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Stefan Georgiev Dragoev Dessislava Vlahova-Vangelova Dessislav Balev Aydun Igenbaev Samat Kassimov

Abstract

The objective of this study was to recognize the specificity of microstructural changes of DFD sheep m. Longissimus dorsi during its ripening, and to try to explain them by biochemical and physicochemical amendments of meat. The fresh (4 h post mortem) DFD sheep m. Longissimus dorsi with pH1 = 6.95 stored at 2 ± 2°C was used. The microstructure, degree of proteolysis, color properties, water holding capacity and pH of DFD sheep meat were evaluated during 5d of storage. The shortenings of the sarcomeres and typical alternation of light and dark bands were established after 48h storage of DFD sheep muscles. Simultaneously, pH and water holding capacity decreased with 16.5% and 50.6% resp. (p ≤ 0.05), accompanied with the lowest protein solubility, and a disappearance of myosin heavy chains. On the 3d post mortem sarcomeres were partly regenerated and their native structure was recovered, A- and I-disks were visible, and Z-lines were undamaged. On the 4d post mortem was found large gap formation in sarcomeres and difficulty recognizable A- and I-disks. On the 5d post mortem the pH and water holding capacity were similar (p > 0.05) with the initial values but free amino nitrogen decreased with 34.5%.

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References

Bertram H.C., Purslow P.P., Andersen H.J. Relationship between meat structure, water mobility and distribution: A low field nuclear magnetic resonance study. Journal of Agriculture and Food Chemistry, 2002, 50(4): 824-829. http://dx.doi.org/10.1021/jf010738f

Bond J.J., Warner R.D. Ion distribution and protein proteolysis affect water holding capacity of Longissimus thoracis et lumborum in meat of lamb subjected to ante mortem exercise. Meat Science, 2007, 75(3): 406-414. http://dx.doi.org/10.1016/j.meatsci.2006.08.005

Braggins T.J. Effect of stress-related changes in sheep meat ultimate pH on cooked odor and flavor. Journal of Agriculture and Food Chemistry, 1996, 44(8): 2352-2360. http://dx.doi.org/10.1021/jf960136+

Bouton P.E., Carroll F.D., Fisher A.L., Harris P.V., Shorthose W.R. Effect of altering ultimate pH on bovine muscle tenderness. Journal of Food Science, 1973, 38(5): 816-820. https://doi.org/10.1111/j.1365-2621.1973.tb02083.x

Bouton P.E., Harris P.V., Shorthose W.R. Effect of ultimate pH upon the water holding capacity and tenderness of mutton. Journal of Food Science, 1971, 36(3): 435-439. https://doi.org/10.1111/j.1365-2621.1971.tb06382.x

Chen L., Feng X.C., Lu F., Xu X.L., Zhou G.H., Li, Q.Y., Guo X.Y. Effects of camptothecin, etoposide and Ca2+ on caspase-3 activity and myofibrillar disruption of chicken during post mortem ageing. Meat Science, 2011, 87(3): 165-174. http://dx.doi.org/10.1016/j.meatsci.2010.10.002

Damez, J.L., Clerjon S. Meat quality assessment using biophysical methods related to meat structure. Review. Meat Science, 2008, 80(1): 132-149. http://dx.doi.org/10.1016/j.meatsci.2008.05.039

Dransfield E. Eating Quality of DFD Beef. In: The Problem of Dark-Cutting in Beef. Current Topics in Veterinary Medicine and Animal Science (Hood D.E., Tarrant P.V. Eds.). Volume 10, Springer, Dordrecht. 1981, рр. 344-361, Print ISBN: 978-94-009-8324-3, Online ISBN: 978-94-009-8322-9. https://doi.org/10.1007/978-94-009-8322-9

Farouk M.M., Price J.F., Salih A.M. Post-exsanguination infusion of ovine carcasses: effect on tenderness indicators and muscle microstructure. Journal of Food Science, 1992, 57(6): 1311-1315. http://dx.doi.org/10.1111/j.1365-2621.1992.tb06844.x

Ferguson D.M., Warner R.D. Have we underestimated the impact of pre-slaughter stress on meat quality in ruminants? Review. Meat Science, 2008, 80(1): 12-19. https://doi.org/10.1016/j.meatsci.2008.05.004

Fritz J.D., Swartz D.R., Greaser M.L. Factors affecting polyacrylamide gel electrophoresis and electroblotting of high-molecular-weight myofibrillar proteins myofibrillar proteins. Analytical Biochemistry, 1989, 180(2): 205-210. https://doi.org/10.1016/0003-2697(89)90116-4

Geay Y., Bauchart D., Hocquette J.F., Culioli J. Effect of nutri-tional factors on biochemical, structural and metabolic character-ristics of muscles in ruminants, consequences on dietetic value and sensorial qualities of meat. Reproduction Nutrition Development, 2001, 41(1): 1-26. http://dx.doi.org/10.1051/rnd:2001101

Hopkins D.L., Thompson J.M. Factors contributing to proteolysis and disruption of myofibrillar proteins and the impact on tenderisation in beef and sheep meat. Australian Journal of Agricultural Research 2002.53(2): 149-166. https://doi.org/10.1071/AR01079

Huff-Lonergan E., Lonergan S.M. Postmortem Mechanisms of Meat Tenderisation: The Role of Structural Proteins and the Calpain System. In: Quality Attributes of Muscle Foods (Xiong, Y.L., Ho, C.-T., Shahidi F. Eds). New York: Kluwert Academics/Plenum Publishers. 1999, pp. 229-251, eBook ISBN 978-1-4615-4731-0_16 http://www.springer.com/la/book/9780306461163

Huff-Lonergan E., Lonergan S.M. Mechanisms of water holding capacity of meat: The role of postmortem biochemical and struc-tural changes. Meat Science 2005. 71(1): 194-204. http://dx.doi.org/10.1016/j.meatsci.2005.04.022

Hunt M., King A., Barbut Sh., Claus J., Cornforth, D., Hanson D. Section VIII. Guidelines, Instrumental Meat Colour Measurement. In: AMSA Meat Colour Measurement Guidelines (M. Hunt, A. King Eds.). Champaign: American Meat Science Association. 2012, pp. 45-52. https://www.meatscience.org/docs/default-source/publications-resources/Hot-Topics/2012_12_meat_clr_guide.pdf?sfvrsn=d818b8b3_0

Hwang I.H., Devine C.E., Hopkins D.L. The biochemical and physical effects of electrical stimulation on beef and sheep meat tenderness. Review. Meat Science, 2003, 65(2): 677-691. http://dx.doi.org/10.1016/S0309-1740(02)00271-1

Khan, A. Extraction and fractionation of proteins in fresh chicken muscle. Journal of Food Science, 1962, 27(5): 430-434. http://dx.doi.org/10.1111/j.1365-2621.1962.tb00122.x

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 Science, 2003, 64(1): 77-83. https://doi.org/10.1016/S0309-1740(02)00164-X

Koohmaraie, M. Muscle proteinases and meat aging. Meat Science, 1994, 36(1-2): 93-104. https://doi.org/10.1016/0309-1740(94)90036-1

Koohmaraie T.M., Darrel E. Is Z-Disk degradation responsible for post mortem tenderization? Journal of Animal Science, 1995, 73(5): 1351-1367. http://dx.doi.org/10.2527/1995.7351351x

Lorenzo J.M., Garcı´a Fontán M.C., Franco I., Carballo J. Proteolytic and lipolytic modifications during the manufacture of dry-cured lacón, a Spanish traditional meat product: effect of some additives. Food Chemistry, 2008, 100(1): 137-149. http://dx.doi.org/10.1016/j.foodchem.2008.02.002

Lowry O., Rosebrough N., Farr A., Randall R. Protein measurement with the folin phenol reagent. The Journal of Biological Chemistry, 1951, 193(1): 265-275. http://www.jbc.org/content/193/1/265.full.pdf

Miranda-de la Lama G.C., Villarroel M., Olleta J.L., Alierta S., Sañudo C., Maria G.A. Effect of the pre-slaughter logistic chain on meat quality of lambs. Meat Science, 2009, 83(4): 604-609. https://doi.org/10.1016/j.meatsci.2009.07.009

Modzelewska-Kapitula M., Cierach M. Effect of pressure and sample weight on free water content in beef estimated according to Grau-Hamm method using computer image analysis. Science Nature Technologies, 2009, 3(4): 144. https://pbn.nauka.gov.pl/polindex-webapp/browse/article/article-c2833508-1dd2-48c2-b92a -41b3f3be3a19

Nagaraj N.S., Anilakumar K.R., Santhanam K. Post mortem changes in myofibrillar proteins of goat skeletal muscles. Journal of Food Biochemistry, 2005, 29(2): 152-170. http://dx.doi.org/10.1111/j.1745-4514.2005.00011.x

Newton K.G., Gill C.O. Storage quality of dark, firm, dry meat. Applied and Environmental Microbiology, 1978, 36(2): 375-376. http://aem.asm.org/content/36/2/375.full.pdf+html

Okeudo N.J., Moss B.W. Interrelationships amongst carcass and meat quality characteristics of sheep. Meat Science, 2005, 69(1): 1-8. http://dx.doi.org/10.1016/j.meatsci.2004.04.011

Pearce K.L., Rosenvold K., Andersen H.J., Hopkins D. L. Water distribution and mobility in meat during the conversion of muscle to meat and ageing and the impacts on fresh meat quality attributes - A review. Meat Science, 2011, 89(2): 111-124. http://dx.doi.org/10.1016/j.meatsci.2011.04.007

Polidori P., Marinucci M.T., Fantuz F., Renieri C. Polidori F. Tenderization of weather lambs meat through pre-rigor infusion of calcium ions. Meat Science, 2000, 55(2): 197-200. https://doi.org/10.1016/S0309-1740(99)00143-6

SAS/STAT user’s guide. v.6. vol.1. 4th Edn. Cary, NC, USA, SAS Institute, Inc. 1990. ISBN-10 1555443761, ISBN-13 978-1555443764. https://www.amazon.com/Users-Guide-Version-Fourth-Volumes/dp/1555443761

Shimokomaki M., Ida E.I., Kato T., Pedrão M.R., Coró F.A.G. Hernández-Blazquez F.J. Vol. 1, Meat and Meat Products Microstructure and their Eating Quality. In: Current Microscopy Contributions to Advances in Science and Technology (A. Méndez-Vilas Ed.). Formatex Research Center. Badajoz. 2012, pp. 486-495. ISBN 13: 978-84-939843-5-9 http://www.formatex.info/microscopy5/book/486-495.pdf

Veiseth E., Shackelford S.D., Wheeler T.L. Koohmaraie M. Factors regulating lamb longissimus tenderness are affected by age at slaughter. Meat Science, 2004, 68(4): 635-640. http://dx.doi.org/10.1016/j.meatsci.2004.05.015

Vieira C., Cerdeño A., Seffano E., Lavín P., Mantecón A.R. Breed and ageing extent on carcass and meat quality of beef from adult steers (oxen). Livestock Science, 2007, 107(1): 62-69. https://doi.org/10.1016/j.livsci.2006.09.004

Young O.A., West J., Hart A.L., Van Otterdijk F.F.H. A method for early determination of meat ultimate pH. Meat Science, 2004, 66(1): 493-498. http://dx.doi.org/10.1016/S0309-1740(03)00140-2

How to Cite
DRAGOEV, Stefan Georgiev et al. A specificity of microstructural and biochemical changes during ripening of dark, firm and dry sheep meat. Food Science and Applied Biotechnology, [S.l.], v. 1, n. 2, p. 140-147, oct. 2018. ISSN 2603-3380. Available at: <https://www.ijfsab.com/index.php/fsab/article/view/38>. Date accessed: 03 dec. 2024. doi: https://doi.org/10.30721/fsab2018.v1.i2.38.