Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
1996 | 1 | nr 728 | 185--197
Tytuł artykułu

Rola kalpain w skruszaniu mięsa

Warianty tytułu
Role of Calpains in Meat Tenderisation
Języki publikacji
Powszechnie przyjmuje się, że proteinazy są włączone w pośmiertną proteolizę powodującą skruszanie mięsa. Kontrowersyjne pozostaje, które z nich: tj. lizosomalne katepsyny, multikatalityczny kompleks proteinaz (MCP) czy kalpainy - biorą udział w tym procesie.
W oparciu o aktualne doniesienia sugeruje się, że katepsyny lizosomalne nie odgrywają istotnej roli w pośmiertnej proteolizie. Wynika to z faktu, że podczas przechowywania mięsa w temp. 2-4° C nie stwierdzono degradacji miozyny i aktyny, które wśród białek miofibrylarnych są głównym substratem dla katepsyn. Ponadto katepsyny są zlokalizowane w lizosomach i muszą być z nich uwolnione, aby mieć dostęp do miofibryli. Jedynie podczas przechowywania mięsa w temp. 25° C lub wyższej obserwuje się degradację miozyny, aktyny, α-aktyniny i jest prawdopodobne, że w tych warunkach przechowywania katepsyny są odpowiedzialne za degradację białek miofibrylarnych. (fragment tekstu)
Tenderness is one of the most important criterion of meat acceptability and its variability has been a major concern to the meat industry and to the consumer. Post-mortem tenderisation is a complex process that is affected by a large number of factors including rate of glycolysis, rate of pH decline, osmolarity of muscle cells, temperature and genetic factors inherent to the animal. These many factors, according to the newest hypothesis, exert their effects through a few basic processes ie. the nature of the actin/myosin interaction and calpain induced cleavage of certain cytoskeletal proteins that constitute the costameres (vinculin, dystrophin, desmin), intermyofibrillar linkages (desmin) and Z-disc//sarcomer connections (nebulin, titin). The objective of this paper was to discuss, on the basis of the broad literature review, the role of neutral proteinases (calpains) in post-mortem protein degradation and meat tenderisation. (original abstract)
Opis fizyczny
  • Akademia Ekonomiczna we Wrocławiu
  • Goli D.E., Geesink G.H., Taylor R.G., Thompson У.E.: Does proteolysis cause all post-mortem tenderization, or are changes in the actin/myosin interaction involved? Proc. 41st Int. Cong. Meat Sci. and Technol., San Antonio, Texas, 11:537 (1995).
  • Koohmaraie M.: Muscle proteinoses and meat aging. Meat Science, 36, 93 (1994).
  • Goli D.E., Otsuka Y., Nagainis P.A., Shannon J.D., Sathe S.K., Muguruma M.: Role of muscle proteinoses in maintenance of muscle integrity and mass. Journal of Food Biochemistry, 7, 137 (1983).
  • Koohmaraie M., Seideman S. C, Schollmeyer J. E., Dutson T. R., Babiker A.S.: Factors associated with the tenderness of three bovine muscles. J. of Food Science, 53, 2V 407 (1988).
  • Koohmaraie M., Whipple G., Kretchman D.H., Crouse J.D., Mersman H.J.: Post-mortem proteolysis in longissimus muscle from beef, lamb and pork carcasses. J. Anim. Sci., 69, 617 (1991).
  • Koohmaraie M.: The role of Ca2+ - dependent proteases (calpains) in post-mortem proteolysis and meat tenderness. Biochimie, 74, 239 (1992).
  • Goli D.E.: Role of proteinases and protein turnover in muscle growth and meat quality. Proc. 44th Reciproc. Meat Conf., Chicago, 44, 25 (1991).
  • Etherington D. J., Taylor M.A.J., Wakefield D.K., Cousins A., Dransfield E.: Proteinase (cathepsin B, D, L and calpains) levels and conditioning rates in normal, electrically stimulated and high-ultimate-pH chicken muscle. Meat Science, 28, 88 (1990).
  • Ouali A.: Proteolytic and physicochemical mechanisms involved in meat texture development. Biochimie, 74, 251 (1992).
  • Ouali A.: Osmotic pressure changes in post-mortem bovine muscles: factors of variation and possible causative agents., Proc. 37th Intern. Cong. Meat Sci. and Technol., Kulmbach, Germany, 3: 33, 452 (1991).
  • Koohmaraie M.: Role of the neutral proteinoses in postmortem muscle protein degradation and meat tenderness. Reciproc. Meat Conf. 45, 63 (1992).
  • Goll D.E., Thompson Y.F., Taylor R.G., Zalewska T.: Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin. BioEssays, 14, 8, 549 (1992).
  • Koohmaraie M.: Ovine skeletal muscle multicatalytic proteinase complex (proteasome): Purification, characterization and comparison of its effect on myofibrils with u-calpains. J. Anim. Sei., 70, 3697 (1992).
  • Cong J., Thompson V.F., Goll D.E.: Effect of monoclonal antibodies specific for the 28-kDa subunit on catalytic properties of the calpains. The Journal of Biological Chemistry, 268, 34, 25740 (1993).
  • Goll D.E., Thompson V.F., Taylor R.G., Christiansen J.A.: Role of the calpain system in muscle growth. Biochimie, 74, 225 (1992).
  • Koohmaraie M.: Effect of pH, temperature and inhibitors on autolysis and catalytic activity of bovine skeletal muscle u-calpain. J. Anim. Sci., 70, 3071 (1992).
  • Goll D.E., Kleese W.C., Szpacenko A.: Skeletal muscle proteases and protein turnover. [w:] Animal growth regulation. Edited by D.R. Campion, G.J. Hausman, R.J. Martin, 141 (1989).
  • Killefer J., Koohmaraie M.: Bovine skeletal muscle calpastatin: cloning, sequence analysis and steady-state mRNA expression. J. Anim. Sci., 72, 606 (1994).
  • Kendall T.L., Koohmaraie M., Arbona J.R., Williams S.E, Young L.L.: Effect of pH and ionic strength on bovine m-calpain and calpastatin activity. J. Anim. Sci., 71, 96 (1993).
  • Tarrant P.V.: Review: Muscle biology and biochemistry. Proc. European Meeting of Meat Research Workers, 1 (1987).
  • Dransfield E., Wakefield D.K., Parkman I.D.: Modelling post-mortem tenderisation-I: Texture of electrically stimulated and non-stimulated beef. Meat Science, 31, 57 (1992).
  • Dransfield E., Etherington D.J., Taylor M.A.J.: Modelling post-mortem tenderisation-II: Enzyme changes during storage of electrically stimulated and non-stimulated beef. Meat Science, 31, 75 (1992).
  • Dransfield E.: Modelling post-mortem tenderisation-III: Role of calpain I in conditioning. Meat Science, 31, 85 (1992).
  • Dransfield E.: Modeling post-mortem tenderisation-IV: Role of calpains and calpastatin in conditioning. Meat Science, 34, 217 (1993).
  • Dransfield E.: Modelling post-mortem tenderisation-V: Inactivation of calpains. Meat Science, 37, 391 (1994).
  • Dransfield E.: A unified model for meat tenderness. Meat Focus International, 1, 5, 237 (1992).
  • Dransfield E.: Optimisation of tenderisation, ageing and tenderness. Meat Science, 36, 105 (1994).
  • Ouali A.: Sensory quality of meat as affected by muscle biochemistry and modem technologies, [w:] Animal Biotechnology and the Quality of Meat Production, by L.O. Friems, B.G. Cottyn, D.I. Demeyer, Amsterdam (1985).
  • Wheeler T.L., Koohmaraie M.: Effects of the B-adrenergic agonist L644,969 on muscle protein turnover, endogenous proteinas activities and meat tenderness in steers. J. Anim. Sci., 70, 3035 (1992).
  • Ouali A.: Meat tenderisation: Possible causes and mechanisms. A review. J. of Muscle Foods, 1, 129 (1990).
  • Ouali A., Talmant A.: Calpains and calpastatin distribution in bovine, porcine and ovine skeletal muscles. Meat Science, 28, 331 (1990).
  • Dransfield E., Jones R.C.D., Macfie H.J.H.: Tenderising in m. longissimus dorsi of beef, veal, rabbit, lamb and pork. Meat Science, 5, 139 (1980/1981).
  • Etherington D.J., Taylor M.A.J., Dransfield E.: Conditioning of meat from different species. Relationship between tenderising and the levels of cathepsins B, cathepsin L, calpain I, calpain II and B-glucuronidase. Meat Science, 20, 1 (1987).
  • Johari S., Maeda Y., Okamoto S., Hashiguchi T.: Comparison of calpain and calpastatin activities in skeletal muscle of broiler and layer chickens. British Poultry Science, 34, 819 (1993).
  • Wheeler T.L., Koohmaraie M.: Pre-rigor and post-rigor changes in tenderness of ovine longissimus muscle. J. Anim. Sci., 72, 1232 (1994).
  • Eikelenboom G.: Effects of various processing methods on the meat quality of beef and pork. Proc. 38th Intern. Cong. Meat Sci. and Technol., Calgary, Alberta, Canada, 3: 95 (1993).
  • Lesiów T.: Zastosowanie elektrostymulacji w przetwórstwie mięsa bydlęcego. Gospodarka Mięsna, 2, 22 (1993).
  • Koohmaraie M., Babiker A.S., Schroeder A.L., Merkel R.A., Dutson T.R.: Acceleration of post-mortem tenderisation in ovine carcasses through activation of Ca2+ - dependent proteases. J. Food Science, 53, 6,1638 (1988).
  • Wheeler T.L., Crouse J.D., Koohmaraie M.: The effect of post-mortem time of injection and freezing on the effectiveness of calcium chloride for improving beef tenderness. J. Anim. Sci., 70, 3451 (1992).
  • Koohmaraie M., Wheeler T.L., Schackelford S.D.: Eliminating inconsistent beef tenderness with calcium-activated tenderisation. Presented at Nebraska Seedstock Symposium (1993).
  • Morgan J.B., Miller R.K., Mendez F.M., Hale D.S., Saveli J.W.: Using calcium chloride injection to improve tenderness of beef from mature cows. J. Anim. Sci., 69, 4469 (1991).
  • Koohmaraie M., Wheeler T.L., Schackelford S.D.: Beef tenderness: Regulation and predication. Beef Vanguard 94, Int'l Congress Buenos Aires, Argentina (1994).
  • Schackelford S.D., Koohmaraie M., Cundiff L.V., Gregory K.E., Rohrer G.A., Saveli J.W.: Heritabilities and phenotypic and genetic correlations for bovine post-rigor calpastaiin activity, intramuscular fat content. Wamer-Bratzler shear force, retail product yield and growth rate. J. Anim. Sci., 72, 857 (1994).
Typ dokumentu
Identyfikator YADDA

Zgłoszenie zostało wysłane

Zgłoszenie zostało wysłane

Musisz być zalogowany aby pisać komentarze.
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.