Distribution of optical scattering properties in four beef muscles

  • Jinjun Xia
  • Amanda Weaver
  • David E. Gerrard
  • Gang Yao
Original Paper
First Online:
Received:
Accepted:

Abstract

The objective of this study was to determine the influence of the mechanisms regulating tenderness on optical scattering properties of beef. Optical scattering properties of four beef muscles with different amounts of connective tissue and varying sarcomere lengths across a range of aging periods were determined. The optical scattering coefficient of beef muscles were measured based on a diffusive fitting of spatially resolved reflectance measurements. As a reference to beef tenderness, Warner-Bratzler shear forces were also measured in this study. Variation in muscle composition resulted in a range of optical scattering properties across muscles. Our results implied that connective tissue and sarcomere structure have different effects on the optical scattering properties of muscle. In addition, proteolysis of muscle proteins significantly changes the optical scattering properties. These results provide useful information in understanding the originations of optical scattering in beef.

Keywords

Beef Tenderness Aging Fiber optics Optical scattering 
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Notes

Acknowledgement

This project was funded in part by the National Research Initiative of the USDA Cooperative State Research, Education and Extension Service under grant number 2006-35503-17619.

References

  1. 1.
    E. Dransfield Evidence of consumer reaction to meat of different origins. in The long-term definition of meat quality: controlling the variability of quality in beef, veal, pigment and lamb, ed. by G. Harrington (Commission for the European Communities, Brussels, 1985), p. 45Google Scholar
  2. 2.
    K.L. Huffman, M.F. Miller, L.C. Hoover, C.K. Wu, H.C. Brittin, C.B. Ramsey, Effect of beef tenderness on consumer satisfaction with steaks consumed in the home and restaurant. J. Anim. Sci. 74, 91–97 (1996)Google Scholar
  3. 3.
    D.L. Roeber, P.D. Mies, C.D. Smith, K.E. Belk, G.C. Smith, T.G. Field, J.D. Tatum, J.A. Scanga, National Market Cow and Bull Beef Quality Audit—(1999) 2000 Research Report, (The Department of Animal Sciences, Colorado State University, 2000)Google Scholar
  4. 4.
    S.D. Shackelford, T.L. Wheeler, M.K. Meade, J.O. Reagan, B.L. Byrnes, M. Kooharaie, Consumer impressions of tender select beef. J. Anim. Sci. 79, 2605–2614 (2001)Google Scholar
  5. 5.
    K.L. Lusk, J.A. Fox, T.C. Schroeder, J. Mintert, M. Koohmaraie, In-store valuation of steak tenderness. Am. J. Agric. Econ. 83, 539–550 (2001)CrossRefGoogle Scholar
  6. 6.
    H.J. Swatland, Physical measurements of meat quality: optical measurements, pros and cons. Meat Sci. 36, 251–259 (1994)CrossRefGoogle Scholar
  7. 7.
    S.D. Shackelford, T.L. Wheeler, M. Koohmaraie, Tenderness classification of beef: II. Design and analysis of a system to measure beef longissimus shear force under commercial processing conditions. J. Anim. Sci. 77, 1474–1481 (1999)Google Scholar
  8. 8.
    D.J. Vote, K.E. Belk, J.D. Tatum, J.A. Scanga, G.C. Smith, Online prediction of beef tenderness using a computer vision system equipped with a BeefCam module. J. Anim. Sci. 81, 457–465 (2003)Google Scholar
  9. 9.
    K.I. Hildrum, T. Isaksson, T. Naes, B.N. Nilsen, M. Rodbotten, P. Lea, Near-infrared reflectance spectroscopy in the prediction of sensory properties of beef. J. Near Infrared Spectrosc. 3, 81–87 (1995)Google Scholar
  10. 10.
    G. Yao, J. Xia, Optical characterization of muscle. Proc. SPIE 5996, 356–363 (2005)Google Scholar
  11. 11.
    J. Xia, A. Weaver, D.E. Gerrard, G. Yao, Monitoring sarcomere structure changes in whole muscle using diffuse light reflectance. J. Biomed. Opt. 11, 040504 (2006)CrossRefGoogle Scholar
  12. 12.
    J. Xia, E.P. Berg, J.W. Lee, G. Yao, Characterizing beef muscles with optical scattering and absorption coefficients in VIS−NIR region. Meat Sci. 75, 78–83 (2007)CrossRefGoogle Scholar
  13. 13.
    M. Koohmaraie, M.P. Kent, S.D. Shackelford, E. Veiseth, T.L. Wheeler, Meat tenderness and muscle growth: is there any relationship? Meat Sci. 62, 345–352 (2002)CrossRefGoogle Scholar
  14. 14.
    J. Xia, A. Weaver, D. Gerrard, G. Yao, Heating induced optical property changes in beef muscles. J. Food Eng. 84, 75–81 (2008)CrossRefGoogle Scholar
  15. 15.
    S.P. Lin, L.H. Wang, S.L. Jacques, F.K. Tittel, Measurement of tissue optical properties by the use of oblique-incidence optical fiber reflectometry. Appl. Opt. 36, 136–143 (1997)CrossRefGoogle Scholar
  16. 16.
    G. Marquez, L.V. Wang, S.P. Lin, J.A. Schwartz, S.L. Thomsen, Anisotropy in the absorption and scattering spectra of chicken breast tissue. Appl. Opt. 37, 798–804 (1998)CrossRefGoogle Scholar
  17. 17.
    N.S. Shelud’ko, Optical properties of myofibril and actomyosin suspensions. 1. Angular dependence of light scattering by myofibril suspensions and its changes under myofibril contraction. Biochim. Biophys. Acta 1038(3), 315–321 (1990)Google Scholar
  18. 18.
    I.S. Saidi, S.L. Jacques, F.K. Tittel, Mie and Rayleigh modeling of visible-light scattering in neonatal skin. Appl. Opt. 34, 7410–7418 (1995)Google Scholar
  19. 19.
    H.K. Herring, R.G. Cassens, E.J. Briskey, Sarcomere length of frees and restrained bovine muscles at low temperature as related to tenderness. J. Sci. Food Agric. 16, 379–384 (1965)CrossRefGoogle Scholar
  20. 20.
    R.H. Locker, Degree of muscular contraction as a factor in tenderness of beef. J. Food Sci. 25, 304–307 (1960)CrossRefGoogle Scholar
  21. 21.
    M.S. Rhee, T.L. Wheeler, S.D. Shackelford, M. Koohmaraie, Variation in palatability and biochemical traits within and among eleven beef muscles. J. Anim. Sci. 82, 534–550 (2004)Google Scholar
  22. 22.
    G.D. Stolowski, B.E. Baird, R.K. Miller, J.W. Savell, A.R. Sams, J.F. Taylor, J.O. Sanders, S.B. Smith, Factors influencing the variation in tenderness of seven major beef muscles from three Angus and Brahman breed crosses. Meat Sci. 73, 475–483 (2006)CrossRefGoogle Scholar
  23. 23.
    R.J. Mccormick, Extracellular modifications to muscle collagen: implications for meat quality. Poult. Sci. 78, 785–791 (1999)Google Scholar
  24. 24.
    B.B. Marsh, N.G. Leet, Studies in meat tenderness. III. The effects of cold shortening on tenderness. J. Food Sci. 31, 450–459 (1966)CrossRefGoogle Scholar
  25. 25.
    M. Koohmaraie, The role of Ca2+-dependent proteases (calpains) in postmortem proteolysis and meat tenderness. Biochimie 74, 239–245 (1992)CrossRefGoogle Scholar
  26. 26.
    M. Koohmaraie, Muscle proteinases and meat aging. Meat Sci. 36, 93–104 (1994)CrossRefGoogle Scholar
  27. 27.
    E. Veiseth, S.D. Shackelford, T.L. Wheeler, M. Koohmaraie, Effect of postmortem storage on m-calpain and μ-calpain in ovine skeletal muscle. J. Anim. Sci. 79, 1502–1508 (2001)Google Scholar

Copyright information

© Springer Science+Business Media, LLC 2008

Authors and Affiliations

  • Jinjun Xia
    • 1
  • Amanda Weaver
    • 2
  • David E. Gerrard
    • 3
  • Gang Yao
    • 1
  1. 1.Department of Biological EngineeringUniversity of Missouri-ColumbiaColumbiaUSA
  2. 2.Department of Animal ScienceSouth Dakota State UniversityBrookingsUSA
  3. 3.Department of Animal SciencePurdue UniversityWest LafayetteUSA

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