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2010 | 60 | 1 |

Tytuł artykułu

Selected properties of I-Z-I band proteins of sonicated beef

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Treść / Zawartość

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The objective of the reported study was to determine the effect of meat sonication within up to 2 h after slaughter with low-frequency ultrasounds (25 kHz) and at medium vibration intensity (2 W/cm2) on selected properties of myofibrilar proteins of the I-Z-I band isolated from ageing beef. Proteins were isolated directly after sonication as well as after 24, 48 and 72 h of storage at a temperature of +4°C. The isolated protein fraction was determined for: myofibrillar fragmentation index (MFI), content of reactive sulphydryl groups, redox potential, surface hydrophobicity, and proteins capability for fat emulsification. Based on the results of analyses of the isolated proteins of the I-Z-I band, no significant effect of post-slaughter sonication immediately after the slaughter was noted on the content of reactive sulphydryl groups, area of hydrophobic surface, myofibrillar fragmentation index nor redox potential. The results obtained point to a significant decrease in the capability of I-Z-I band proteins isolated from sonicated meat for fat emulsification. The research needs to be continued and extended at a molecular level in order to determine which of the myofibrillar proteins are the most susceptible to the action of ultrasounds, and to identify the mechanism of their action on biologically-complex protein systems in meat.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

60

Numer

1

Opis fizyczny

p.51-55,ref.

Twórcy

autor
  • Department of Meat Technology and Food Quality, Faculty of Food Sciences and Biotechnology, University of Life Sciences in Lublin, Skromna 8, 20-704 Lublin, Poland

Bibliografia

  • 1. Ahn D.-H., Shimada K., Takahashi K., Relationship between weakening of Z-disk band liberation of phospholipids during postmortem aging of pork and beef. J. Food Sci., 2003, 68, 94–98.
  • 2. Babick F., Hinze F., Ripperger S., Dependence of ultrasonic attenuation on the material. Properties colloids and surfaces A: Physicochemical and Engineering Aspects, 2000, 172, 33–46.
  • 3. Badyal J.P., Cameron A.M., Cameron N.R., Coe D.M., Cox R., Davis B.G., Oates L.J., Oye G., Steel P.G., A simple method for the quantitative analysis of resin bound thiol groups. Tetrahedron, 2001, 42, 8531–8533.
  • 4. Dolatowski Z.J., Effect of treatment with low frequency ultrasounds on the structure and qualitative traits of meat. Rozprawy Naukowe AR Lublin, 1999, 221 (in Polish).
  • 5. Dolatowski Z.J., Stadnik J., Stasiak D., Application of ultrasound in food technology. Acta Sci. Pol., Technol. Aliment., 2007, 6, 89–99.
  • 6. Dolatowski Z.J., Twarda J., Einfluss von Ultraschall auf das Wasserbindungsvermögen von Rindfleisch. Fleischwirtschaft, 2004, 12, 95–99.
  • 7. Ellman G.L., Tissue sulfhydryl groups. Archives Biochem. Biophys., 1959, 82, 70–77.
  • 8. Farouk M.M., Wieliczko K.J., Merts I., Ultra-fast freezing and low storage temperature are not necessary to maintain the functional properties of manufacturing beef. Meat Sci., 2003, 66, 171–179.
  • 9. Got F., Culioli J., Berge P., Vignon X., Astruc T., Quideau J.M., Lethiecq M., Effects of high-intensity high-frequency ultrasound on ageing rate, ultrastructure and some physico-chemical properties of beef. Meat Sci., 1999, 51, 35–42.
  • 10. Hopkins D.L., Littlefield P.J., Thompson J.M., A research note on factors affecting the determination of myofibrillar fragmentation. Meat Sci., 2000, 56, 19–22.
  • 11. Imm J.Y., Regenstein J.M., Interaction of commercial dairy proteins and chicken breast myosin in an emulsion system. J. Food Sci., 1997, 62, 967–972.
  • 12. John L, Cornforth D., Carpenter Ch.E., Sorheim O., Pettee B.C., Whittier D.R., Color and thiobarbituric acid values of cooked top sirloin steaks packaged in modified atmospheres of 80% oxygen, or 0.4% carbon monoxide, or vacuum. Meat Sci., 2005, 69, 441–449.
  • 13. Konieczny P. Uchman W., comparative characterization of surface hydrofobicity and other physico-chemical properties of selected protein preparations. EJPAU, 2002, Food Sci. Technol. 5(2), [art.10. www.ejpau.media.pl/volume5/issue2/food/art-10.html].
  • 14. Konieczny P., Surface hydrophobicity as a factor determining selected functional properties of protein preparations. Roczniki AR w Poznaniu. 2001, Rozpr. Nauk. 319 (in Polish).
  • 15. Koohmaraie M., Biochemical factors regulating the toughening and tenderization processes of meat. Meat Sci., 1996, 43, S193–201.
  • 16. Krusemark C.J., Ferguson J.T., Wegner C.D., Kelleher N.L., Belshaw P.J., Global amine and acid functional group modification in proteins. Anal. Chem., 2008, 80, 713–720.
  • 17. Latoch A., Dolatowski Z.J., Water retention in gels of sonicated beef homogenates. Inż. Rol., 2006, 82, 301–309 (in Polish).
  • 18. Latoch A., Sonication influence on myofibrillar gels propertiesduring beef ageing. Żywność. Nauka. Technologia. Jakość., 2007, 54, 365–371 (in Polish).
  • 19. Lieske B., Konrad G., A new approach to estimate surface hydrophobicity of proteins. Milchwissenschaft, 1994, 49, 663–666.
  • 20. Lyng J.G., Allen P., The influence of high intensity ultrasound baths on aspects of beef tenderness. J. Muscle Foods, 1997, 8, 237–249.
  • 21. Lyng J.G., Allen P., McKenna B.M., The effect on aspects of beef tenderness of pre- and post-rigor exposure to a high intensity ultrasound probe. J. Sci. Food Agric., 1998, 78, 308–314.
  • 22. Marcone F.M., Current challenges facing the further understanding of the interrelationship between protein structure and function. Food Res. Inter., 2000, 33, 635.
  • 23. Mason T.J., Paniwnyk L., Lorimer J.P., The uses of ultrasound in food technology. Ultrasonic Sonochem., 1996, 3, S253––S260.
  • 24. Olson D.G., Parrish Jr. F.C., Stromer M.H., Myofibril fragmentation and shear resistance of three bovine muscles during post mortem storage. J. Food Sci., 1976, 41, 1036–1041.
  • 25. Pohlman F.W., Dikeman M.E., Zayas J.F., The effect of low-intensity ultrasound treatment on shear properties, color stability and shelf-life of vacuum-packaged beef semitendinosus and biceps femoris muscles. Meat Sci., 1997, 45, 329–337(9).
  • 26. Pospiech E., Grześ B., Łyczyński A., Borzuta K., Szalata M., Mikołajczak B., Muscle proteins and their changes in the process of meat tenderization. Anim. Sci. Pap. Rep., 2003, suppl. 21(1), 133–151.
  • 27. Pospiech E., Grześ B., Mikołajczak B., Iwańska E., Łyczyński A., Proteins of meat as a potential indicator of its quality – a review. Pol. J. Food Nutr. Sci., 2007, 57, 11–16.
  • 28. Pospiech E., Grześ B., Selected cytoskeletal proteins and their role in determining functional properties of muscle tissue. Żywność. Nauka. Technologia. Jakość, 1997, 12, 5–12 (in Polish).
  • 29. Stadnik J., Dolatowski Z.J., Surface hydrophobicity of myofibrillar proteins of sonicated beef. Roczn. Inst. Przem. Mięsn. Tł., 2007, 45, 35–42 (in Polish).
  • 30. Takahashi K., Structural weakening of skeletal muscle tissue during post mortem ageing of meat: the non – enzymatic mechanism of meat tenderization. Meat Sci., 1996, 43, S67-S80.
  • 31. Wang H., Pato M.D., Shand P.J., Biochemical properties of natural actomyosin extracted from normal and pale, soft and exudative pork loin after frozen storage. J. Food Sci., 2005, 70, 390–398.

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Bibliografia

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