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Autor
Nowak Marzena (Akademia Rolnicza w Krakowie)
Tytuł
Rola kalpain w procesie kruszenia mięsa
The Role of Calpains in the Meat Tenderization Process
Źródło
Żywność: nauka - technologia - jakość, 2005, R. 12, nr 1 (42), s. 5-17, bibliogr. 61 poz.
Słowa kluczowe
Żywność, Jakość mięsa, Badanie żywności, Technologia produkcji żywności
Food, Meat quality, Food research, Food production technology
Uwagi
streszcz., summ.
Abstrakt
Kruchość mięsa oraz czynniki na nią wpływające od dawna są przedmiotem badań. Istnieje kilka teorii wyjaśniających proces kruszenia mięsa. Za najbardziej prawdopodobną uznana została kalpainowa teoria tenderyzacji. Kalpainy spełniają podstawowe kryteria stawiane czynnikom wpływającym na proces kruszenia mięsa. Enzymy te są obecne w komórce mięśniowej, a w doświadczeniach przeprowadzanych in vitro prowadzą do tych samych produktów degradacji białek, jakie wykrywane są w mięsie po okresie dojrzewania. Mają one dostęp do miofibryli w komórce. Aktywność kalpain oraz stosunek aktywności kalpainy do aktywności kalpastatyny są skorelowane z twardością mięsa. Im wyższa jest aktywność kalpain i im wyższy stosunek kalpaina/kalpastatyna, tym bardziej kruche mięso otrzymuje się. Warunki w jakich enzymy te wykazują aktywność są zbliżone do warunków panujących w tkance mięśniowej po śmierci zwierzęcia. Na aktywność kalpain w mięsie działają zarówno czynniki przyżyciowe, w tym genetyczne, jak i pośmiertne. Mimo, że mechanizm działania kalpain nie jest całkowicie wyjaśniony, na podstawie wyników licznych doświadczeń można stwierdzić, że kalpainy pełnią ważną rolę w procesie tenderyzacji mięsa. W artykule scharakteryzowano kalpainy i opisano niektóre z czynników wpływających na ich aktywność. (abstrakt oryginalny)

Meat tenderness and factors influencing it have been investigated for a long time. There are several theories explaining the process of meat tenderization. The calpain theory of tenderization has been accepted as the most feasible one. Calpains meet the basic criteria defined for factors that impact meat tenderization. These enzymes are present in a muscle cell, and in vitro experiments, when calpains are used, there are detected the same protein degradation products as in the meat after its raping. Calpains have access to myofibrils in cells. The activeness of calpains and the ratio between it and the calpastatin are correlated with the meat hardness. The higher the hardness of meat and the higher the ratio: calpain to calpastatin, the more tender meat can be obtained. Conditions under which these enzymes are active are close to conditions in the meat tissue after the death of animal. The calpain activity depends both on the survival, including genetic, and the post-mortem factors. Although the mechanism of calpain activity has not been satisfactorily explained so far, but on the basis of results obtained, it can be concluded that they play an important role in the meat tenderization process. In this paper, calpains are characterized and some factors influencing their activeness are described. (original abstract)
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Biblioteka Główna Uniwersytetu Ekonomicznego w Krakowie
Biblioteka Główna Uniwersytetu Ekonomicznego w Poznaniu
Biblioteka Główna Uniwersytetu Ekonomicznego we Wrocławiu
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Bibliografia
Pokaż
  1. Boehm M.L., Kendall T.L., Thompson V.F., Goll D.E.: Changes in the calpains and calpastatin during post mortem storage of bovine muscle. J. Anim. Sci. 1998, 76, 2415-2434.
  2. Carragher N.O., Frame M.C.: Calpain: a role in cell transformation and migration. Int. J. Bioch. Cell Biol., 2002, 34, 1539-1543.
  3. Dąbrowska R., Wrzosek A.: Molekularne podstawy kontroli skurczu mięśni przez jony wapnia. Kosmos, 1997, 46 (4) 555-562.
  4. Delgado E.F., Geesink G. H., Marchello J.A., Goll D.E., Koohmaraie M.: The calpain system in three muscles of normal and callipyge sheep. J. Anim. Sci., 2001, 79, 398-412.
  5. Delgado E.F., Geesink G.H., Marchello J.A., Goll D.E., Koohmaraie M.: Properties of miofibrilbound calpain activity in longissimus muscle of callipyge and normal sheep. J. Anim. Sci., 2001, 79, 2097-2107.
  6. Dransfield E.: Modelling post-mortem tenderization-IV: Role of calpains and calpastatin in conditioning. Meat Sci., 1993, 34, 217-234.
  7. Dransfield E.: Calpains from thaw rigor muscle. Meat Sci., 1996, 43, 311-320.
  8. Dransfield E.: Meat tenderness-the μ-calpain hypothesis. 45th ICoMST, 1999, pp. 220-228.
  9. Duckett S.K., Klein T.A., Leckie R.K., Thorngate J.H., Busboom J.R., Snowder G.D.: Effect of freezing on calpastatin activity and tenderness of callipyge lamb. J. Anim. Sci., 1998, 76, 1869-1874.
  10. Ertbjerg P., Henckel P., Karlsson A., Larsen L. M., Møller A. J.: Combined effect of epinerphine and exercise on calpain/calpastatin and cathepsin B and L activity in porcine longissimus muscle. J. Anim. Sci., 1999, 77, 2428-2436.
  11. Freking B.A., Keele J. W., Beattie C.W., Kappes S.M., Smith T.P.L., Sonstegard T.S., Nielsen M.K., Leymaster K.A.: Evaluation of the ovine callipyge locus: I. Relative chromosomal position and gene action. J. Anim. Sci., 1998, 76, 2062-2071.
  12. Geesink G.H., Koohmaraie M.: Postmortem proteolysis and calpain/calpastatin activity in callipyge and normal lamb biceps femoris during extended postmortem storage. J. Anim. Sci., 1999 77, 1490-1501.
  13. Geesink G.H., Taylor R.G., Bekhit A.E.D., Bickerstaffe R.: Evidence against the non-enzymatic calcium theory of tenderization. Meat Sci., 2001, 59, 417-422.
  14. Goll D.E., Dayton W.R., Singh I., Robson R.M.: Studies of the a-actinin/actin interaction in the Zdisc by using calpain. J. Biol. Chem., 1991, 266, 13, 8501-8510.
  15. Goll D.E., Thompson V.F., Taylor R.G., Ouali A.: The calpain system and skeletal muscle growth. Can. J. Anim. Sci., 1998, 78, 503-512.
  16. Harris S.E., Huff-Lonergan E., Lonergan S.M., Jones W.R., Rankins D.: Antioxidant status affects color stability and tenderness of calcium chloride-injected beef. J. Anim. Sci., 2001, 79, 666-677.
  17. Hopkins D.L., Thompson J.M.: Inhibition of protease activity 2. Degradation of myofibrillar proteins, myofibril examination of free calcium levels. Meat Sci., 2001, 59, 199-209.
  18. Huff-Lonergan E., Mitsuhashi T., Beekman D. D., Parrish F. C., Jr., 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.
  19. Hughes M.C., Geary S., Dransfield E., McSweeney P.L.H., O'Neill E.E.: Characterization of peptides released from rabbit skeletal muscle tin-T by μ-calpain under conditions of low temperature and high ionic strength. Meat Sci., 2001, 59, 61-69.
  20. Hwang I.H., Thompson J.M.: The effect of time and type of electrical stimulation on the calpain system and meat tenderness in beef longissimus dorsi muscle. Meat Sci., 2001, 58, 135-144.
  21. Ilian M.A., Morton J.D., Kent M.P., Le Conteur C.E., Hickford J., Cowley R., Bickerstaffe R.: Intermuscular variation in tenderness: Association with the ubiquitous and muscle specific calpains. J. Anim. Sci., 2001, 79, 12-132.
  22. Jakubiec-Puka A.: Rola proteolitycznego systemu kalpainowego w komórkach zwierzęcych. Postępy Biochemii, 1993, 39 (4) 251-258.
  23. Jakubiec-Puka A.: Kalpainy. Kosmos, 1997, 46 (4), 609-614.
  24. JeacockeR. E.: The concentrations of free magnesium and free calcium ions both increase in skeletal muscle fibres entering rigor mortis. Meat Sci., 1993, 35, 27-45.
  25. Kanawa R., J. J., Takahashi K.: Inactivity of μ-calpain throughout post mortem aging of meat. J. Food Sci., 2002, 67, 2, 635-638.
  26. Klont R.E., Brocks L., Eikelenboom G.: Muscle fibre type and meat quality. Meat Sci., 1998, 49 (Suppl. 1), S219-S229.
  27. Koohmaraie M.: Effect of pH, Temperature, and inhibitors on autolysis and catalytic activity of bovine skeletal muscle b-calpain. J. Anim. Sci., 1992, 70, 3071-3080.
  28. Koohmaraie M.: The role of Ca2+ dependent proteinases i post mortem proteolysis and meat tenderness. Biochimie, 1992, 74, 3, 239-245 (English abstract).
  29. Koohmaraie M.: Muscle proteinases and meat aging. Meat Sci., 1994, 36, 93-104.
  30. Koohmaraie M.: Biochemical factors regulating the toughening and tenderization processes of meat. Meat Sci., 1996, 43, S, S193-S201.
  31. Kristensen L., Therkildsen M., Riis B., Sørensen M.T., Oksbjerg N., Purslow P.P., Ertbjerg P.: Dietary induced growth rate in pigs: Effects on in vivo and post mortem muscle proteolysis and meat quality. J. Anim. Sci., 2002, 80, 2862-2871.
  32. Kurebayashi N., Harkins A.B., Baylor S. M.: Use of fura red as an intracellular calcium indicator in frog skeletal muscle fibers. Biophys. J., 1993, 64, 1934-1960.
  33. Lawrie R.A.: Meat Science. Pergamon Press, Oxford 1985.
  34. Lee S., Polidori P., Kaufman R.G., Kim B.C.: Low-voltage electrical stimulation effects on proteolysis and lamb tenderness. J. Food Sci., 2000, 65 (5), 786-790.
  35. Ma H., Fukiage Ch., Kim Y.H., Duncan M.K., Reed N. A., Shih M., Azuma M., Shearer T.R.: Characterization and expression of calpain 10. J. Biol. Chem., 2001, 276 (30), 28525-28531.
  36. Maribo H., Ertbjerg P., Andersson M., Barton-Gade P., Møller A.J.: Electrical stimulation of pigseffect on pH fall, meat quality and Cathepsin B+L activity. Meat Sci., 1999, 52, 172-187.
  37. Morton J.D., Bickerstaffe R., Kent M.P., Dransfield E., Keeley G.M.: Calpain-calpastatin and thoughness in m. longissimus from electrically stimulated lamb and beef carcasses. Meat Sci., 1999, 52, 71-79.
  38. Northcutt J.K., Pringle T.D., Dickens J.A., Buhr R.J., Young L.L.: Effects of age and tissue type on the calpain proteolytic system in turkey skeletal muscle. Poultry Sci., 1998, 77, 367-372.
  39. Ouali A.: Meat tenderization: Possible causes and mechanisms. A Review. J. Muscle Foods, 1990, 1 (2) 129-165.
  40. Parr T., Sensky P.L., Scothern G.P., Bardsley R.G., Buttery P.J., Wood J.D. Warkup C.: Relationship between skeletal muscle-specific calpain and tenderness of conditioned porcine longissimus muscle. J. Anim. Sci., 1999, 77, 661-668.
  41. Pringle T.D., Harrelson J.M., West R.L, Williams S.E., Johnson D.D.: Calcium-activated tenderization of strip loin, top sirloin, and top round steaks in diverse genotypes of cattle. J. Anim. Sci., 1999, 77, 3230-3237.
  42. Purslow P.P., Ertbjerg P., Baron C.P., Christensen M., Lawson M. A.: Patterns of variation in enzyme activity and cytoskeletal proteolysis in muscle. 47th ICoMST, 2001, pp. 38-43.
  43. Rosochacki S.J.: Proteoliza w mięśniach po uboju zwierząt. Przeg. Hod., 1999, 9, 26-29.
  44. Sensky P.L., Parr T., Bardsley R.G., Buttery P.J.: The relationship between plasma epinephrine concentration and the activity of the calpain enzyme system in porcine longissimus muscle. J. Anim. Sci., 1996, 74, 380-387.
  45. Sensky P.L., Parr T., Lockley A.K., Bardsley R.G., Butery P.J., Wood J.D., Warkup C.: Altered calpain levels in longissimus muscle from normal pigs and heterozygotes with the ryanodine receptor mutation. J. Anim. Sci., 1999, 77, 2956-2964.
  46. Sentandreu M.A., Coulis G., Ouali A.: Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends Food Sci. Technol., 2002, 13, 398-419.
  47. Simmons N.J., Young O.A., Dobbie P.M., Singh K., Thompson B.C., Speck P.A.: Post-mortem calpain-system kinetics in lamb: Effect of clenbuterol and preslaugter exercise. Meat Sci., 1997, 47, 1/2, 135-146.
  48. Sorimachi H., Kinbara K., Kimura S., Takahashi M., Ishiura S., Sasagawa N., Sorimachi N., Shimada H., Tagawa K., Maruyama K., Suzuki K.: Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connection through IS2, a p94-specific sequence. J. Biol. Chem., 1995, 270 (52), 31158-31162.
  49. Sorimachi H., Ishiura S., Suzuki K.: Structure and physiological function of calpains. Biochem. J., 1997, 328, 721-732.
  50. Spadoni C., Forkas A., Sinka R., Tompa P. Friedrich P.: Molecular cloning and RNA expression of a novel Drosophila calpain, calpain C. Biochem. Biophys. Res. Commun., 2003, 303, 343-349.
  51. Sreenan S.K., Zhou Y-P., Otani K., Hansen P.A., Currie K.P.M., Pan Ch-Y., Lee J-P., Ostrega D. M., Pugh W., Horikawa Y., Cox N. J., Harris C. L., Burant Ch. F., Fox A. P., Bell G. T., Polonsky K. S.: Calpains play a role in insulin secretion and action. Diabetes, 2001, 50, 2013-2020.
  52. Steen D., Claeys E., Uytterhaegen L., De Smet S., Demeyer D.: Early post-mortem conditions and the calpain/calpastatin system in relation to tenderness of double-muscled beef. Meat Sci., 1997, 45, 3, 307-319.
  53. Swanek S.S., Morgan J.B., Owens F.N., Gill D. R., Strasia A., Dolezal H.G., Ray F.K.: Vitamin D3 supplementation of beef seers increases longissimus tenderness. J. Anim. Sci., 1999, 77, 874-881.
  54. Takahashi K.: Structural weakening of skeletal muscle tissue during post-mortem ageing of meat: Non-enzymatic mechanism of meat tenderization. Meat Sci., 1996, 43, S, S67-S80.
  55. Takahashi K.: Mechanism of meat tenderization during post-mortem ageing: Calcium Theory. 45th ICoMST, 1999, pp. 230-235.
  56. Thomson B.C., Dobbie P.M., Singh K., Speck P.A.: Post-mortem kinetics of meat tenderness and the components of calpain system in bull skeletal muscle. Meat Sci., 1996, 44 (3) 151-157.
  57. Veeramuthu G.I., Sams A.R.: Post mortem pH, myofibrillar fragmentation, and calpain activity in pectoralis from electrically stimulated and muscle tensioned broiler carcasses. Poultry Sci., 1999, 78, 272-276.
  58. Watanabe A., Daly C.C., Devine C.E.: The effects of the ultimate pH of meat on tenderness changes during ageing. Meat Sci., 1996, 42 (1) 67-78.
  59. Whipple G., Koohmaraie M.: Degradation of myofibril proteins by extractable lysosomal enzymes and m-calpain, and the effects of zinc chloride. J. Anim. Sci., 1991, 69, 4449-4460.
  60. Whipple G., Koohmaraie M.: Calcium chloride marination effects on beef steak tenderness and calpain proteolytic activity. Meat Sci., 1993, 33, 265-275.
  61. Yoshizawa T., Sorimachi H., Tomioka S., Ishiura S., Suzuki K.: Calpain dissociates into subunits in the presence of calcium ions. Biochem. Biophys. Res. Commun., 1995, 208 (1) 376-383.
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ISSN
2451-0769
Język
pol
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