Effect of gender and slaughter conditions on pH decline and proteolysis of ostrich meat during ageing by SDS-PAGE

Baghaei, H.; Varidi, M.J.; Varidi, Mehdi; Es´haghi, Z.

doi:10.22101/JRIFST.2013.07.03.212

Effect of gender and slaughter conditions on pH decline and proteolysis of ostrich meat during ageing by SDS-PAGE

Document Type : Original Paper

Authors

¹ PhD. student, Department of Food Science and Technology, College of Agriculture, Ferdowsi University of Mashhad

² Associated professor, Department of Food Science and Technology, Ferdowsi University of Mashhad

³ Assistant Professor, Department of Food Science and Technology, Ferdowsi University of Mashhad, Mashhad, Iran

⁴ Associated professor, Department of Chemistry, Faculty of Sciences, Payame Noor University, Mashhad

10.22101/JRIFST.2013.07.03.212

Abstract

Postmortem proteolysis is one of the best ways to study meat tenderizing process. In this research, two groups of ostriches (male and female) were slaughtered by two methods: commercial (without electrical shock) and noncommercial (by electrical shock at 80 v/ 500 mA/ 10 s). pH decline of M. Gastrocnemius pars externa muscle was measured at 0, 1, 3, 6, 9, 18 and 24 hours and 3, 5, 7, 14 days during aging. Myofibrillar protein changes were evaluated at 1, 3, 5, 7 and 14 days postmortem by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Results showed that electrical stunning accelerated glycolysis rate especially at 1 to 3 hours postmortem (P<0.05). Female ostriches had faster pH decline (P<0.05). Myofibrillar patterns indicated that major changes was corresponded to the gradual degradation of troponin T from day 1 onwards and simultaneously appearance of 25 to 32 KDa peptides (P<0.05). Myosin Heavy Chain (MHC), α-actinin and desmin were degraded during storage period and polypeptides of 60 and 100 KDa were observed at this time. Because of accelerated pH decline, gender and slaughter conditions had significant effect (P<0.05) on degradation of most proteins that were substrates for calpaein enzymes.

Keywords

References

محمدی، ا. 1385. نوپروری شترمرغ در ایران. انتشارات اطلاعات.

Bandman, E. & Zdanis, D. 1988. An immunological method to asses protein degradation in postmortem muscle. Meat Science, 22: 1–19.

Buts, B., Claeys, E. & Demyer, D. 1986. Relation between concentrations of troponin-T, 30,000-Dalton and titin on SDS–PAGE and tenderness of bull longissimus dorsi. 32nd European Meeting of Meat Research Workers, 24 – 29 August, Ghent, Belgium.

Channon, H. A., Payne, A. M. & Warner, R. D. 2002. Comparison of CO2 stunning with manual electrical stunning (50 Hz) of pigs on carcass and meat quality. Meat Science, 60: 63–68.

Claeys, E., Uytterhaegen, L., Buts B. & Demeyer, D. 1995. Quantification of beef myofibrillar proteins by SDS-PAGE. Meat Science, 39: 177-193.

Choi, Y.M., Lee, S.H., Choe, J.H., Rhee, S.M., Lee, S.K., Joo S.T. & Kim, B.C. 2010. Protein solubility is related to myosin isoforms, muscle fiber types, meat quality traits, and postmortem protein changes in porcine longissimus dorsi muscle. Livestock Science, 127: 183–191.

Choi, Y.M. & Kim, B.C. 2009. Muscle fiber characteristics, myofibrillar protein isoforms, and meat quality (review). Livestock Science, 122: 105–118.

Culler, R. D., Parrish, F. C., Smith, G. C. & Cross. H. R. 1978. Relationship of myofibril fragmentation Index to certain chemical, physical and sensory characteristics of bovine longissmus muscle. Journal of Food Science, 43: 1177.

Dayton, W. R., Goll, D. E., Stromer, M. H., Reville, W. J., Zeece, M. G. & Robson, R. M. 1975. Some properties of a Ca2+ activated protease that may be involved in myofibrillar protein turnover. Cold Spring Harbor Conferences in Cell Proliferation, Volume 2. In: Proteases and biological control (E., Reich, D. B., Rifkin, & E., Shaw, eds). Cold Spring Harbor, New York

Dunker, A. K. & Reuckert, R. R. 1969. Journal of Biology Chemical, 244: 5047.

Dransfield, E. 1994. Tenderness of meat, poultry, and fish. Chapman and Hall, London, 289-315.

Geesink, G.H., Kuchay, S., Chishti A.H. & Koohmaraie, M. 2006. Micro-calpain is essential for postmortem proteolysis of muscle proteins. Journal of Animal Science, 84: 2834-2840.

Gheisari, H. R., Aminlari, M. & Shekarforoush, S.H. 2009. A comparative study of the biochemical and functional properties of camel and cattle meat during frozen storage. Veterinarski Arhive, 79 (1): 51-68.

Gil, M. Ramírez J.A., Pla, M., Ariño, B., Hernández, P., Pascual, M., Blasco, A., Guerrero, L., Hajós, G., Szerdahelyi, E.N. & Oliver, M.Á. 2006. Effect of selection for growth rate on the ageing of myofibrils, meat texture properties and the muscle proteolytic potentional of m. longissmus in rabbits. Meat Science, 72: 121-129.

Goll, D. E., Otsuka, Y., Nagainis, P. A., Shannon, J. D., Sathe, S. K. & Muguruma, M. 1983. Role of muscle proteinases in maintenance of muscle integrity and mass. Journal of Food Biochemistry, 7: 137-177.

Ho, C. Y., Stromer, M. H. & Robson, R. M. 1994. Identification of the 30 kDa polypeptide in postmortem skeletal muscle as a degradation product of troponin-T. Biochimie, 76: 369–375.

Hoffman, L. C., Botha, S. C. & Britz, T. J. 2007. Muscle pH and temperature changes in hot- and cold-deboned ostrich Muscularis gastrocnemius, pars intra and Muscularis iliofibularis during the first 23 h post-mortem. Meat Science, 75: 343-349.

Huff-Lonergan, E., Zhang W. & Lonergan, M. S. 2010. Biochemistry of postmortem muscle- lessons on mechanisms of meat tenderization (review). Meat Science, 86: 184-195.

Hwang, H. I., Devine C. E. & Hopkins, D. L. 2003. The biochemical and physical effects of electrical stimulation on beef and sheep meat tenderness (review). Meat Science, 65: 677- 691.

Jiang, S. T. 1998. Contribution of muscle proteinases to meat tenderization (review). Proceedings of the National Science Council, 22 (3): 97-107.

Kandeepan, G., Anjaneyyulu, A. S. R., Kondiaiah, N., Mendiratta, S. K. & Lakshmanan, V. 2009. Effect of age and gender on the processing characteristics of buffalo meat. Meat Science, 83: 10-14.

Kemp, C. M., Sensky, P. L., Bardsley, R. G., Buttery, P. J. & Parr, T., 2010. Tenderness-an enzymatic view. Meat Science, 84: 284-256.

Kent, M.P., Spencer, M.J. & Koohmaraie, M. 2004. Postmortem proteolysis is reduced in transgenic mice over expressing calpastatin. Journal of Animal Science, 82: 794-801.

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.

Koohmaraie, M. 1994. Muscle proteinases and meat aging. Meat Science, 36: 93- 104.

Koohmaraie, M., et al.1995. Calpastatin-based methods for predicting meat tenderness. ECCEAMST, USA.

Laemmli, U. K. 1970. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature, 227: 680 – 685.

Lamare, M. Taylor, R.G., Farout, L., Briand, Y. & Briand, M. 2002. Changes in proteasome activity during postmortem aging of bovine muscle. Meat Science, 61: 199- 204.

Linares, M. B., Bornez, R. & Vergara. H. 2007. Effect of different stunning systems on meat quality of light lamb. Meat Science, 76: 675–681.

Neath, K. E., Del Barrio, A.N., Lapitanb, R.M., Herrerab, J.R.V., Cruzb, L.C., Fujiharac, T., Muroyad, S., Chikunid, K., Hirabayashia, M. & Kanai, Y. 2007. Differences in tenderness and pH decline between water buffalo meat and beef during postmortem aging. Meat Science, 75: 299-505.

Nowak, B., Mueffling, T. V. & Hartung. J. 2007. Effect of different carbon dioxide concentrations and exposure times in stunning of slaughter pigs: Impact on animal welfare and meat quality. Meat Science, 75: 300–308.

Olson, D. G., Parrish, F. C., Dayton, W. R. & Goll. D. E. 1977. Effect of postmortem storage and calcium activated factor on the myofibrilllar proteins of bovine skeletal muscle. Journal of Food Science, 42: 117-123.

O’Shea, J. M., Robson, R. M., Huiatt, T. W., Hartzer, M. K. & Stromer, M. H. 1979. Purified desmin from adult mammalian skeletal muscle: a peptide mapping comparison with desmins from adult mammalian and avian smooth muscle. Biochemistry Biophysical Research Communications, 89: 972-980.

Ouali, A. 1990. Meat tenderization: possible causes and mechanism (a review). Journal of Muscle Foods, 1: 129-165.

Ouali, A. 1992. Proteolytic and physicochemical mechanisms involved in meat texture development. Biochimie, 74: 251-265.

Paleari, M. A., Corsico, P. & Beretta, G. 1995. The ostrich: breeding, reproduction, slaughtering and national value of the meat. Fleischwirtschaft, 75: 1120-1123.

Rosenvold, K. & Andersen, H. J. 2003. Factors of significance, for pork quality (review). Meat Science, 64: 219–237.

Sales, J. & Mellet, F. D. 1996. Post-mortem pH decline in different ostrich muscles. Meat Science, 42 (2): 235-238.

Salm, C. P., Forrest, J. C., Aberle, E. D., Mills, E. W., Snyder, A. C. & Judge. M. D. 1983. Bovine muscle shortening and protein degradation after electrical stimulation, excision and chilling. Meat Science, 8: 163–183.

Sentandreu, M. A., Coulis, G. & Ouali, A. 2002. Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends in Food Science and Technology, 13: 400–421.

Skaara, T. & Regenstein, M. 1990. The structure and properties of myofibrillar proteins in beef, poultry and fish. Journal of Muscle Foods, 1: 269-291.

Smulders, F. J. M., Toldra, F., Flores, J. & Prieto, M. 1992. New technologies for meat and meat products (eds). ECCEAMST, Utrecht.

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, 21: 1351-1367.

Thomas, A. R., Gondoza, H., Hoffman, L. C., Oosthuizen, V. & Naudé, R. J. 2004. Roles of the 20S proteasome, and cathepsins B, L, H and D, in ostrich meat tenderisation. Meat Science, 67: 113-120.

Van Jaarsveld, F. P. 1998. The role of calcium-dependent proteases and cathepsins in postmortem proteolysis and tenderness of ostrich meat. PhD thesis, University of Port Elizabeth, Port Elizabeth, South Africa.

Vergara, H., Linares, M. B., Berruga, M. I. & Gallego, L. 2005. Meat quality in suckling lambs: Effect of pre-slaughter handling. Meat Science, 69: 473–478.

Yates, L. D. Dutson, T. R., Caldwell, J. & Carpenter, Z. L. 1983. Effect of temperature and pH on the postmortem degradation of myofibrillar proteins. Meat Science, 1: 157-179.