Animal Bioscience

Asian Australasian Association of Animal Production Societies (아세아태평양축산학회)
권호 표지
DOI QR코드

DOI QR Code

Feeding strategies and ageing time alter calpain system proteins activities and meat quality of Braford steers

  • Coria, Maria Sumampa (Animal Production and Reproduction Laboratory, NOA Institute of Bionanotechnology (INBIONATEC)) ;
  • Pighin, Dario (National Council of Scientific and Technical Research (CONICET)) ;
  • Grigioni, Gabriela (National Council of Scientific and Technical Research (CONICET)) ;
  • Palma, Gustavo Adolfo (Animal Production and Reproduction Laboratory, NOA Institute of Bionanotechnology (INBIONATEC))
  • Received : 2021.05.14
  • Accepted : 2021.09.11
  • Published : 2022.02.01
Download PDF
⟨ Previous Next ⟩

Abstract

Objective: The aim of this study was to evaluate the effect of ageing and feeding strategies on the calpain protease system and meat quality traits in Braford steers. Methods: Thirty Braford steers were employed; 15 animals were supplemented with corn silage during finishing and 15 were kept only on pasture. Meat quality traits and calpain system protein activity were evaluated in longissimus thoracis et lumborum (LTL) steaks aged for 2, 7, 14, and 21 days. Results: Aged meat showed higher pH and calcium content, while Warner Bratzler shear force (WBSF) decreased to day 21. No interaction between ageing and diet was seen for quality traits. Steers finished with corn silage showed higher values of water holding capacity, WBSF and free calcium, and lower values of pH and cooking loss. Calpain and calpastatin activities decreased with ageing. Finishing steers on pasture produced higher values of calpains and lower values of calpastatin activities. The higher values of calpain 1 activity were observed in muscles aged 2 days from pasture finished animals, and the lower activity of the inhibitor in the 21 days aged samples of the same group. Conclusion: These results suggest a diet by ageing interaction in calpains and calpastatin and this interaction impact in Warner Bratzler Shear Force in Braford LTL muscle.

Keywords

Acknowledgement

The authors would like to acknowledge Mrs. Karina Moreno, PhD Sebastian Cunzolo and PhD. Eduardo A. Parellada for the technical assistance in determining the physical characteristics and biochemical composition of beef and to Eng. Horacio Coria and Mgs. Noemi Comba for their technical assistance in handling and shipping samples.

References

  1. Rearte D. Meat production in Argentina. Sitio Argentino Prod Animal; c2007 [cited 2021 Feb 26]. pp. 1-25. Available from: https://www.produccion-animal.com.ar
  2. Bidner TD, Wyatt WE, Humes PE, Franke DE, Blouin DC. Influence of Brahman-derivative breeds and Angus on carcass traits, physical composition, and palatability. J Anim Sci 2002;80:2126-33. https://doi.org/10.2527/2002.8082126x
  3. Pringle TD, Williams SE, Lamb BS, Johnson DD, West RL. Carcass characteristics, the calpain proteinase system, and aged tenderness of Angus and Brahman crossbred steers. J Anim Sci 1997;75:2955-61. https://doi.org/10.2527/1997.75112955x
  4. Colle MJ, Doumit ME. Effect of extended aging on calpain-1 and -2 activity in beef longissimus lumborum and semimembranosus muscles. Meat Sci 2017;131:142-5. https://doi.org/10.1016/j.meatsci.2017.05.014
  5. Coria MS, Carranza PG, Palma GA. Calpain system in meat tenderization: a molecular approach. Rev MVZ Cordoba 2018;23:6523-36. https://doi.org/10.21897/rmvz.1247
  6. Goll DE, Thompson VF, Li H, Wei W, Cong J. The calpain system. Physiol Rev 2003;83:731-801. https://doi.org/10.1152/physrev.00029.2002
  7. Koohmaraie M, Geesink GH. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Sci 2006;74:34-43. https://doi.org/10.1016/j.meatsci.2006.04.025
  8. Geesink GH, Kuchay S, Chishti AH, Koohmaraie M. µ-Calpain is essential for postmortem proteolysis of muscle proteins. J Anim Sci 2006;84:2834-40. https://doi.org/10.2527/jas.2006-122
  9. Giusti J, Castan E, Dal Pai M, Arrigoni MDB, Rodrigues Baldin S, De Oliveira HN. Expression of genes related to quality of Longissimus dorsi muscle meat in Nellore (Bos indicus) and Canchim (5/8 Bos taurus × 3/8 Bos indicus) cattle. Meat Sci 2013;94:247-52. https://doi.org/10.1016/j.meatsci.2013.02.006
  10. Strydom PE, Frylinck L, Montgomery JL, Smith MF. The comparison of three β-agonists for growth performance, carcass characteristics and meat quality of feedlot cattle. Meat Sci 2009;81:557-64. https://doi.org/10.1016/j.meatsci.2008.10.011
  11. Coria MS, Reineri PS, Pighin D, et al. Feeding strategies alter gene expression of the calpain system and meat quality in the longissimus muscle of Braford steers. Asian-Australas J Anim Sci 2020;33:753-62. https://doi.org/10.5713/ajas.19.0163
  12. Nishimura T. The role of intramuscular connective tissue in meat texture. Anim Sci J 2010;81:21-7. https://doi.org/10.1111/j.1740-0929.2009.00696.x
  13. Di Rienzo JA, Casanoves F, Balzarini MG, Gonzalez L, Tablada M, Robledo CW. InfoStat version 2012. Cordoba, Argentina: Grupo InfoStat, FCA, Universidad Nacional de Cordoba. Available from: http://www.infostat.com.ar
  14. Immonen K, Ruusunen M, Hissa K, Puolanne E. Bovine muscle glycogen concentration in relation to finishing diet, slaughter and ultimate pH. Meat Sci 2000;55:25-31. https://doi.org/10.1016/S0309-1740(99)00121-7
  15. Stanisic N, Petricevic M, Zivkovic D, et al. Changes of physical-chemical properties of beef during 14 days of chilling. Biotechnol Anim Husb 2012;28:77-85. https://doi.org/10.2298/BAH1201077S
  16. Wyrwisz J, Moczkowska M, Kurek M, Stelmasiak A, Poltorak A, Wierzbicka A. Influence of 21 days of vacuum-aging on color, bloom development, and WBSF of beef semimembranosus. Meat Sci 2016;122:48-54. https://doi.org/10.1016/j.meatsci.2016.07.018
  17. Beriain MJ, Goni MV, Indurain G, Sarries MV, Insausti K. Predicting Longissimus dorsi myoglobin oxidation in aged beef based on early post-mortem colour measurements on the carcass as a colour stability index. Meat Sci 2009;81:439-45. https://doi.org/10.1016/j.meatsci.2008.09.009
  18. Papaleo Mazzucco JP, Melucci LM, Villarreal EL, et al. Effect of ageing and µ-calpain markers on meat quality from Brangus steers finished on pasture. Meat Sci 2010;86:878-82. https://doi.org/10.1016/j.meatsci.2010.07.015
  19. Tullio RR, Juarez M, Larsen IL, Basarab JA, Aalhaus JL. Effect of quality parameters on beef meat tenderness. iComst-Proceedings; 2013. pp. 1-5.
  20. Marino R, Albenzio M, della Malva A, Caroprese M, Santillo A, Sevi A. Changes in meat quality traits and sarcoplasmic proteins during aging in three different cattle breeds. Meat Sci 2014;98:178-86. https://doi.org/10.1016/j.meatsci.2014.05.024
  21. Huff Lonergan E, Zhang W, Lonergan SM. Biochemistry of postmortem muscle - lessons on mechanisms of meat tenderization. Meat Sci 2010;86:184-95. https://doi.org/10.1016/j.meatsci.2010.05.004
  22. Huff-Lonergan E, Lonergan SM. Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes. Meat Sci 2005;71:194-204. https://doi.org/10.1016/j.meatsci.2005.04.022
  23. Parrish FC, Selvig CJ, Culler RD, Zeece MG. CAF activity, calcium concentration, and the 30,000-Dalton component of tough and tender bovine longissimus muscle. J Food Sci 1981;46:308-11. https://doi.org/10.1111/j.1365-2621.1981.tb14593.x
  24. Senaratne LS. Mechanism and control of beef toughening during retail display in high oxygen modified atmosphere packages [Theses and Dissertations]. Lincoln, NE, USA: Animal Science, Univ Nebraska-Lincoln; 2012. https://digitalcommons.unl.edu/animalscidiss/54
  25. Silva JA, Patarata L, Martins C. Influence of ultimate pH on bovine meat tenderness during ageing. Meat Sci 1999;52:453-9. https://doi.org/10.1016/S0309-1740(99)00029-7
  26. Palka K. The influence of post-mortem ageing and roasting on the microstructure, texture and collagen solubility of bovine semitendinosus muscle. Meat Sci 2003;64:191-8. https://doi.org/0.1016/s0309-1740(02)00179-1 https://doi.org/10.1016/s0309-1740(02)00179-1
  27. Christensen M, Ertbjerg P, Failla S, et al. Relationship between collagen characteristics, lipid content and raw and cooked texture of meat from young bulls of fifteen European breeds. Meat Sci 2011;87:61-5. https://doi.org/10.1016/j.meatsci.2010.09.003
  28. Teira G, Perlo F, Bonato P, et al. Finishing phase and meat quality. 2. Tenderness. Rev Argentina Prod Anim 2004;24(suppl 1).
  29. del Campo M, Brito G, de Lima JMS, et al. Effects of feeding strategies including different proportion of pasture and concentrate, on carcass and meat quality traits in Uruguayan steers. Meat Sci 2008;80:753-60. https://doi.org/10.1016/j.meatsci.2008.03.026
  30. del Campo M, Brito G, Soares de Lima J, Hernandez P, Montossi F. Finishing diet, temperament and lairage time effects on carcass and meat quality traits in steers. Meat Sci 2010;86:908-14. https://doi.org/10.1016/j.meatsci.2010.07.014
  31. Latimori NJ, Kloster AM, Garcia PT, Carduza FJ, Grigioni G, Pensel NA. Diet and genotype effects on the quality index of beef produced in the Argentine Pampeana region. Meat Sci 2008;79:463-9. https://doi.org/10.1016/j.meatsci.2007.10.008
  32. Faucitano L, Berthiaume R, D'Amours M, Pellerin D, Ouellet DR. Effects of corn grain particle size and treated soybean meal on carcass and meat quality characteristics of beef steers finished on a corn silage diet. Meat Sci 2011;88:750-4. https://doi.org/10.1016/j.meatsci.2011.03.008
  33. He L, Wu H, Wang G, Meng Q, Zhou Z. The effects of including corn silage, corn stalk silage, and corn grain in finishing ration of beef steers on meat quality and oxidative stability. Meat Sci 2018;139:142-8. https://doi.org/10.1016/j.meatsci.2018.01.023
  34. Mandell IB, Buchanan-Smith JG, Campbell CP. Effects of forage vs grain feeding on carcass characteristics, fatty acid composition, and beef quality in Limousin-Cross Steers when time on feed is controlled. J Anim Sci 1998;76:2619-30. https://doi.org/10.2527/1998.76102619x
  35. Vestergaard M, Therkildsen M, Henckel P, Jensen LR, Andersen HR, Sejrsen K. Influence of feeding intensity, grazing and finishing feeding on meat and eating quality of young bulls and the relationship between muscle fibre characteristics, fibre fragmentation and meat tenderness. Meat Sci 2000;54:187-95. https://doi.org/10.1016/s0309-1740(99)00098-4
  36. Purslow PP, Oiseth S, Hughes J, Warnerd RD, Warner RD. The structural basis of cooking loss in beef: Variations with temperature and ageing. Food Res Int 2016;89:739-48. https://doi.org/10.1016/j.foodres.2016.09.010
  37. Orellana C, Pena F, Garcia A, et al. Carcass characteristics, fatty acid composition, and meat quality of Criollo Argentino and Braford steers raised on forage in a semi-tropical region of Argentina. Meat Sci 2009;81:57-64. https://doi.org/10.1016/j.meatsci.2008.06.015
  38. Lagerstedt A, Enfalt L, Johansson L, Lundstrom K. Effect of freezing on sensory quality, shear force and water loss in beef m. longissimus dorsi. Meat Sci 2008;80:457-61. https://doi.org/10.1016/j.meatsci.2008.01.009
  39. Chao M. Impact of wet distillers grains plus solubles and antioxidants on a basic mechanism of beef tenderization [Theses and Dissertations]. Lincoln NE, USA: Animal Science, University of Nebraska; 2015. http://digitalcommons.unl.edu/animalscidiss/105
  40. Korn KT, Lemenager RP, Claeys MC, Waddell JN, Engstrom M, Schoonmaker JP. Supplemental vitamin D3 and zilpaterol hydrochloride. II. Effect on calcium concentration, muscle fiber type, and calpain gene expression of feedlot steers. J Anim Sci 2013;91:3332-40. https://doi.org/10.2527/jas.2012-5962
  41. Destefanis G, Brugiapaglia A, Barge MT, Dal Molin E. Relationship between beef consumer tenderness perception and Warner-Bratzler shear force. Meat Sci 2008;78:153-6. https://doi.org/10.1016/j.meatsci.2007.05.031
  42. Latimori N, Kloster AM, Amigone MA, Garcia PT, Carduza FJ, Pensel NA. Beef quality according to genotye and feeding system. Rev Argentina Prod Anim 2005; 25(Suppl. 1):365-7.
  43. Realini CE, Duckett SK, Brito GW, Dalla Rizza M, De Mattos D. Effect of pasture vs. concentrate feeding with or without antioxidants on carcass characteristics, fatty acid composition, and quality of Uruguayan beef. Meat Sci 2004;66:567-77. https://doi.org/10.1016/S0309-1740(03)00160-8
  44. Moran L, O'Sullivan MG, Kerry JP, et al. Effect of a grazing period prior to finishing on a high concentrate diet on meat quality from bulls and steers. Meat Sci 2017;125:76-83. https://doi.org/10.1016/j.meatsci.2016.11.021
  45. Koohmaraie M. Quantification of Ca2(+)-dependent protease activities by hydrophobic and ion-exchange chromatography. J Anim Sci 1990;68:659-65. https://doi.org/10.2527/1990.683659x
  46. Ilian MA, Morton JD, Kent MP, et al. Intermuscular variation in tenderness: Association with the ubiquitous and muscle-specific calpains. J Anim Sci 2001;79:122-32. https://doi.org/10.2527/2001.791122x
  47. Pomponio L, Ertbjerg P. The effect of temperature on the activity of µ - and m-calpain and calpastatin during post-mortem storage of porcine longissimus muscle. Meat Sci 2012;91:50-5. https://doi.org/10.1016/j.meatsci.2011.12.005
  48. Kristensen L, Christensen M, Ertbjerg P. Activities of calpastatin, µ -calpain and m-calpain are stable during frozen storage of meat. Meat Sci 2006;72:116-20. https://doi.org/10.1016/j.meatsci.2005.06.010
  49. Volpelli LA, Failla S, Sepulcri A, Piasentier E. Calpain system in vitro activity and myofibril fragmentation index in fallow deer (Dama dama): Effects of age and supplementary feeding. Meat Sci 2005;69:579-82. https://doi.org/10.1016/j.meatsci.2004.09.009
  50. Kristensen L, Therkildsen M, Riis B, et al. Dietary-induced changes of muscle growth rate in pigs: Effects on in vivo and postmortem muscle proteolysis and meat quality. J Anim Sci 2002;80:2862-71. https://doi.org/10.2527/2002.80112862x
  51. Dransfield E. Optimisation of tenderisation, ageing and tenderness. Meat Sci 1994;36:105-21. https://doi.org/10.1016/0309-1740(94)90037-X