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)
  • 투고 : 2020.11.24
  • 심사 : 2021.04.10
  • 발행 : 2021.09.01


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.



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.


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