Effects of muscle shortening and proteolysis on Warner-Bratzler shear force in beef longissimus and semitendinosus

Meat Science

Volumn 68, Issue 3, 2004, Pages 497-505

  Hwang, I H ^a   Park, B Y ^a   Cho, S H ^a   Lee, J M ^a  

^a National Institute of Animal Science   (South Korea)

Author keywords

Beef; Proteolysis; Rigor temperature; Sarcomere length; WB shear force

Indexed keywords

BEEF; PROTEOLYSIS; RIGOR TEMPERATURE; SARCOMORE LENGTH;

CALCIUM; ENZYMES; FOOD PRODUCTS; IONS; MUSCLE; PH EFFECTS; SHEAR STRENGTH; THERMAL EFFECTS;

PROTEINS;

EID: 5444247716     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2004.04.002     Document Type: Article

References (38)

1. Bailey, A. J., & Light, N. D. (1989). Connective tissue in meat and meat products. London: Elsevier Science Publisher.
2. Bendall, J. R. (1973). Postmortem changes in muscle. In O. H. Bourne (Ed.), The structure and function of muscle (pp. 244-306). New York: Academic Press.
3. Bendall, J. R. (1976). Electrical stimulation of rabbit and lamb carcasses. Journal of the Science of Food and Agriculture, 27, 819-826.
4. Celio, M. R., Pauls, T. L., & Schwaller, B. (1996). Guidebook to the calcium-binding proteins. New York: Oxford University Press Inc.
5. Cornforth, D. P., Pearson, A. M., & Merkel, R. A. (1980). Relationship of mitochondria and sarcoplasmic reticulum to cold shortening. Meat Science, 4, 103-121.
6. Cross, H. R., West, R. L., & Dutson, T. R. (1981). Comparison of methods for measuring sarcomere length in beef semitendinosus muscle. Meat Science, 5, 261-266.
7. Devine, C. E., Payne, S. R., Peachey, B. M., Lowe, T. E., Ingram, J. R., & Cook, C. J. (2002). High and low rigor temperature effects on sheep meat tenderness and ageing. Meat Science, 60, 141-146.
8. Devine, C. E., Wahlgren, N. M., & Tornberg, E. (1999). Effect of rigor temperature on muscle shortening and tenderisation of restrained and unrestrained beef m. longissimus thoracicus and lumborum. Meat Science, 51, 61-72.
9. Dransfield, E. (1994). Optimisation of tenderisation, ageing and tenderness. Meat Science, 36, 105-121.
10. Dransfield, E. (1999). Meat tenderness - The μ-calpain hypothesis. In Proceedings 45th international congress of meat science and technology (pp. 220-228), Yokohama, Japan.
11. Dransfield, E., Wakefield, D. K., & Parkman, I. D. (1992). Modeling post-mortem tenderisation - I: Texture of electrically stimulated and non-stimulated beef. Meat Science, 31, 57-73.
12. Geesink, G. H., & Koohmaraie, M. (2000). Ionic strength-induced inactivation of μ-calpain in postmortem muscle. Journal of Animal Science, 78, 2336-2343.
13. Hertzman, C., Olsson, U., & Tornberg, E. (1993). The influence of high temperature, type of muscle and electrical stimulation on the course of rigor, ageing and tenderness of beef muscles. Meat Science, 35, 119-141.
14. Heukeshove, J., & Dernick, R. (1985). Simplified method for silver staining of proteins in polyacrylamide gels and the mechanisms of silver staining. Electrophoresis, 6, 103-112.
15. Hopkins, D. L., & Thompson, J. M. (2001). Inhibition of protease activity 2. Degradation of myofibrillar proteins, myofibril examination and determination of free calcium levels. Meat Science, 59, 199-209.
16. Hopkins, D. L., & Thompson, J. M. (2002). The relationship between post-mortem calcium concentration or pH and indicators of proteolysis in ovine muscle. Meat Science, 61, 411-414.
17. Hwang, I. H., & Thompson, J. M. (2001a). The effect of time and type of electrical stimulation on the calpain system and meat tenderness in beef longissimus dorsi muscle. Meat Science, 58, 135-144.
18. Hwang, I. H., & Thompson, J. M. (2001b). The interaction between pH and temperature decline early postmortem on the calpain system and objective tenderness in electrically stimulated beef longissimus dorsi muscle. Meat Science, 58, 167-174.
19. Hwang, I. H., Devine, C. E., & Hopkins, D. L. (2003). The biochemical and physical effects of electrical stimulation on beef and sheep meat tenderness. Meat Science, 65, 677-691.
20. Jeacocke, R. E. (1977). The temperature dependence of anaerobic glycolysis in beef muscle held in a linear temperature gradient. Journal of the Science of Food Agriculture, 28, 551-556.
21. Jeacocke, R. E. (1993). The concentrations of free magnesium and free calcium ions both increase in skeletal muscle fibres entering rigor mortis. Meat Science, 35, 27-45.
22. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
23. Locker, R. H., & Wild, D. J. C. (1984). "Aging" of cold shortened meat depends on the criterion. Meat Science, 10, 235-238.
24. Locker, R. H., & Hagyard, C. J. (1963). A cold shortening effect in beef muscles. Journal of the Science of Food and Agriculture, 14, 787-793.
25. Nuss, J. I., & Wolfe, F. H. (1980). Effect of post-mortem storage temperatures on isometric tension pH, ATP, glycogen and glucose-6-phosphate for selected bovine muscles. Meat Science, 5, 201-213.
26. Offer, G., & Cousins, T. (1992). The mechanism of drip production: Formation of two compartments of extracellular space in muscle post mortem. Journal of the Science of Food and Agriculture, 58, 107-116.
27. Pearson, A. M., & Dutson, T. R. (1985). Scientific basis for electrical stimulation. In A. M. Pearson & T. R. Dutson (Eds.), Advanced in meat research - Electrical stimulation (pp. 185-218). New York: Van Nostrand Reinhold Company.
28. Rowe, R. W. D. (1977). The effect of pre-rigor stretch and contraction on the post-rigor geometry of meat samples in relation to meat toughness. Meat Science, 1, 205-218.
29. SAS. (1997). Applied statistics and the SAS programming language. Cary, NC, USA: SAS Institute INC.
30. Simmons, N. J., Cairney, J. M., & Daly, C. C. (1997). Effect of prerigor temperature and muscle prestraint on the biophysical properties of meat tenderness development. In Proceedings 43rd international congress of meat science and technology (pp. 608-609), Auckland, New Zealand.
31. Simmons, N. J., Singh, K., Dobbie, P., & Devine, C. E. (1996). The effect of prerigor holding temperature on calpain and calpastatin activity and meat tenderness. In Proceedings 42nd International congress of meat science and technology (pp. 414-415), Lillehammer, Norway.
32. Smulders, F. J. M. Marsh, B. B., Swartz, D. R., Russell, R. L., & Hoenecke, M. E. (1990). Beef tenderness and sarcomere length. Meat Science, 28, 349-363.
33. Somlyo, A. V., Gonzalez-Serratos, H., Shuman, H., McClellan, G., & Somlyo, A. P. (1981). Calcium release and ionic changes in the sacoplasmic reticulum of tetanized muscle: An electron-probe study. Journal of Cell Biology, 90, 577-594.
34. Tornberg, E. (1996). Biophysical aspects of meat tenderness. Meat Science, 43, S175-S191.
35. Westerblad, H., & Allen, D. G. (1993). The influence of intracellular pH on contraction, relaxation and [Ca2+]I in intact single fibres from mouse muscle. Journal of Physiology, 466, 611-628.
36. Wheeler, T. D., & Koomaraie, M. (1999). The extent of proteolysis is independent of sarcomere length in lamb longissimus and psoas major. Journal of Animal Science, 77, 2444-2451.
37. Wheeler, T. L., Shackelford, S. D., & Koohmaraie, M. (2000). Relationship of beef longissimus tenderness classes to tenderness of gluteus medius, semimembranosus, and biceps femoris. Journal of Animal Science, 78, 2856-2861.
38. Whiting, R. C. (1980). Calcium uptake by bovine muscle mitochondria and sarcoplasmic reticulum. Journal of Food Science, 45, 288-292.