Skip to main content
Log in

Dynamical Changes of Beef Intramuscular Connective Tissue and Muscle Fiber during Heating and their Effects on Beef Shear Force

  • Original Paper
  • Published:
Food and Bioprocess Technology Aims and scope Submit manuscript

Abstract

Changes of meat shear force and its characteristics during cooking have been extensively studied, but great variability existed due to the cooking method among different studies. This study was designed to focus on the dynamic changes of beef intramuscular connective tissue (IMCT) and muscle fiber during water-bath heating and their effects on beef shear force. At 4 d postmortem, beef semitendinosus muscles were divided into 11 steaks and then cooked respectively to an internal temperature of 40, 50, 55, 60, 65, 70, 75, 80, 85, and 90°C (the remainder was not cooked as control). Collagen content and its solubility, transition temperature of perimysia and endomysia, fiber diameter, and Warner–Bratzler shear force values (WBSF) were determined. The results showed that fiber diameter decreased gradually during cooking, concomitant with the increases in filtering residue and WBSF. The maximum transition temperature (T max) of endomysial components was lower than that of perimysial components (50.2 vs. 65.2°C). Muscle fiber and IMCT (especially perimysia) shrank during cooking, resulting in the increase of WBSF when the internal temperature was lower than 75°C, but further cooking led to the disintegration of perimysial structure, lowing up the increase of WBSF between 75 and 90°C. For beef semitendinosus muscle, the internal temperature of 65°C is a critical cooking point where meat gets tougher.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3

Similar content being viewed by others

References

  • American Meat Science Association (1995). Research guidelines for cookery, sensory evaluation and instrumental tenderness measurements of fresh meat. Chicago: National Live Stock and Meat Board.

    Google Scholar 

  • Bergman, I., & Loxley, R. (1963). Two improved and simplified methods for spectrophotometric determination of hydroxyproline. Analytical Chemistry, 35, 1961–1965. doi:10.1021/ac60205a053.

    Article  CAS  Google Scholar 

  • Bouton, P. E., & Harris, P. V. (1972). The effects of some postslaughter treatments on the mechanical properties of bovine and ovine muscle. Journal of Food Science, 37, 539–543. doi:10.1111/j.1365-2621.1972.tb02687.x.

    Article  Google Scholar 

  • Bouton, P. E., Harris, P. V., & Ratcliff, D. (1981). Effect of cooking temperature and time on the shear properties of meat. Journal of Food Science, 46, 1082–1087. doi:10.1111/j.1365-2621.1981.tb02996.x.

    Article  Google Scholar 

  • Christensen, M., Purslow, P. P., & Larsen, L. M. (2000). The effect of cooking temperature on mechanical properties of whole meat, single muscle fibers and perimysial connective tissue. Meat Science, 55, 301–307. doi:10.1016/S0309-1740(99)00157-6.

    Article  Google Scholar 

  • Davey, C. L., & Gilbert, K. V. (1974). Temperature dependent cooking toughness in beef. Journal of the Science of Food and Agriculture, 25, 931–938. doi:10.1002/jsfa.2740250808.

    Article  CAS  Google Scholar 

  • Fang, S. H., Nishimura, T., & Takahashi, K. (1999). Relationship between development of intramuscular connective tissue and toughness of pork during growth of pigs. Journal of Animal Science, 77, 120–130.

    CAS  Google Scholar 

  • Flint, F. O., & Pickering, K. (1984). Demonstration of collagen in meat products by an improved picro-sirius red polarization method. Analyst (Lond), 109, 1505–1508. doi:10.1039/an9840901505.

    Article  CAS  Google Scholar 

  • Hill, F. (1966). The solubility of intramuscular collagen in meat animals of various ages. Journal of Food Science, 31, 161–166. doi:10.1111/j.1365-2621.1966.tb00472.x.

    Article  CAS  Google Scholar 

  • Kopp, J., & Bonnet, M. (1987). Stress–strain and isometric tension measurements in collagen. In A. M. Pearson, T. M. Dutson, & A. J. Baily (Eds.), Advances in meat research vol. 4: Collagen as a food (pp. 163–185). New York: Van Nostrand.

    Google Scholar 

  • Lawrie, R. A., & Ledward, D. A. (2006). Lawrie’s meat science (17th ed.). Cambridge: Woodhead Publishing.

    Google Scholar 

  • Light, N., & Champion, A. E. (1984). Characterization of muscle epimysium, perimysium and endomysium collagens. Biochemical Journal, 219, 1017–26.

    CAS  Google Scholar 

  • López Osornio, M. M., Hough, G., Salvador, A., Chambers IV, E., McGraw, S., & Fiszman, S. (2008). Beef’s optimum internal cooking temperature as seen by consumers from different countries using survival analysis statistics. Food Quality and Preference, 19, 12–20.

    Article  Google Scholar 

  • Martens, H., Stabussvik, E., & Martens, M. (1982). Texture and color changes in meat during cooking related to thermal denaturation of muscle proteins. Journal of Texture Studies, 13, 291–309. doi:10.1111/j.1745-4603.1982.tb00885.x.

    Article  Google Scholar 

  • Nishimura, T., Hattori, A., & Takahashi, K. (1999). Structural changes in intramuscular connective tissue during the fattening of Japanese Black cattle, effect of marbling on beef tenderization. Journal of Animal Science, 77, 93–104.

    CAS  Google Scholar 

  • Powell, T. H., Dikeman, M. E., & Hunt, M. C. (2000). Tenderness and collagen composition of beef semitendinosus roasts cooked by conventional convective cooking and modeled, multistage convective cooking. Meat Science, 55, 421–425. doi:10.1016/S0309-1740(99)00171-0.

    Article  Google Scholar 

  • Purslow, P. P. (1999). The intramuscular connective tissue matrix and cell–matrix interactions in relation to meat toughness. In Proceedings of the 45th International Congress of Meat Science and Technology, Yokohama, Japan (pp. 210–219).

  • Torrescano, G., Sánchez, E. A., Giménez, B., Roncalés, P., & Beltrán, J. A. (2003). Shear values of raw samples of 14 bovine muscles and their relation to muscle collagen characteristics. Meat Science, 64, 85–91. doi:10.1016/S0309-1740(02)00165-1.

    Article  Google Scholar 

  • Wright, D. J., & Wilding, P. (1984). Differential scanning calorimetric study of muscle and its proteins: Myosin and its subfragments. Journal of the Science of Food and Agriculture, 35, 357–372. doi:10.1002/jsfa.2740350317.

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to G. H. Zhou.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Li, C.B., Zhou, G.H. & Xu, X.L. Dynamical Changes of Beef Intramuscular Connective Tissue and Muscle Fiber during Heating and their Effects on Beef Shear Force. Food Bioprocess Technol 3, 521–527 (2010). https://doi.org/10.1007/s11947-008-0117-3

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11947-008-0117-3

Keywords

Navigation