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http://dx.doi.org/10.5851/kosfa.2022.e40

Comparison of Meat Quality and Muscle Fiber Characteristics between Porcine Skeletal Muscles with Different Architectures  

Park, Junyoung (Mgenic Bio)
Song, Sumin (Graduate School of International Agricultural Technology, Seoul National University)
Cheng, Huilin (Graduate School of International Agricultural Technology, Seoul National University)
Im, Choeun (Graduate School of International Agricultural Technology, Seoul National University)
Jung, Eun-Young (Institutes of Green Bio Science & Technology, Seoul National University)
Moon, Sung Sil (Sunjin Technology & Research Institute)
Choi, Jungseok (Department of Animal Science, Chungbuk National University)
Hur, Sun Jin (Department of Animal Science and Technology, Chung-Ang University)
Joo, Seon-Tea (Division of Applied Life Science (BK21 Four), Institute of Agriculture & Life Science, Gyeongsang National University)
Kim, Gap-Don (Graduate School of International Agricultural Technology, Seoul National University)
Publication Information
Food Science of Animal Resources / v.42, no.5, 2022 , pp. 874-888 More about this Journal
Abstract
This study aimed to compare the similarities, physicochemical properties, and muscle fiber characteristics of porcine skeletal muscles. Fourteen types of muscles were collected from nine pig carcasses at 24 h post-mortem and classified by muscle architecture into two main groups, namely parallel and pennate. The muscles were further differentiated into three subtypes per group. These included fan-shaped, fusiform, and strap for the parallel group, and unipennate, bipennate, and multipennate for the pennate group. Parallel-fibered muscles, which were composed of larger I, IIA, IIX, and IIXB fibers and a lower density of IIA fibers, showed higher redness and yellowness values than pennate-fibered muscles (p<0.05). However, the relative fiber area was not significantly different between the parallel and pennate groups (p>0.05). In the subtypes of parallel architecture, the strap group showed lower moisture content and higher redness values than the other subtypes and had considerably higher amounts of oxidative fibers (I and IIA; 72.3%) than the fan-shaped and fusiform groups (p<0.05). In the pennate group, unipennate showed comparatively lower moisture content and higher lightness than other pennate subtypes and was composed of smaller I, IIA, and IIX fibers than the bipennate and multipennate groups (p<0.05). Finally, a different trend of muscle clustering by hierarchical cluster analysis was found between physicochemical properties and muscle fiber characteristics. These results suggest that the physicochemical properties and muscle fiber characteristics of porcine skeletal muscles are not significantly dependent on morphological properties but are rather related to the intrinsic properties of the individual muscles.
Keywords
muscle architecture; parallel; pennate; meat quality; muscle fiber characteristics;
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1 Choi YM, Ryu YC, Kim BC. 2007. Influence of myosin heavy- and light chain isoforms on early postmortem glycolytic rate and pork quality. Meat Sci 76:281-288.   DOI
2 Davies AS. 1981. Quadrupedal mechanics: Anatomical principles of the musculoskeletal system. Massey University Press, Palmerston North, New Zealand. pp 31-40.
3 Ryu YC, Kim BC. 2005. The relationship between muscle fiber characteristics, postmortem metabolic rate, and meat quality of pig longissimus dorsi muscle. Meat Sci 71:351-357.   DOI
4 Song S, Ahn CH, Kim GD. 2020. Muscle fiber typing in bovine and porcine skeletal muscles using immunofluorescence with monoclonal antibodies specific to myosin heavy chain isoforms. Food Sci Anim Resour 40:132-144.   DOI
5 Totland GK, Kryvi H. 1991. Distribution patterns of muscle fibre types in major muscles of the bull (Bos taurus). Anat Embryol 184:441-450.   DOI
6 Hwang YH, Kim GD, Jeong JY, Hur SJ, Joo ST. 2010. The relationship between muscle fiber characteristics and meat quality traits of highly marbled Hanwoo (Korean native cattle) steers. Meat Sci 86:456-461.   DOI
7 Farup J, Sorensen H, Kjolhede T. 2014. Similar changes in muscle fiber phenotype with differentiated consequences for rate of force development: Endurance versus resistance training. Hum Mov Sci 34:109-119.   DOI
8 Guth L, Samaha FJ. 1969. Qualitative differences between actomyosin ATPase of slow and fast mammalian muscle. Exp Neurol 25:138-152.   DOI
9 Honikel KO. 1987. How to measure the water-holding capacity of meat? Recommendation of standardized methods. In Evaluation and control of meat quality in pigs. Tarrant PV, Eikelenboom G, Monin G (ed). Springer, Dordrecht, Netherlands. pp 129-142.
10 Joo ST, Kim GD, Hwang YH, Ryu YC. 2013. Control of fresh meat quality through manipulation of muscle fiber characteristics. Meat Sci 95:828-836.   DOI
11 Karlsson AH, Klont RE, Fernandez X. 1999. Skeletal muscle fibres as factors for pork quality. Livest Prod Sci 60:255-269.   DOI
12 Lieber RL, Friden J. 2000. Functional and clinical significance of skeletal muscle architecture. Muscle Nerve 23:1647-1666.   DOI
13 Kim GD, Jeong JY, Hur SJ, Yang HS, Jeon JT, Joo ST. 2010. The relationship between meat color (CIE L* and a*), myoglobin content, and their influence on muscle fiber characteristics and pork quality. Korean J Food Sci Anim Resour 30:626-633.   DOI
14 Kim GD, Overholt MF, Lowell JE, Harsh BN, Klehm BJ, Dilger AC, Boler DD. 2018. Evaluation of muscle fiber characteristics based on muscle fiber volume in porcine longissimus muscle in relation to pork quality. Meat Muscle Biol 2:362-374.   DOI
15 Kim GD, Yang HS, Jeong JY. 2016. Comparison of characteristics of myosin heavy chain-based fiber and meat quality among four bovine skeletal muscles. Korean J Food Sci Anim Resour 36:819-828.   DOI
16 Klont RE, Brocks L, Eikelenboom G. 1998. Muscle fibre type and meat quality. Meat Sci 49:S219-S229.   DOI
17 Lieber RL. 2002. Skeletal muscle structure, function, and plasticity. Lippincott Williams & Wilkins, Philadelphia, PA, USA. pp 35-41.
18 Maclntosh BR, Gardiner PF, McComas AJ. 2006. Skeletal muscle: Form and function. 2nd ed. Human Kinetics, Champaign, IL, USA. pp 4-64.
19 Maltin CA, Warkup CC, Matthews KR, Grant CM, Porter AD, Delday MI. 1997. Pig muscle fibre characteristics as a source of variation in eating quality. Meat Sci 47:237-248.   DOI
20 Ward SR, Eng CM, Smallwood LH, Lieber RL. 2009. Are current measurements of lower extremity muscle architecture accurate? Clin Orthop Relat Res 467:1074-1082.   DOI
21 Wilson PD. 2014. Reference module in biomedical sciences: Anatomy of muscle. 3rd ed. Elsevier, Amsterdam, Netherlands. pp 823-824.
22 Woittiez RD, Huijing PA, Boom HBK, Rozendal RH. 1984. A three-dimensional muscle model: A quantified relation between form and function of skeletal muscles. J Morphol 182:95-113.   DOI
23 Sutherland DH, Cooper L, Daniel D. 1980. The role of the ankle plantar flexors in normal walking. J Bone Joint Surg 62:354-363.   DOI
24 Monin G, Ouali A. 1992. Muscle differentiation and meat quality. In Developments in meat science. Lawrie R (ed). Elsevier Applied Science, London, UK. pp 89-157.
25 Narici M. 1999. Human skeletal muscle architecture studied in vivo by non-invasive imaging techniques: Functional significance and applications. J Electromyogr Kinesiol 9:97-103.   DOI
26 Ozawa S, Mitsuhashi T, Mitsumoto M, Matsumoto S, Itoh N, Itagaki K, Kohno Y, Dohgo T. 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.   DOI
27 Pette D, Staron RS. 1990. Cellular and molecular diversities of mammalian skeletal muscle fibers. Rev Physiol Biochem Pharmacol 116:1-76.
28 Roy RR, Edgerton VR. 2009. Skeletal muscle architecture. In Encyclopedia of neuroscience. Hirokawa N, Binder MD, Windhorst U (ed). Springer, Berlin, Germany. pp 272-324.
29 Waritthitham A, Lambertz C, Langholz HJ, Wicke M, Gauly M. 2010. 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 23:665-671.   DOI
30 Zajac FE. 1989. Muscle and tendon: Properties, models, scaling, and application to biomechanics and motor control. Crit Rev Biomed Eng 17:359-411.
31 Folch J, Lees M, Sloane Stanley GH. 1957. A simple method for the isolation and purification of total lipides from animal tissues. J Biol Chem 226:497-509.   DOI
32 Armstrong RB, Delp MD, Goljan EF, Laughlin MH. 1987. Distribution of blood flow in muscles of miniature swine during exercise. J Appl Physiol 62:1285-1298.   DOI
33 Cheng H, Song S, Kim GD. 2021. Frozen/thawed meat quality associated with muscle fiber characteristics of porcine longissimus thoracis et lumborum, psoas major, semimembranosus, and semitendinosus muscles. Sci Rep 11:13354.
34 Commission Internationale de l'Eclairagev [CIE]. 1977. CIE recommendations on uniform color spaces, color differences equations, and metric color terms. Color Res Appl 2:5-6.   DOI
35 Choi YM, Kim BC. 2009. Muscle fiber characteristics, myofibrillar protein isoforms, and meat quality. Livest Sci 122:105-118.   DOI
36 AOAC. 2000. Official methods of analysis of AOAC International. 18th ed. AOAC International, Washington, DC, USA. p 931.
37 Bee G, Guex G, Herzog W. 2004. Free-range rearing of pigs during the winter: Adaptations in muscle fiber characteristics and effects on adipose tissue composition and meat quality traits. J Anim Sci 82:1206-1218.   DOI
38 Cheng H, Song S, Jung EY, Jeong JY, Joo ST, Kim GD. 2020. Comparison of beef quality influenced by freeze-thawing among different beef cuts having different muscle fiber characteristics. Meat Sci 169:108206.