Influence of calpain on lamb myofibrillar proteins degradation during in vitro culture

https://doi.org/10.17221/423/2017-CJFSCitation:Ablikim B., Muhtar M., Ma Y.Q., Abduwali A., Sulayman Y. (2018): Influence of calpain on lamb myofibrillar proteins degradation during in vitro culture. Czech J. Food Sci., 36: 296-300.
download PDF

Tenderness is an important indicator of meat quality, degradation plays important role during the maturation, therefore improving meat quality and tenderness. Understanding the process of myofibrillar and which enzymes affect degradation is more needed to prove. In this study we used longest muscle of Bashibai sheep of Xinjiang as the experiment material. The isolated myofibrillar protein and μ-calpains are incubated at 4°C about 1, 3, 7, 14, and 21 days using in vitro culture method and analysed by SDS-PAGE, Western blotting. Results showed that μ-calpain can improve the degradation of some myofibrillar proteins. Desmin was degraded by the 3rd, troponin–T was completely degraded by the 7th day.

References:
Anderson M.J., Lonergan S.M., Fedler C.A., Prusa K.J., Binning J.M., Huff-Lonergan E. (2012): Profile of biochemical traits influencing tenderness of muscles from the beef round. Meat Science, 91, 247-254 https://doi.org/10.1016/j.meatsci.2012.01.022
 
Costelli P., Reffo P., Penna F., Autelli R., Bonelli G., Baccino F.M. (2005): Ca2+-dependent proteolysis in muscle wasting. International Journal of Biochemistry & Cell Biology, 37: 2134–2146.
 
Cruzen Shannon M., Paulino Pedro V.R., Lonergan Steven M., Huff-Lonergan Elisabeth (2014): Postmortem proteolysis in three muscles from growing and mature beef cattle. Meat Science, 96, 854-861 https://doi.org/10.1016/j.meatsci.2013.09.021
 
Davey C.L., Kuttel H., Gilbert K.V. (1967): Shortening as a factor in meat ageing. International Journal of Food Science & Technology, 2: 53–56.
 
Devine Carrick E, Payne Steven R, Wells Robyn W (2002): Effect of muscle restraint on sheep meat tenderness with rigor mortis at 18°C. Meat Science, 60, 155-159 https://doi.org/10.1016/S0309-1740(01)00117-6
 
Etlinger J. D. (1976): Compositional studies of myofibrils from rabbit striated muscle. The Journal of Cell Biology, 68, 123-141 https://doi.org/10.1083/jcb.68.1.123
 
GOLL DARREL E., THOMPSON VALERY F., LI HONGQI, WEI WEI, CONG JINYANG (2003): The Calpain System. Physiological Reviews, 83, 731-801 https://doi.org/10.1152/physrev.00029.2002
 
HERRING H. K., CASSENS R. G., SUESS G. G., BRUNGARDT V. H., BRISKEY E. J. (1967): Tenderness and Associated Characteristics of Stretched and Contracted Bovine Muscles. Journal of Food Science, 32, 317-323 https://doi.org/10.1111/j.1365-2621.1967.tb01321_32_3.x
 
HOPKINS D.L., THOMPSON J. M. (2002): THE DEGRADATION OF MYOFIBRILLAR PROTEINS IN BEEF AND LAMB USING DENATURING ELECTROPHORESIS - AN OVERVIEW. Journal of Muscle Foods, 13, 81-102 https://doi.org/10.1111/j.1745-4573.2002.tb00323.x
 
Huang M., Zhao L., Xu X., Zhou G. (2004): Effects of calcium ion and exogenous calpains inhibitors on calpains activity and ultrastructure of beef. Journal of Nanjing Agricultural University, 27: 101–104.
 
Harris S E, Huff-Lonergan E, Lonergan S M, Jones W R, Rankins D (2001): Antioxidant status affects color stability and tenderness of calcium chloride-injected beef.. Journal of Animal Science, 79, 666- https://doi.org/10.2527/2001.793666x
 
Koohmaraie M., Geesink G.H. (2006): Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Science, 74, 34-43 https://doi.org/10.1016/j.meatsci.2006.04.025
 
Koohmaraie Mohammad (1996): Biochemical factors regulating the toughening and tenderization processes of meat. Meat Science, 43, 193-201 https://doi.org/10.1016/0309-1740(96)00065-4
 
Kemp Caroline M., Parr Tim (2012): Advances in apoptotic mediated proteolysis in meat tenderisation. Meat Science, 92, 252-259 https://doi.org/10.1016/j.meatsci.2012.03.013
 
Kristensen Lars, Purslow Peter P. (2001): The effect of ageing on the water-holding capacity of pork: role of cytoskeletal proteins. Meat Science, 58, 17-23 https://doi.org/10.1016/S0309-1740(00)00125-X
 
LOCKER R. H. (1960): DEGREE OF MUSCULAR CONTRACTION AS A FACTOR IN TENDERNESS OF BEEF. Journal of Food Science, 25, 304-307 https://doi.org/10.1111/j.1365-2621.1960.tb00335.x
 
Huff Lonergan Elisabeth, Zhang Wangang, Lonergan Steven M. (2010): Biochemistry of postmortem muscle — Lessons on mechanisms of meat tenderization. Meat Science, 86, 184-195 https://doi.org/10.1016/j.meatsci.2010.05.004
 
Li Zheng, Li Xin, Gao Xing, Shen Qingwu W., Du Manting, Zhang Dequan (2017): Phosphorylation prevents in vitro myofibrillar proteins degradation by μ-calpain. Food Chemistry, 218, 455-462 https://doi.org/10.1016/j.foodchem.2016.09.048
 
Maltin Charlotte, Balcerzak Denis, Tilley Rachel, Delday Margaret (2003): Determinants of meat quality: tenderness. Proceedings of the Nutrition Society, 62, 337-347 https://doi.org/10.1079/PNS2003248
 
Marino R., della Malva A., Albenzio M. (2015): Proteolytic changes of myofibrillar proteins in Podolian meat during aging: focusing on tenderness. Journal of Animal Science, 93, 1376- https://doi.org/10.2527/jas.2014-8351
 
Macfarlane J.J., Harris P.V., Shorthose W.R. (1974): Manipulation of meat quality, particularly tenderness, by the processor. Animal products, 10: 219–226.
 
Muroya Susumu, Ertbjerg Per, Pomponio Luigi, Christensen Mette (2010): Desmin and troponin T are degraded faster in type IIb muscle fibers than in type I fibers during postmortem aging of porcine muscle. Meat Science, 86, 764-769 https://doi.org/10.1016/j.meatsci.2010.06.019
 
Nollet L.M.L., Toldrá F. (2006): Advanced Technologies for Meat Processing. CRC Press, Taylor & Francis. - PAGES?
 
Pereira Paula Manuela de Castro Cardoso, Vicente Ana Filipa dos Reis Baltazar (2013): Meat nutritional composition and nutritive role in the human diet. Meat Science, 93, 586-592 https://doi.org/10.1016/j.meatsci.2012.09.018
 
PAULIN D, LI Z (2004): Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle. Experimental Cell Research, 301, 1-7 https://doi.org/10.1016/j.yexcr.2004.08.004
 
Ristic M., Miscevic B. (2012): Survey of the tenderness of meat of beef, pork poultry and rabbit – a comparison. Fleischwirtschaft Frankfurt, 92: 100–104.
 
Smuder A.J., Kavazis A.N., Hudson M.B., Nelson W.B., Powers S.K. (2010): Oxidation enhances myofibrillar protein degradation via calpain and caspase-3. Free Radical Biology & Medicine, 49: 1152–1160.
 
Taylor R.G., Geesink G.H., Thompson V.F., Koohmaraie M., Goll D.E. (1995): Is z-disk degradation responsible for postmortem tenderization? Journal of Animal Science, 73: 1351–1367.
 
TAKAHASHI Koui (1999): Tenderization Mechanism of Meat during Post-mortem Aging: The Calcium Theory of Meat Tenderization. Nihon Chikusan Gakkaiho, 70, 1-11 https://doi.org/10.2508/chikusan.70.1
 
Xue M., Huang J.C., Qian Z., Huang M., Zhou G.H. (2012): Effects of μ-calpain oxidation on bovine myofibrillar proteins degradation in vitro. Journal of Nanjing Agricultural University, 35: 121–125.
 
download PDF

© 2018 Czech Academy of Agricultural Sciences