In recent years, consumers have increasingly sought niche food products with specific aroma and flavour, and rich in nutrients. With a growing demand for quality poultry products, there is an opportunity to increase production of capons, which are more and more often marketed as high quality products, because their meat is more delicate, tender and juicy. Therefore the objective of this study was to compare meat quality parameters and rate of protein degradation between capon and cockerel breast muscle during postmortem aging. Fibre type diameter, intact desmin and dystrophin contents at 15 min, 24 h, and 48 h postmortem and the following technological parameters of breast meat were also determined: pH15, pH24, pH48, drip loss, shear force. The study was carried out on hybrids between Rhode Island Red cockerels (R-11) and Yellowleg Partridge hens (Ż-33) aged 24 weeks. The current findings indicate that compared with cockerel breast muscles, the capon breast muscles had significantly higher pH15 (P≤0.01), and lower drip loss (P≤0.01) and shear force values (P≤0.05). Additionally, the intensity of intact desmin and dystrophin in capon breast samples at 24 h and 48 h postmortem was significantly lower (P≤0.05) than that in the cockerel breast sample. In turn, the lower rate of desmin and dystrophin degradation (P≤0.05), along with higher drip loss in cockerel compared to capon breast muscles, may account for their lower muscle fibre diameters at 24 h and 48 h postmortem. Moreover, the rate of early postmortem pH decline can partly explain the variation of desmin and dystrophin degradation.
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Adamski M., Kuźniacka J., Banaszak M., Wegner M. (2016). The analysis of meat traits of Sussex cockerels and capons (S11) at different ages. Poultry Sci., 95: 125–132.
Bee G., Anderson A.L., Lonergan S.M., Huff-Lonergan E. (2007). Rate and extent of pH decline affect proteolysis of cytoskeletal proteins and water-holding capacity in pork. Meat Sci., 76: 359–365.
Calik J., Połtowicz K., Świątkiewicz S., Krawczyk J., Nowak J. (2015). Effect of caponization on meat quality of Greenleg Partridge cockerels. Ann. Anim. Sci., 15: 541–553.
Chang Y.-S., Chou R.-G.R. (2010). Postmortem degradation of desmin and calpain in breast and leg and thigh muscles from Taiwan black-feathered country chickens. J. Sci. Food Agric., 90: 2664–2668.
Chang Y.-S., Chou R.-G.R. (2012). Postmortem role of calpains in Pekin duck skeletal muscles. J. Sci. Food Agric., 92: 1620–1626.
Chen K.L., Hsieh T.Y., Chiou P.W.S. (2006). Caponization effects on growth performance and lipid metabolism in Taiwan country chicken cockerels. Asian-Austral. J. Anim. Sci., 19: 438–443.
Chen K.L. Chen T.T., Lin K.J., Chiou P.W.S. (2007). The effect of caponization age on muscle characteristics in male chicken. Asian-Austral. J. Anim. Sci., 20: 1684–1688.
Dolatowski Z. J., Twarda J., Dudek M. (2004). Changes in hydration of meat during the ageing process (in Polish). Annales UMCS, 59: 1595–1606.
Franco D., Pateiro M., Rois D., Vázquez J.A., Lorenzo J.M. (2016). Effects of caponization on growth performance, carcass and meat quality of Mos breed capons reared in free-range production system. Ann. Anim. Sci., 16: 909–929.
Gesek M., Zawadzka M., Murawska D. (2017). Effects of caponization and age on the histology, lipid localization, and fiber diameter in muscles from Greenleg Partridge cockerels. Poultry Sci., 96: 1759–1766.
Goll D.E., Kleese W.C., Okitani A., Kumamoto T., Cong J., Kapprell H-P. (1990). Historical background and current status of the Ca2+-dependent proteinase system. In: Intracellular Calcium-Dependent Proteolysis, Mellgren R.L. Murachi T. (eds). Boca Raton, FL: CRC, pp. 3–24.
Huff-Lonergan E., Lonergan S.M. (2005). Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes. Meat Sci., 71: 194–204.
Huff-Lonergan E., Baas T.J., Malek M., Dekkers J.C.M., Prusa K., Rothschild M.F. (2002). Correlations among selected pork quality traits. J. Anim. Sci., 80: 2–10.
Huff-Lonergan E., Zhang W., Lonergan S.M. (2010). Biochemistry of postmortem muscle – lessons on mechanisms of meat tenderization. Meat Sci., 86: 184–195.
Hughes J.M., Oiseth S.K., Purslow P.P., Warner R.D. (2014). A structural approach to understanding the interactions between colour, water-holding capacity and tenderness. Meat Sci., 98: 520–532.
Johnson G.V., Guttmann R.P. (1997). Calpains: intact and active? Bioessays, 19: 1011–1018.
Koohmaraie M. (1992). Effect of pH, temperature, and inhibitors on autolysis and catalytic activity of bovine skeletal muscle μ-calpain. J. Anim. Sci., 70: 3071–3080.
Koohmaraie M. (1994). Muscle proteinases and meat aging. Meat Sci., 36: 93–104.
Kristensen L., Purslow P.P. (2001). The effect of ageing on water holding capacity of pork: the role of cytoskeletal proteins. Meat Sci., 58: 17–23.
Kwiecień M., Kasperek K., Tomaszewska E., Muszyński S., Jeżewska-|-Witkowska G., Winiarska-Mieczan A., Grela E.R., Kamińska E. (2018). Effect of breed and caponisation on the growth performance, carcass composition, and fatty acid profile in the muscles of Greenleg Partridge and Polbar breeds. Braz. J. Poultry Sci., 20: 583–594.
Lee H.L., Santé-Lhoutellier V., Vigouroux S., Briand Y., Briand M. (2008). Role of calpains in postmortem proteolysis in chicken muscle. Poultry Sci., 87: 2126–2132.
Maddock K.R., Huff-Lonergan E.J., Rowe L.J., Lonergan S.M. (2005). Effect of pH and ionic strength on μ- and m-calpain inhibition by calpastatin. J. Anim. Sci., 83: 1370–1376.
Melody J.L., Lonergan S.M., Rowe L.J., Huiatt T.W., Mayes M.S., Huff-Lonergan E. (2004). Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles. J. Anim. Sci., 82: 1195–1205.
Minetti C., Beltrame F., Marcenaro G., Bonilla E. (1992). Dystrophin at the plasma membrane of human muscle fibers shows a costameric localization. J. Clin. Neuromuscul. Dis., 2: 99–109.
Morrison H.E., Mielche M.M., Purlsow P.P. (1998). Immunolocalisation of intermediate filament proteins in porcine meat. Fibre type and muscle-specific variations during conditioning. Meat Sci., 50: 91–104.
Offer G., Cousins T. (1992). The mechanism of drip production: formation of two compartments of extracellular space in muscle post mortem. J. Sci. Food Agr., 58: 107–116.
Ouali A. (1992). Proteolytic and physicochemical mechanisms involved in meat texture development. Biochimie, 74: 251–265.
Shackelford S.D., Wheeler T.L., Meade M.K., Reagan J.O., Byrnes B.L., Koohmaraie M. (2001). Consumer impressions of tender select beef. J. Anim Sci., 79: 2605–2614.
Shao Y., Wu C., Li J., Zhao C. (2009). The effect of different caponization age on growth performance and blood parameters in male Tibetan chicken. Asian J. Anim. Sci., 4: 228–236.
Sinanoglou V.J., Mantis F., Miniadis-Meimaroglous S., Symeon G.K., Bizelis I.A. (2011). Effects of caponisation on lipid and fatty acid composition of intramuscular and abdominal fat of medium-growth broilers. Br. Poultry Sci., 52: 310–317.
Soglia F., Zeng Z., Gao J., Cavani C., Petracci M., Ertbjerg P. (2018). Evolution of proteolytic indicators during storage of broiler wooden breast meat. Poultry Sci., 97: 1448–1455.
Sorimachi H., Tsukahara T., Okada-Ban M., Sugita H., Ishiura S., Suzuki K. (1995). Identification of third ubiquitous calpain species – chicken muscle expresses four distinct calpains. Biochim. Biophys. Acta, 1261: 381–393.
Taylor R.G., Geesink G.H., Thompson V.F., Koohmaraie M., Goll D.E. (1995). Is Z-disk degradation responsible for postmortem tenderization? J. Anim. Sci., 73: 1351–1367.
Therkildsen M., Melchior Larsen L., Bang H.G., Vestergaard M. (2002). Effect of growth rate on tenderness development and final tenderness of meat from Friesian calves. J. Anim. Sci., 74: 253–264.
Tor M., Estany J., Villalba D., Molina E., Cubilò M.D. (2002). Comparison of carcass composition by parts and tissues between cocks and capons. Anim. Res., 51: 421–443.
Tor M., Estany J., Francesch D.A., Cubilò M.D. (2005). Comparison of fatty acid profiles of edible meat, adipose tissues and muscles between cocks and capons. Anim. Res., 54: 413–424.
Wojtysiak D., Górska M. (2018). Effect of aging time on meat quality and rate of desmin and dystrophin degradation of pale, soft, exudative (PSE) and normal turkey breast muscle. Folia Biol. (Krakow), 66: 63–72.
Wojtysiak D., Połtowicz K. (2015). Effect of ageing time on microstructure, rate of desmin degradation and meat quality of pig longissimus lumborum and adductor muscles. Folia Biol. (Krakow), 63: 151–158.
Wojtysiak D., Połtowicz K., Karasiński J. (2008). Relationship between post mortem desmin degradation and meat quality of poultry breast muscle. Med. Weter., 64: 1003–1006.
Young O.A., Graafhuis A.E., Davey C.L. (1980). Post-mortem changes in cytoskeletal proteins of muscle. Meat Sci., 5: 41–55.
Zhang W.G., Lonergan S.M., Gardner M.A., Huff-Lonergan E. (2006). Contribution of postmortem changes of integrin, desmin and μ-calpain to variation in water holding capacity of pork. Meat Sci., 74: 578–585.