. Xie X, Meng Q, Cui Z, Ren L. Effect of cattle breed on meat quality, muscle fiber characteristics, lipid oxidation and fatty acids in China. Asian-Australas J Anim Sci 2012;25:824-31. https://doi.org/10.5713/ajas.2011.11462
  22. 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
  23. Ferguson DM, Gerrard DE. Regulation of post-mortem glycolysis in ruminant muscle. Anim Prod Sci 2014;54:464-81. https://doi.org/10.1071/AN13088
  24. Onopiuk A, Poltorak A, Wierzbicka A. Influence of post-mortem muscle glycogen content on the quality of beef during aging. J Vet Res 2016;60:301-7. https://doi.org/10.1515/jvetres2016-0046
  25. Torrescano G, Sanchez-Escalante A, Gimenez B, Roncales P, Beltran JA. Shear values of raw samples of 14 bovine muscles and their relation to muscle collagen characteristics. Meat Sci 2003;64:85-91. https://doi.org/10.1016/S0309-1740(02)00165-1
  26. Rhee MS, Wheeler T, Shackelford S, Koohmaraie M. Variation in palatability and biochemical traits within and among eleven beef muscles. J Anim Sci 2004;82:534-50. https://doi.org/10.2527/2004.822534x
  27. Tortora GJ. Principles of human anatomy. 10th ed. Hoboken, NJ, USA: John Wiley & Sons, Inc; 2005.
  28. Nishimura T. The role of intramuscular connective tissue in meat texture. Anim Sci J 2010;81:21-7. https://doi.org/10.1111/j.1740-0929.2009.00696.x
  29. Sullivan G, Calkins C. Ranking beef muscles for Warner-Bratzler shear force and trained sensory panel ratings from published literature. J Food Qual 2011;34:195-203. https://doi.org/10.1111/j.1745-4557.2011.00386.x
  30. Christensen M, Henckel P, Purslow PP. Effect of muscle type on the rate of post-mortem proteolysis in pigs. Meat Sci 2004;66:595-601. https://doi.org/10.1016/S0309-1740(03)00175-x
  31. Koohmaraie M, Whipple G, Kretchmar DH, Crouse JD, Mersmann HJ. Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses. J Anim Sci 1991;69: 617-24. https://doi.org/10.2527/1991.692617x
  32. Whipple G, Koohmaraie M, Dikeman ME, Crouse JD, Hunt MC, Klemm RD. Evaluation of attributes that affect longissimus muscle tenderness in Bos taurus and Bos indicus cattle. J Anim Sci 1990;68:2716-28. https://doi.org/10.2527/1990.6892716x
  33. Geesink GH, Koohmaraie M. Postmortem proteolysis and calpain/calpastatin activity in callipyge and normal lamb biceps femoris during extended postmortem storage. J Anim Sci 1999;77:1490-501. https://doi.org/10.2527/1999.7761490x

Cited by

  1. The Effects of Using Pineapple Stem Starch as an Alternative Starch Source and Ageing Period on Meat Quality, Texture Profile, Ribonucleotide Content, and Fatty Acid Composition of Longissimus Thoraci vol.10, pp.10, 2021, https://doi.org/10.3390/foods10102319