Pengcheng WEN, Qiaoneng YANG, Weibing ZHANG, Min YANG, Qi LIANG, Yaoyao JIAO, Yanli ZHU

Comparison of Tenderness and Calpains Activity of Yak Meat in Different Ages During Postmortem Aging

Yak is a rare breed of resources in Tibetan Plateau, with high protein and low-fat content, and has other important application value. Yaks are managed by herders and slaughtered in various ages, changing from three years to twelve years of age, and there has a significant difference on meat tenderness in different ages. This study was conducted to investigate the effects of age at harvest, ageing time and the correlation analysis to meat tenderness calpains activity. The work may be used to establish a classification system and grading standards for yak meat. Four groups were established as fewer than 3 years-old, 3-5 years-old, 5-7 years-old and more than 7-years old. The results demonstrated that the content of tenderness has significantly different (P

Farklı Yaşlardaki Yaklara Ait Etlerin Postmortem Olgunlaştırma Sürecinde Yumuşaklık ve Kalpain Aktivitelerinin Karşılaştırılması

Yak, Tibet Platosu’nda yaşayan, yüksek protein ve düşük yağ içerikli etinin yanı sıra uygulamada önemli değere sahip diğer nitelikleri ile nadir bir cinstir. Çobanlar tarafından idare edilen Yakların, 3-20 arasında değişen yaşlarda kesimleri gerçekleştirilir ve bu yaş farklılıkları etin yumuşaklığı üzerinde belirgin bir fark oluşturur. Bu çalışma, kesim yaşı, olgunlaştırma zamanı ve korelasyon analizinin etin yumuşaklık kalpain aktivitesine etkisini araştırmak üzere yürütülmüştür. Çalışma sonuçları, Yak etinin sınınıflandırma sistemi ve derecelendirme standardının oluşturulmasında yararlı olabilir. Araştırmada 3 yaşından küçük, 3-5 yaş arası, 5-7 yaş arası ve 7 yaşından büyük olmak üzere 4 grup oluşturulmuştur. Bulgular, yumuşaklık göstergesi olan parametrelerin yaş gruplarına göre belirgin bir şekilde değiştiğini (P

PDF

___

1. Mishra BP, Mishra J, Pati PK, Rath PK: Dehydrated meat products: A review. Int J Livest Res, 7, 10-22, 2017. DOI: 10.5455/ijlr.20170812035616

2. Lopa B, Herbert WO: Yak’s Biochemistry contain the factors that make it possible for human habitation on the top of the world in central Asia. Biomed J Sci Tech Res, 1 (5): 1325-1327, 2017. DOI: 10.26717/ BJSTR.2017.01.000430

3. Bai B, Hao L, Chai S, Niu J, Wang W, Liu S: Progress in understanding meat quality characteristics of yak. Food Sci, 35, 290-296, 2014.

4. Hao L, Yang X, Huang Y, Hocquette JF, Bryant RH, Xun W, Niu J, Sun L, Chai S, Ding L, Long R, Liu S: Using mineral elements to authenticate the geographical origin of Yak meat. Kafkas Univ Vet Fak Derg, 25 (1): 9398, 2019. DOI: 10.9775/kvfd.2018.20366

5. Luo XL, Tong ZB, Wei YP, Zhao XQ: Meat characteristics of Qinghai yak and semi‐wild yak. Anim Sci J, 77 (2): 230-234, 2006. DOI: 10.1111/j.17400929.2006.00342.x

6. Kim JH, Kim DH, Ji DS, Lee HJ, Yoon DK, Lee CH: Effect of aging process and time on physicochemical and sensory evaluation of raw beef top round and shank muscles using an electronic tongue. Korean J Food Sci Anim Resour, 37 (6): 823–832, 2017. DOI: 10.5851/kosfa.2017.37.6.823

7. Sosin-Bzducha E, Puchała M: Effect of breed and aging time on physicochemical and organoleptic quality of beef and its oxidative stability. Arch Anim Breed, 60, 191-198, 2017. DOI: 10.5194/aab-60-191-2017.

8. Cafferky J, Hamill RM, Allen P, O’Doherty JV, Cromie A, Sweeney T: Effect of breed and gender on meat quality of m. longissimus thoracis et lumborum muscle from crossbred beef bulls and steers. Foods, 8 (5): 173, 2019. DOI: 10.3390/foods8050173

9. Ramayo-Caldas Y, Renand G, Ballester M, Saintilan R, Rocha D: Multi-breed and multi-trait co-association analysis of meat tenderness and other meat quality traits in three French beef cattle breeds. Genet Sel Evol, 48:37, 2016. DOI: 10.1186/s12711-016-0216-y

10. Li S, Tang S, Yan L, Li R: Effects of microwave heating on physicochemical properties, microstructure and volatile profiles of yak meat. J Appl Anim Res, 47, 262-272, 2019. DOI: 10.1080/09712119.2019.1624553

11. Wiklund E, Kemp RM, LeRoux GJ, Li Y, Wu G: Spray chilling of deer carcasses - Effects on carcass weight, meat moisture content, purge and microbiological quality. Meat Sci, 86 (4): 926-930, 2010. DOI: 10.1016/j. meatsci.2010.07.018

12. Kriese PR, Soares AL, Guarnieri PD, Prudencio SH, Ida E, lza I, Shimokomaki M: Biochemical and sensorial evaluation of intact and boned broiler breast meat tenderness during ageing. Food Chem, 104 (4): 1618-1621, 2007. DOI: 10.1016/j.foodchem.2007.03.003

13. Xu PT, Li Q, Sheng JJ, Chang H, Song Z, Yu ZB: Passive stretch reduces calpain activity through nitric oxide pathway in unloaded soleus muscles. Mol Cell Biochem, 367 (1-2): 113-124, 2012. DOI: 10.1007/s11010012-1325-8

14. Delgado EF, Geesink GH, Marchello JA, Goll DE, Koohmaraie: The calpain system in three muscles of normal and callipyge sheep. J Anim Sci, 79 (2): 398-412, 2001. DOI: 10.2527/2001.792398x

15. Koohmaraie M, Geesink GH: Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpainsystem. Meat Sci, 74, 34-43, 2006. DOI: 10.1016/j. meatsci.2006.04.025

16. Huang J, Forsberg NE: Role of calpain in skeletal-muscle protein degradation. Proc Natl Acad Sci USA, 95, 12100-12105, 1998. DOI: 10.1073/ pnas.95.21.12100

17. Liu G, Xiong YL: Contribution of lipid and protein oxidation to rheological differences between chicken white and red muscle mvofibrilla proteins. J Agric Food Chem, 44, 779-784, 1996. DOI: 10.1021/jf9506242

18. Beckman JS, Beckman TW, Chen J, Marshall PA, Freeman BA: Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci USA, 87 (4): 1620-1624, 1990. DOI: 10.1073/pnas.87.4.1620

19. Hu P, Luo X, Du F: A review on purification about calpains of bovine m. longissimus by deae-sepharose-ff ion-exchange chromatography. Innovational Edition of Farm Products Processing, 59, 43-45, 2010.

20. Brooks JC, Savell JW: Perimysium thickness as an indicator of beef tenderness. Meat Sci, 67, 329-334, 2004. DOI: 10.1016/j.meatsci. 2003.10.019

21. Light N, Champion AE, Voyle C, Bailey AJ: The role of epimysial, perimysial and endomysial collagen in determining texture in six bovine muscles. Meat Sci, 13 (3): 137-149, 1985. DOI: 10.1016/03091740(85)90054-3

22. Veiseth E, Shackelford SD, Wheeler TL, Koohmaraie M: Indicators of tenderization are detectable by 12 h postmortem in ovine longissimus. J Anim Sci, 82 (5): 1428-1436, 2004. DOI: 10.2527/2004.8251428x

23. Kolczak T, Pospiech E, Palka K, Łącki J: Changes in structure of psoasmajor and minor and semitendinosus muscles from calves, heifers and cows during postmortem aging. Meat Sci, 64, 77-83, 2003. DOI: 10.1016/S0309-1740(02)00164-X

24. Bo X, Guanghong Z, Xinglin X, Chunbao L: Venison in different parts of the maturation process after slaughter ultrastructure. Bulletin of Nanjing Agricultural University, 31 (1): 107-111, 2008.

25. Hopkins DL, Thompson JM: Inhibition of protease activity. Part 1. The effect on tenderness and indicators of proteolysis in ovine muscle. Meat Sci, 59 (2): 175-185, 2001. DOI: 10.1016/S0309-1740(01)00068-7

26. Koohmaraie M: Quantification of Ca2+-dependent protease activities byhydrophobic ion-exchange chromatography. J Anim Sci, 68, 659-665, 1990. DOI: 10.2527/1990.683659x

27. Bhat ZF, Morton JD, Mason SL, Bekhit AEA: Role of calpain system in meat tenderness: A review. Food Sci Hum Well, 7, 196-204, 2018. DOI: 10.1016/j.fshw.2018.08.002

28. Kristensen L, Christensen M, Ertbjerg P: Activities of calpastatin, μ-calpain and m-calpain are stable during frozen storage of meat. Meat Sci, 72 (1): 116-120, 2006. DOI: 10.1016/j.meatsci.2005.06.010

29. Kristensen L, Therkildsen M, Riis B, Sørensen MT, Oksbjerg N, Purslow PP, Ertbjerg P: Dietary-induced changes of muscle growth rate in pigs: Effects on in vivo and postmortem muscle proteolysis and meat quality. J Anim Sci, 80 (11): 2862-2871, 2002. DOI: 10.2527/2002.80112862x

30. Whipple G, Koohmaraie M: Calcium chloride marination effects on beef steak tenderness and calpainproteolytic activity. Meat Sci, 33 (2): 265-275, 1993. DOI: 10.1016/0309-1740(93)90064-O

31. Pringle TD, Harrelson JM, West RL,Williams SE, Johnson DD: Calcium-activated tenderization of strip loin, top sirloin, and top round steaks in diverse genotypes of cattle. J Anim Sci, 77 (12): 3230-3237, 1999. DOI: 10.2527/1999.77123230x

32. Cheng LI, Xie T, Gang FU, Dai-wen C: Correlation analysis among tenderness indexes during postmortem chilling aging of pork. Food Sci, 30 (17): 163-166, 2009.

33. Telci A, Çakatay U, Salman S, Satman I, Sivas A: Oxidative protein damage in early stage Type 1 diabetic patients. Diabet Res Clin Pract, 50 (3): 213-223, 2000. DOI: 10.1016/s0168-8227(00)00197-2

34. Grune T, Blasig IE, Sitte N, Roloff B, Haseloff R, Davies KJ: Peroxynitrite increases the degradation of aconitase and other cellular proteins by proteasome. J Biol Chem, 273 (18): 10857-10862, 1998.

35. Rowe LJ, Maddock KR, Lonergan SM, Huff-Lonergan E: Oxidative environments decrease tenderization of beef steaks through inactivation of μ-calpain. J Anim Sci, 82 (11): 3254-3266, 2004. DOI: 10.2527/ 2004.82113254x