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

키워드

참고문헌 (33)

1. Information and Communication Technology Center, "National Animal Statistics", Department of Livestock Development, ~ (2018)
2. Wangkumhang P, "Genetic analysis of Thai cattle reveals a Southeast Asian indicine ancestry", Peer J, 3, pp.e1318~ (2015)[DOI]
3. A. K. Kahi, "Indigenous Thai Beef Cattle Breeding Scheme Incorporating Indirect Measures of Adaptation: Sensitivity to Changes in Heritabilities of and Genetic Correlations between Adaptation Traits", Animal Bioscience, 17(8), pp.1039~1046 (2004), 아세아·태평양축산학회
4. Sethakul J, "Beef quality under production systems in Thailand: preliminary remarks", Proceedings of the 13th, AAAP Animal Science Congress (2008)
5. Awis Q. Sazili, "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", 한국축산학회지, 58(6), pp.1~17 (2016), 한국축산학회
6. Lefaucheur L, "New insights into muscle fiber types in the pig", J Histochem Cytochem, 50, pp.719~730 (2002)[DOI]
7. Choi Y, "Muscle fiber characteristics, myofibrillar protein isoforms, and meat quality", Livest Sci, 122, pp.105~118 (2009)[DOI]
8. Hwang Y-H, "The relationship between muscle fiber characteristics and meat quality traits of highly marbled Hanwoo(Korean native cattle)steers", Meat Sci, 86, pp.456~461 (2010)[DOI]
9. Koohmaraie M, "Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system", Meat Sci, 74, pp.34~43 (2006)[DOI]
10. Picard B, "Protocol for high-resolution electrophoresis separation of myosin heavy chain isoforms in bovine skeletal muscle", Electrophoresis, 32, pp.1804~1806 (2011)[DOI]
11. Arther JSC, "Calpain methods and protocols. Methods in molecular biology", pp.109~116 (2000), Humana Press
12. Lowry OH, "Protein measurement with the Folin phenol reagent", J Biol Chem, 193, pp.265~275 (1951)
13. Chaosap C, "Myosin heavy chain isoforms expression, calpain system and quality characteristics of different muscles in goats", Food Chem, 321, pp.126677~ (2020)[DOI]
14. AOAC International, "Official methods of analysis of AOAC International. 18th ed", AOAC International, ~ (2005)
15. Dreiling CE, "Muscle glycogen : comparison of iodine binding and enzyme digestion assays and application to meat samples", Meat Sci, 20, pp.167~177 (1987)[DOI]
16. Hill F, "The solubility of intramuscular collagen in meat animals of various ages", J Food Sci, 31, pp.161~166 (1966)
17. Picard B, "Evidence for expression of IIb myosin heavy chain isoform in some skeletal muscles of Blonde d’Aquitaine bulls", Meat Sci, 82, pp.30~36 (2009)[DOI]
18. 김갑돈, "Comparison of Characteristics of Myosin Heavy Chain-based Fiber and Meat Quality among Four Bovine Skeletal Muscles", 한국축산식품학회지, 36(6), pp.819~828 (2016), 한국축산식품학회
19. C. Lambertz, "Muscle Fiber Characteristics and Their Relationship to Water Holding Capacity of Longissimus dorsi Muscle in Brahman and Charolais Crossbred Bulls", Animal Bioscience, 23(5), pp.665~671 (2010), 아세아·태평양축산학회
20. Kirchofer K, "Fiber-type composition of muscles of the beef chuck and round", J Anim Sci, 80, pp.2872~2878 (2002)[DOI]
21. Xiangxue Xie, "Effect of Cattle Breed on Meat Quality, Muscle Fiber Characteristics, Lipid Oxidation and Fatty Acids in China", Animal Bioscience, 25(6), pp.824~831 (2012), 아세아·태평양축산학회[DOI]
22. Choe JH, "The relation between glycogen, lactate content and muscle fiber type composition, and their influence on postmortem glycolytic rate and pork quality", Meat Sci, 80, pp.355~362 (2008)[DOI]
23. Ferguson DM, "Regulation of post-mortem glycolysis in ruminant muscle", Anim Prod Sci, 54, pp.464~481 (2014)[DOI]
24. Onopiuk A, "Influence of postmortem muscle glycogen content on the quality of beef during aging", J Vet Res, 60, pp.301~307 (2016)[DOI]
25. Torrescano G, "Shear values of raw samples of 14 bovine muscles and their relation to muscle collagen characteristics", Meat Sci, 64, pp.85~91 (2003)[DOI]
26. Rhee MS, "Variation in palatability and biochemical traits within and among eleven beef muscles", J Anim Sci, 82, pp.534~550 (2004)[DOI]
27. Tortora GJ, "Principles of human anatomy" (2005), John Wiley & Sons, Inc
28. Nishimura T, "The role of intramuscular connective tissue in meat texture", Anim Sci J, 81, pp.21~27 (2010)[DOI]
29. Sullivan G, "Ranking beef muscles for Warner–Bratzler shear force and trained sensory panel ratings from published literature", J Food Qual, 34, pp.195~203 (2011)[DOI]
30. Christensen M, "Effect of muscle type on the rate of post-mortem proteolysis in pigs", Meat Sci, 66, pp.595~601 (2004)[DOI]
31. Koohmaraie M, "Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses", J Anim Sci, 69, pp.617~624 (1991)[DOI]
32. Whipple G, "Evaluation of attributes that affect longissimus muscle tenderness in Bos taurus and Bos indicus cattle", J Anim Sci, 68, pp.2716~2728 (1990)[DOI]
33. Geesink GH, "Postmortem proteolysis and calpain", calpastatin activity in callipyge and normal lamb biceps femoris during extended postmortem storage, 1999, pp.77, 1490~1501

관련 논문AI추천