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 stud...
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.
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.
* AI 자동 식별 결과로 적합하지 않은 문장이 있을 수 있으니, 이용에 유의하시기 바랍니다.
문제 정의
Therefore, the purpose of this study is to investigate the different characteristics of MHC-based muscle fiber among four major bovine skeletal muscles and consequently, the differences in beef quality. Immunohistochemistry using commercial monoclonal antibodies specific to bovine MHCs was conducted to classify the MHCbased fiber types.
(2010) reported that the fiber size (diameter) is negatively correlated with myoglobin content regardless of fiber types. These observations support our findings regarding the myoglobin content and its relationship with muscle fiber density and CSA. Nevertheless, meat color did not follow myoglobin content with regard to muscle fiber characteristics.
대상 데이터
Four bovine skeletal muscles (LT, PM, SM and ST) were obtained from eighteen Hanwoo (Korean native cattle) steers (653±48 kg body weight at 28 mon old) at 24 h postmortem from a commercial slaughter house.
데이터처리
An analysis of variance test and Duncan’s multiple range tests were performed to determine the differences in the muscle fiber characteristics and meat quality among the muscles using the Statistical Analysis Software (SAS, ver. 9.4, SAS Institute Inc., USA).
The relationships among the muscle fiber characteristics and between muscle fiber characteristics and meat quality were analyzed using Pearson’s correlation coefficients (r).
To estimate the relationships between muscle fiber density, CSA and fiber area composition, Pearson correlation coefficients were evaluated (Fig. 3). Fiber density negatively correlated with CSA regardless of fiber type (p<0.
이론/모형
3198) and presented as the Commission Internationale de l’Eclairage (CIE) L*, a*, and b* values. Drip loss (%) was determined using the Honikel (1987) method. For analysis of cooking loss, the muscle samples were packed with plastic bags and cooked in a water bath at 75℃ to an internal tempera ture of 70℃.
0 g muscle homogenates in 27 mL of deionized water. Moisture content (%) was determined according to the AOAC (2000) method. Fat content was determined by Folch et al.
Preparation of myofibrillar proteins for LC-MS/MS analysis was conducted by the Talmadge and Roy (1993) method with modification. In brief, eighty transverse sections (10 µm thickness) were collected using a cryostat microtome (CM 1860, Leica Biosystems, Germany) at -21℃ and myofibrillar proteins were extracted in 1.
, USA) for Warner-Bratzer shear force (WBSF) (N). Sarcomere length was determined according to the Cross et al. (1981) method. In brief, muscle samples were placed in solution I (0.
The pellet was resuspended in 500 µl of buffer (7 M urea and 2 M thiourea) and centrifuged at 10,000 g for 30 min. The protein concentration was determined by the Bradford (1976) method. Reduction and alkylation were conducted with 5 mM DTT at 37℃ for 45 min and 25 mM iodoacetamide at RT for 1 h, respectively.
성능/효과
However, ST muscle had the highest composition of type IIX and had poor quality (low pH, redness and sarcomere length and high drip loss). In conclusion, 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.
Significantly higher CSA was observed in type IIX than in types I and IIA in LT, PM and SM muscles (p<0.05), whereas SM muscle had no significant difference in CSA among the fiber types (p>0.05).
Similar to the fiber density, LT, PM and SM muscles had the highest composition of type IIA fibers (58.9% for LT, 46.3% for PM, and 44.3% for SM), whereas ST muscle had a higher composition of type IIX fibers (62.3%), compared to the other fiber types (p<0.05).
The lowest drip loss was observed in LT muscle, while the lowest WBSF and the highest sarcomere length were found in PM among the muscles (p<0.05).
The remarkable finding is that all the fiber types of PM had the highest density compared to other muscles (p<0.05).
These results indicate that the muscle fiber composition of type IIX is closely related to poor beef quality, especially color (negatively correlated with myoglobin content and CIE a*), WHC (positively correlated with drip loss) and tenderness (positively correlation with WBSF and negatively correlated with sarcomere length). However, the fiber area composition of type IIA is closely related to high redness (CIE a*) and WHC (negatively correlated with drip loss).
참고문헌 (38)
1. Abreu E. Quirox-Rothe E. Mayoral A. I. Vivo J. M. Robina Á. Guillén M. T. Agüera E. Rivero J. L. 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. 2006 74 359 372 10.1016/j.meatsci.2006.04.002 22062847
2. Acevedo L. M. Rivero J. L. L. New insights into skeletal muscle fibre types in the dog with particular focus towards hybrid myosin phenotypes Cell Tissue Res. 2006 323 283 303 10.1007/s00441-005-0057-4 16163488
3. AOAC Official methods of analysis (17th ed.) Association of Official Analytical Chemists Gaithersburg, MD 2000
4. Arbanas J. Klasan G. S. Nikolic M. Jerkovic R. Miljanovic I. Malner D. Fibre type composition of the human psoas major muscle with regard to the level of its orgin J. Anat. 2009 215 636 641 10.1111/j.1469-7580.2009.01155.x 19930517
5. Bexa T. J. Hutcheson J. P. Miller M. F. Brooks J. C. Nichols W. T. Streeter M. N. Yates D. A. Johnson B. J. 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. 2010 88 330 337 10.2527/jas.2009-1797 19783693
6. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding Anal. Biochem. 1976 72 248 254 10.1016/0003-2697(76)90527-3 942051
7. Brooke M. H. Kaiser K. K. Three myosin adenosine triphosphatase system: The nature of their pH liability and sulphydryl dependence J. Histochem. Cytochem. 1970 18 670 672 10.1177/18.9.670 4249441
8. Chang K. C. Costa N. Blackley R. Southwood O. Evans G. Plastow G. Wood J. D. Richardson R. I. Relationships of myosin heavy chain fibre types to meat quality traits in traditional and modern pigs Meat Sci. 2003 64 93 103 10.1016/S0309-1740(02)00208-5 22062667
9. Chikuni K. Muroya S. Nakajima I. Myosin heavy chains expressed in bovine skeletal muscles Meat Sci. 2004 67 87 94 10.1016/j.meatsci.2003.09.011 22061120
10. Cross H. R. West R. L. Dutson T. R. Comparison of methods for measuring sarcomere length in beef semitendinosus muscle Meat Sci. 1981 5 261 266 10.1016/0309-1740(81)90016-4 22056091
11. Folch J. Lees M. Sloane-Stanley G. H. A simple method for the isolation and purification of total lipids from animal tissues J. Biol. Chem. 1957 226 497 509 13428781
12. Gonzalez J. M. Johnson S. E. Thrift T. A. Sevell J. D. Ouellette S. E. Johnson D. D. Effect of ractopamine-hydrochloride on the fiber type distribution and shelf-life of six muscles of steers J. Anim. Sci. 2009 87 1764 1771 10.2527/jas.2008-1469 19181765
13. Greenwood P. L. Tomkins N. W. Hunter R. A. Allingham P. G. Harden S. Harper G. S. Bovine myofiber characteristics are influenced by postweaning nutrition J. Anim. Sci. 2009 87 3114 3132 10.2527/jas.2009-1936 19542515
14. Guth L. Samaha F. J. Qualitative differences between actomyosin ATPase of slow and fast mammalian muscle Exp. Neurol. 1969 25 138 152 10.1016/0014-4886(69)90077-6 4241609
15. Herpin P. Lefaucheur L. Adaptive changes in oxidative metabolism in skeletal muscle of cold-acclimated piglets J. Therm. Biol. 1992 17 277 285 10.1016/0306-4565(92)90067-P
16. Honikel K. O. Tarrant P. V. Eikelenboom G. Monin G. Recommendation of standardized methods. Evaluation and control of meat quality in pigs Martinus Nijhoff Dordecht, The Netherlands 1987 129 142 How to measure the water-holding capacity of meat?
17. 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 86 456 461 10.1016/j.meatsci.2010.05.034 20598446
18. Jurie C. Picard B. Geay Y. Influences of the method of housing bulls on their body composition and muscle fibre types Meat Sci. 1998 50 457 469 10.1016/S0309-1740(98)00059-X 22061348
19. Karlsson A. Enfalt A. C. Essen-Gustavsson B. Lundstrom K. Rydhmer L. Stern S. Muscle histochemical and biochemical properties in relation to meat quality during selection for increased lean tissue growth rate in pigs J. Anim. Sci. 1993 71 930 938 8478293
20. Kim G. D. Analysis of myosin heavy chain isoforms from longissimus thoracis muscle of Hanwoo steer by electrophoresis and LC-MS/MS Korean J. Food Sci. An. 2014 34 656 664 10.5851/kosfa.2014.34.5.656
21. Kim G. D. Ryu Y. C. Jeong J. Y. Yang H. S. Joo S. T. Relationship between pork quality and characteristics of muscle fibers classified by the distribution of myosin heavy chain isoforms J. Anim. Sci. 2013 91 5525 5534 10.2527/jas.2013-6614 23989883
22. Kim G. D. Ryu Y. C. Jo C. Lee J. K. Yang H. S. Jeong J. Y. Joo S. T. The characteristics of myosin heavy chain-based fiber types in porcine longissimus dorsi muscle Meat Sci. 2014 96 712 718 10.1016/j.meatsci.2013.09.028 24200562
23. Kirchofer K. S. Calkins C. R. Gwartney B. L. Fiber-type composition of muscles of the beef chuck and round J. Anim. Sci. 2002 80 2872 2878 10.2527/2002.80112872x 12462254
24. Kołczak T. Pospiech E. Palka K. Łącki J. Changes in structure of psoas major and minor and semitendinosus muscles of calves, heifers and cows during post-mortem ageing Meat Sci. 2003 64 77 83 10.1016/S0309-1740(02)00164-X 22062665
25. Larzul C. Lefaucheur L. Ecolan P. Gogue J. Talmant A. Sellier P. 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. 1997 75 3126 3137 10.2527/1997.75123126x 9419985
27. Lefaucheur L. Ecolan P. Plantard L. Gueguen N. New insights into muscle fiber types in the pig J. Histochem. Cytochem. 2002 50 719 730 10.1177/002215540205000513 11967283
28. Levitsky D. I. Actomyosin systems of biological motility Biochemistry (Moscow) 2004 69 Levitsky, D. I. 1177 1189 10.1007/s10541-005-0063-x 15627371
29. Maccatrozzo L. Patruno M. Toniolo L. Reggiani C. Mascarello F. Myosin heavy chain 2B isoform is expressed in specialized eye muscles but not in trunk and limb muscles of cattle Eur. J. Histochem. 2004 48 357 366 15718201
30. McKenna D. R. Mies P. D. Baird B. E. Pfeiffer K. D. Ellebracht J. W. Savell J. W. Biochemical and physical factors affecting discoloration characteristics of 19 bovine muscles Meat Sci. 2005 70 665 682 10.1016/j.meatsci.2005.02.016 22063894
32. Ozawa S. Mitsuhashi T. Mitsumoto M. Matsumoto S. Itoh N. Itagaki K. 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 10.1016/S0309-1740(99)00072-8 22063713
33. Renand G. Picard B. Touraille C. Berge P. Lepetit J. Relationships between muscle characteristics and meat quality traits of young Charolais bulls Meat Sci. 2001 59 49 60 10.1016/S0309-1740(01)00051-1 22062505
34. Rodriguez J. Unruh J. Villarreal M. Murillo O. Rojas S. Camacho J. Jaeger J. Reinhardt C. Carcass and meat quality characteristics of Brahman cross bulls and steers finished on tropical pastures in Costa Rica Meat Sci. 2014 96 1340 1344 10.1016/j.meatsci.2013.10.024 24342184
35. Ryu Y. C. Choi Y. M. Lee S. H. Shin H. G. Choe J. H. Kim B. C. Comparing the histochemical characteristics and meat quality traits of different pig breeds Meat Sci. 2008 80 363 369 10.1016/j.meatsci.2007.12.020 22063341
36. Ryu Y. C. Kim B. C. The relationship between muscle fiber characteristics, postmortem metabolic rate, and meat quality of pig longissimus dorsi muscle Meat Sci. 2005 71 351 357 10.1016/j.meatsci.2005.04.015 22064236
37. Solomon M. B. Lynch G. P. Biochemical, histochemical and palatability characteristics of young ram lambs as affected by diet and electrical stimulation J. Anim. Sci. 1988 66 1955 1962 10.2527/jas1988.6681955x
※ AI-Helper는 부적절한 답변을 할 수 있습니다.