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2008 | 64 | 08 |

Tytuł artykułu

Relationship between post mortem desmin degradation and meat quality of poultry breast muscle

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The objective of the study was to determine the level of post mortem intact desmin and compare the intact desmin with physico-chemical properties of poultry breast muscle during 168 hours cool storage at +4°C. The research was conducted on 6 40-day-old Ross 308 broiler chickens slaughtered at a similar body weight. Muscle samples were taken immediately after slaughter of animals (15 min) and on 24, 96 and 168 hours after slaughter. The post mortem intact desmin and degradation products were determined using SDS-PAGE and Western blot analysis. The following technological parameters of meat were also determined: pH, colour L*a*b*, drip loss, thermal loss, free water, and shear force. The current findings indicate that the fastest rate of desmin degradation and the greatest changes in the physico-chemical properties of meat occurred within the first 24 h of storage. Longer storage of meat had no effect on meat quality traits except drip loss. Moreover, our results indicate that levels of intact desmin positively related with drip loss values and negatively with pH and shear force.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

64

Numer

08

Opis fizyczny

p.1003-1006,fig.,ref.

Twórcy

autor
  • Department of Reproduction and Animal Anatomy, Faculty of Animal Breeding and Biology, Agricultural University, Al. Mickiewicza 24/28, 30-059 Krakow, Poland
autor

Bibliografia

  • 1. Bee G., Anderson A. L., Lonergan S. M., Huff-Lonergan E.: Rate and extent of pH decline affect proteolysis of cytoskeletal proteins and water-holding capacity in pork. Meat Sci. 2007, 76, 359-365.
  • 2. Boulianne M., King A. J.: Biochemical and color characteristics of skinless boneless pale chicken breast. Poultry Sci. 1995, 74, 1693-1698.
  • 3. Cavitt L. C., Meullenet J. F., Gandhapuneni R. K., Youm G. W., Owens C. M.: Rigor development and meat quality of large and small broilers and use of Allo-Kramer shear, needle puncture, and razor blade shear to measure texture. Poultry Sci. 2005, 84, 113-118.
  • 4. Gardzielewska J., Jakubowska M., Buryta B., Karamucki T., Natalczyk-Szymkowska W.: Pomiar pH1 a jakość mięsa kurcząt brojlerów. Medycyna Wet. 2003, 59, 426-428.
  • 5. Helliwell T. R.: Muscle: Part 1 - Normal structure and function. Current Orthopaedics 1999, 13, 33-41.
  • 6. Huff-Lonergan E., Lonergan S. N.: Mechanism of water-holding capacity of meat: The role of post mortem biochemical and structural changes. Meat Sci. 2005, 71, 194-204.
  • 7. Huff-Lonergan E., Mitsuhashi T., Beekman D. D., Parrish F. C., Olson D. G., Robson R. M.: Proteolysis of specific muscle structural proteins by µ-calpain at low pH and temperature is similar to degradation in post mortem bovine muscle. J. Anim. Sci. 1996, 74, 993-1008.
  • 8. Hwan S. F., Bandman E.: Studies of desmin and α-actinin degradation in bovine semitendinosus muscle. J. Food Sci. 1989, 54, 1426-1430.
  • 9. Kristensen L., Purslow P. P.: The effect of ageing on the water-holding capacity of pork: role of cytoskeletal proteins. Meat Sci. 2001, 58, 17-23.
  • 10. Melody J. L., Lonergan S. M., Rowe L. J., Huiatt T. W., Mayes M. S., Huff-Lonergan E.: Early post mortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles. J. Anim. Sci. 2004, 82, 1195-1205.
  • 11. Morrison H. E., Mielche M. M., Purlsow P. P.: Immunolocalisation of intermediate filament protein in porcine meat. Fibre type and muscle-specific variation during conditioning. Meat Sci. 1998, 50, 91-104.
  • 12. Petracci M., Fletcher D. L.: Broiler skin and meat color changes during storage. Poultry Sci. 2002, 81, 1589-1597.
  • 13. Quiao M., Fletcher D. L., Smith D. P., Northcutt J. K.: Effect of broiler breast meat color on pH, moisture, water-holding capacity, and emulsification capacity. Poultry Sci. 2001, 80, 676-680.
  • 14. Remignon H., Molette C., Babile R., Fernandez X.: Current advances in proteomic analysis and its use for the resolution of poultry meat quality problems. World's Poultry Science Journal 2006, 62, 123-129.
  • 15. Schafer A., Rosenvold K., Purslow P. P., Andersen H. J., Henckel P.: Physiological and structural events post mortem of importance for drip loss in pork. Meat Sci. 2002, 61, 355-366.
  • 16. Schreus F. J. G.: Post-mortem changes in chicken muscle. World's Poultry Science Journal 2000, 56, 319-346.
  • 17. Taylor R. G., Koohmaraie M.: Effects of post mortem storage on the ultrastructure of the endomysium and myofibrils in normal and callipyge longissimus. J. Anim. Sci. 1998, 76, 2811-2817.
  • 18. Therkildsen M., Larsen M. L., Bang H. G., Verstergaard M.: Effect of growth rate on tenderness development and final tenderness of meat from Friesian calves. Animal Sci. 2002, 74, 253-264.
  • 19. Thielke S., Lhafi S. K., Kuhner M.: Effect of aging prior to freezing on poultry meat tenderness. Poultry Sci. 2005, 84, 607-612.
  • 20. Van Lack R. L. J. M., Liu C. H., Smith M. O., Loveday H. D.: Characteristics of pale, soft, exudative broiler breast meat. Poultry Sci. 2000, 79, 1057-1061.
  • 21. Wheeler T. L., Koohmaraie M.: The extent of proteolysis is independent of sarcomere length in lamb longissimus and psoas major. J. Anim. Sci. 1999, 77, 2444-2451.
  • 22. Wheeler T. L., Shackelford S. D., Koohmaraie M.: Variation in proteolysis, sarcomere length, collagen content, and tenderness among major pork muscles. Journal of Animal Sci. 2000, 78, 958-965.
  • 23. Yang C. C., Chen T. C.: Effects of refrigerated storage, pH adjustment and marinade on color of raw and microwave cooked chicken meat. Poultry Sci. 1993, 72, 355-362.
  • 24. Zhang W. G., Lonergan S. M., Bargner M. A., Huff-Lonergan E.: Contribution of post mortem changes of integrin, desmin and µ-calpain to variation in water holding capacity of pork. Meat Sci. 2006, 74, 578-585.

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Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.dl-catalog-3e1579f4-742f-4051-bc47-4140ddd10d0b
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