Color — its basis and importance

  • D. Cornforth
Part of the Advances in Meat Research book series (ADMERE, volume 9)

Abstract

Meat color is the primary criterion by which consumers evaluate meat quality and acceptability. Consumers prefer bright-red fresh meats, brown or gray-colored cooked meats and pink cured meats. Any deviations may result in reduced sales, consumer complaints and returned products. The relatively short shelf-life of fresh meats is the single greatest concern to retail meat markets. When brown metmyoglobin reaches 30–40% of total pigments on the surface of fresh retail beef, consumers make a nopurchase decision (Greene et al., 1971). It is estimated that 4–10% of retail meats are either discounted, processed into hamburger, or even discarded due to brown-color development. Efforts continue to extend fresh meat color stability through improved sanitation and antimicrobial treatments, temperature control, packaging, and also through diet modification and improved breeding and handling of live animals.

Keywords

Chrome Arsenate Sodium Chloride Cysteine Respiration 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Aalhus, J.L., Price, M.A., Shand, P.J. and Hawrysh, Z.L. (1991) Endurance-exercised growing sheep. II. Tenderness increase and change in meat quality. Meat Sci. 29, 57.CrossRefGoogle Scholar
  2. Agullo, E., Centurion, M.E., Ramos, V. and Bianchi, M.A. (1990) Determination of total pigments in red meats. J. Food Sci. 55, 250.CrossRefGoogle Scholar
  3. Ahn, D.U. and Maurer, A.J. (1989a) Effects of added nitrite, sodium chloride, and phosphate on color, nitrosoheme pigment, total pigment and residual nitrite in oven-roasted turkey breast. Poult. Sci. 68, 100.CrossRefGoogle Scholar
  4. Ahn, D.U. and Maurer, A.J. (1989b) Effects of sodium chloride, phosphate, and dextrose on the heat stability of purified myoglobin, hemoglobin, and cytochrome c. Poult. Sci. 68, 1218.CrossRefGoogle Scholar
  5. Ahn, D.U. and Maurer, A.J. (1990a) Poultry meat color. Kinds of heme pigments and concentrations of the ligands. Poult. Sci. 69, 157.CrossRefGoogle Scholar
  6. Ahn, D.U. and Maurer, A.J. (1990b) Poultry meat color. Heme-complex-forming ligands and color of cooked turkey breast meat. Poult. Sci. 69, 1769.CrossRefGoogle Scholar
  7. Al-Shaibani, K.A., Price, R.J. and Brown, W.D. (1977) Purification of metmyoglobin reductase from bluefin tuna. J. Food Sci. 42, 1013.CrossRefGoogle Scholar
  8. Andersen, H.J., Bertelsen, G and Skibsted, L.H. (1989) Colour stability of minced beef. Ultraviolet barrier in packaging material reduces light-induced discoloration of frozen products during display. Meat Sci. 25, 155.CrossRefGoogle Scholar
  9. Anderson, M.E., Marshall, R.T., Stringer, W.C. and Naumann, H.D. (1979) Microbial growth on plate beef during extended storage after washing and sanitizing. J. Food Prot. 42, 389.Google Scholar
  10. Anson, M.L. and Mirsky, A.E. (1928) On hemochromogen. J. Gen. Phys. 12, 273.CrossRefGoogle Scholar
  11. Antonini, E. and Brunori, M. (1971) Structure of hemoglobin and myoglobin, in Hemoglobin and Myoglobin in Their Reactions with Ligands (eds A. Neuberger and E.L. Tatum), North Holland Publishing, Amsterdam, p. 19.Google Scholar
  12. Appel, P. and Brown, W.D. (1971) Stability characteristics of deuterated myoglobin. Biopolymers 10, 2309.CrossRefGoogle Scholar
  13. Arihara, K., Itoh, M. and Kondo, Y. (1989a) Detection of cytochrome b5 in bovine skeletal muscle by electrophoretic immunoblotting technique. Jpn J. Zootech. Sci. 60, 97.Google Scholar
  14. Arihara, K., Itoh, M. and Kondo, Y. (1989b). Detection of cytochrome b5 reductase. Jpn. J. Zootech. Sci. 60, 46.Google Scholar
  15. Ashmore, C.R. and Doerr, L. (1971) Comparative aspects of muscle fiber types in different species. Exp. Neurol. 31, 408.CrossRefGoogle Scholar
  16. Ashmore, C.R., Doerr, L., Foster, G. and Carroll, F. (1971) Respiration of mitochondria isolated from dark-cutting beef. J. Anim. Sci. 33, 574.Google Scholar
  17. Ashmore, C.R., Parker, W. and Doerr, L. (1972) Respiration of mitochondria isolated from dark-cutting beef: Post-mortem changes. J. Anim. Sci. 34, 46.Google Scholar
  18. Ashmore, C.R., Carroll, F., Doerr, L., Tompkins, G., Stokes, H. and Parker, W. (1973) Experimental prevention of dark-cutting meat. J. Anim. Sci. 36, 33.Google Scholar
  19. Atkinson, J.L., and Follett, M.J. (1973) Biochemical studies on the discoloration of fresh meat. J. Food Technol. 8, 51.CrossRefGoogle Scholar
  20. Aversano, R.W. (1984) Food preservation composition. US Patent No. 4,476,112.Google Scholar
  21. Bala, K., Marshall, R.T., Stringer, W.C. and Naumann, H.D. (1977) Changes of color of aqueous beef extract caused by Pseudomonas fragi. J. Food Prot. 40, 824.Google Scholar
  22. Banks, J.G., Dalton, H.K., Nychas, G.J. and Board, R.G. (1985) Sulfite, an elective agent in the microbiological and chemical changes occurring in uncooked comminuted meat products. J. Appl. Biochem. 7, 161.Google Scholar
  23. Barnard, R.J., Edgerton, V.R. and Peter, J.B. (1970) Effect of exercise on skeletal muscle, biochemical and histochemical properties. J. Appl. Physiol. 28, 762.Google Scholar
  24. Beecher, G.R., Cassens, R.G., Hoekstra, W.G. and Briskey, E.J. (1965) Red and white fiber content and associated post-mortem properties of seven porcine muscles. J. Food Sci. 30, 969.CrossRefGoogle Scholar
  25. Bendall, J.R. (1972) Consumption of oxygen by the muscles of beef animals and related species, and its effect on the colour of meat. I. Oxygen consumption in pre-rigor muscle. J. Sci. Food Agric. 23, 61.CrossRefGoogle Scholar
  26. Bendall, J.R. and Taylor, A.A. (1972) Consumption of oxygen by the muscles of beef animals and related species. II. Consumption of oxygen by post-rigor muscle. J. Sci. Food Agric. 23, 707.CrossRefGoogle Scholar
  27. Benedict, R.C., Strange, E.D., Palumbo, S.E. and Swift, C.W. (1975) Use of in-package controlled atmospheres for extending the shelf-life of meat products. J. Agric. Food Chem. 23, 1208.CrossRefGoogle Scholar
  28. Bernofsky, C., Fox, J.B. and Schweigert, B.S. (1959) Biochemistry of myoglobin. VI. The effects of low dosage gamma irradiation on beef myoglobin. Arch. Biochem. Biophys. 80, 9.CrossRefGoogle Scholar
  29. Bevilacqua, A.E. and Zaritzky, N.E. (1986) Rate of pigment modifications in packaged refrigerated beef using reflectance spectrophotometry. Food Proc. Preserv. 10, 1.CrossRefGoogle Scholar
  30. Biemuller, G.W., Carpenter, J.A. and Reynolds, A.E. (1973) Reduction of bacteria on pork carcasses. J. Food Sci. 38, 261.CrossRefGoogle Scholar
  31. Binkerd, E.F. and Kolari, O.E. (1975) The history and use of nitrate and nitrite in the curing of meat. Food Cosmet. Toxicol. 13, 655.CrossRefGoogle Scholar
  32. Bodwell, C.E., Pearson, A.M. and Fennell, R.A. (1965) Post-mortem changes in muscle. III. Histochemical observations in beef and pork. J. Food Sci. 30, 944.CrossRefGoogle Scholar
  33. Borchert, L.L. and Briskey, E.J. (1964) Prevention of pale, soft, exudative porcine muscle through partial freezing with liquid nitrogen post-mortem. J. Food Sci. 29, 203.CrossRefGoogle Scholar
  34. Bowen, W.J. (1949) The absorption spectra and extinction coefficients of myoglobin. J. Biol. Chem. 179, 235.Google Scholar
  35. Braddock, R.J. and Dugan, L.R., Jr. (1969) Moisture effect on the nitric oxide pigments in freeze-dried beef. Food Technol. 23, 1085.Google Scholar
  36. Briskey, E.J. (1964). Etiological status and associated studies of pale, soft, exudative porcine musculature. Adv. Food Res. 13, 89.CrossRefGoogle Scholar
  37. Briskey, E.J. and Sayre, R.N. (1964). Muscle protein extractability as influenced by conditions of post-mortem glycolysis. Proc. Soc. Exptl. Biol. Med. 115, 823.Google Scholar
  38. Briskey, E.J. and Wismer-Pedersen, J. (1961) Biochemistry of pork muscle structure. I. Rate of anaerobic glycolysis and temperature change versus the apparent structure of muscle tissue. J. Food Sci. 26, 297.CrossRefGoogle Scholar
  39. Briskey, E.J., Bray, R.W., Hoekstra, W.G., Phillips, P.H. and Grummer, R.H. (1959) The effect of exhaustive exercise and high sucrose regimen on certain chemical and physical pork ham muscle characteristics. J. Anim. Sci. 18, 173.Google Scholar
  40. Briskey, E.J., Hoekstra, W.G., Bray, R.W. and Grummer, R.H. (1960) A comparison of certain physical and chemical characteristics of eight pork muscles. J. Anim. Sci. 19, 214.Google Scholar
  41. Brooke, M.H. and Engel, W.K. (1966) Nitro blue tetrazolium. Selective binding within striated muscle fibers. Neurology 16, 799.CrossRefGoogle Scholar
  42. Brooks, J. (1929) Post-mortem formation of methaemoglobin in red muscle. Biochem. J. 23, 1391.Google Scholar
  43. Brooks, J. (1938) Color of meat. Food Res. 3, 75.CrossRefGoogle Scholar
  44. Broumand, H., Ball, C.O. and Stier, E.F. (1958) Factors affecting the quality of prepackaged meat. II. E. Determining the proportions of heme derivatives in fresh meat. Food Technol. 12, 65.Google Scholar
  45. Brown, W.D. and Dolev, A. (1963) Autoxidation of beef and tuna oxymyoglobins. J. Food Sci., 28, 207.CrossRefGoogle Scholar
  46. Brown, W.D. and Mebine, L.B. (1969) Autooxidation of oxymyoglobins. J. Biol. Chem. 244, 6696.Google Scholar
  47. Brown, W.D. and Snyder, H.E. (1969) Non-enzymatic reduction and oxidation of myoglobin and hemoglobin by nicotinamide adenine dinucleotides and flavins. J. Biol. Chem. 244, 6702.Google Scholar
  48. Brown, W.D. and Tappel, A.L. (1957) Identification of the pink pigment of canned tuna. Food Res. 22, 214.CrossRefGoogle Scholar
  49. Butler, O.D., Bratzler, L.J. and Mallmann, W.L. (1953). The effect of bacteria on the color of prepackaged retail beef cuts. Food Technol. 7, 397.Google Scholar
  50. Calkins, C.R., Savell, J.W., Smith, G.C and Murphey, C.E. (1980) Quality-indicating characteristics of beef as affected by electrical stimulation and postmortem chilling time. J. Food Sci. 45, 1330.CrossRefGoogle Scholar
  51. Calkins, C.R., Goll, S.J. and Mandigo, R.W. (1986) Retail display lighting type and fresh pork color. J. Food Sci. 51, 1141.CrossRefGoogle Scholar
  52. Cassens, R.G. (1970) Morphology of muscle as a food, in The Physiology and Biochemistry of Muscle as a Food, 2., Ch. 33 (eds E.J. Briskey, R.G. Cassens and B.B. Marsh), University of Wisconsin Press, Madison, Wisconsin, p. 692.Google Scholar
  53. Cheah, K.S. and Cheah, A.M. (1971) Post-mortem changes in structure and function of ox muscle mitochondria. I. Electron microscopic and polarographic investigations. J. Bioenergetics 2, 85.CrossRefGoogle Scholar
  54. Cheng, C. (1987) Process for prepackaging fresh meat. US Patent No. 4,683,139.Google Scholar
  55. Clark, D.S. and Lentz, C.P. (1972) Use of carbon dioxide for extending shelf-life of prepackaged beef. Can. Inst. Food Sci. Technol. J. 5, 175.Google Scholar
  56. Cooper, C.C., Cassens, R.G. and Briskey, E.J. (1969) Capillary distribution and fiber characteristics in skeletal muscle of stress-susceptible animals. J. Food Sci. 34, 299.CrossRefGoogle Scholar
  57. Cornforth, D.P. and Egbert, W.R. (1985) Effect of rotenone and pH on the color of prerigor muscle. J. Food Sci., 50, 34.CrossRefGoogle Scholar
  58. Cornforth, D.P., Egbert, W.R. and Sisson, D.V. (1985) Effects of low temperature and increased oxygen concentration on color of intact prerigor muscle. J. Food Sci. 50, 1021.CrossRefGoogle Scholar
  59. Cornforth, D.P., Vahabzadeh, F., Carpenter, C.E. and Bartholomew, D.T. (1986) Role of reduced hemochromes in pink color defect of cooked turkey rolls. Food Sci. 51, 1132.CrossRefGoogle Scholar
  60. Cornforth, D.P., Calkins, C.R. and Faustman, C. (1991) Methods for identification and prevention of pink color in cooked meat. Proc. Recip. Meat Conf. 44, 53.Google Scholar
  61. Cornforth, D.P., Ghorpade, V.M. and Kim, Y. (1993) Effects of various fresh meat storage methods on color of cooked ground pork. J. Muscle Foods 4, 57.CrossRefGoogle Scholar
  62. Coyne, F.P. (1932) The effect of carbon dioxide on bacterial growth with special reference to the preservation of fish. Part I. J. Soc. Chem. Ind. 51 119T.Google Scholar
  63. Coyne, F.P. (1933) The effect of carbon dioxide on bacterial growth with special reference to the preservation of fish. Part II. Gas storage of fresh fish. J. Soc. Chem. Ind. 52, 19T.CrossRefGoogle Scholar
  64. Crenwelge, D.D., Terrell, R.N., Dutson, T.R., Smith, G.C. and Carpenter, Z.L. (1984) Effects of time postmortem of electrical stimulation and post-mortem chilling method on pork quality and palatability traits. J. Food Sci. 49, 294.CrossRefGoogle Scholar
  65. Daun, H., Solberg, M., Franke, W. and Gilbert, S. (1971) Effect of oxygen-enriched atmospheres on storage quality of packaged fresh meat. J. Food Sci. 36, 1011.CrossRefGoogle Scholar
  66. Davey, C.L. and Gilbert, K.V. (1976) Thaw contracture and the disappearance of adenosine-triphosphate in frozen lamb. J. Sci. Food Agric. 27, 1085.CrossRefGoogle Scholar
  67. Davey, C.L. and Graafhuis, A.E. (1981) Early identification of the DFD condition in prerigor beef carcasses, in The Problem of Dark-Cutting in Beef (eds D.E. Hood and P.Y. Tarrant), Martinus Nijhoff, Hague, Netherlands, pp. 231–47.CrossRefGoogle Scholar
  68. Dean, R.W. and Ball, C.O. (1960) Analysis of the myoglobin fractions on the surfaces of beef cuts. Food Technol. 14, 271.Google Scholar
  69. deHoll, J.C. (1981) Encyclopedia of labeling meat and poultry products, 5th edn. Meat Plant Magazine, St. Louis, Missouri, p. 123.Google Scholar
  70. Dickerson, R.E. and Geis, I. (1969) The structure and action of proteins. W.A. Benjamin, Inc., Menlo Park, California, p. 46.Google Scholar
  71. Dobson, B.N. and Cornforth, D.P. (1992) Non-fat dry milk inhibits pink discoloration in turkey rolls. Poult. Sci., 71, 1943.CrossRefGoogle Scholar
  72. Dransfield, E. (1981) Eating quality of DFD beef, in The Problem of Dark-Cutting in Beef (eds D.E. Hood and P.V. Tarrant), Martinus Nijhoff, Hague, Netherlands, pp. 334–58.Google Scholar
  73. Draudt, H.N. and Deatherage, F.E. (1956) Studies on the chemistry of cured meat color fading. Food Res. 21, 122.CrossRefGoogle Scholar
  74. Dymicky, M., Fox, J.B. and Wasserman, A.E. (1975) Color formation in cooked meat and model systems with organic and inorganic compounds. J. Food Sci. 40, 306.CrossRefGoogle Scholar
  75. Echevarne, C., Renerre, M. and Labas R. (1990) Metmyoglobin reductase activity in bovine muscles. Meat Sci. 27, 161.CrossRefGoogle Scholar
  76. Edmundson, A.B. (1965) Amino acid sequence of sperm whale myoglobin. Nature 205, 883.CrossRefGoogle Scholar
  77. El-Badawi, A.A., Cain, R.F., Samuels, C.E. and Anglemeier, A.F. (1964) Color and pigment stability of packaged refrigerated beef. Food Technol. 18(5), 159.Google Scholar
  78. Egan, A.F. and Shay, B.J. (1982) Significance of lactobacilli and film permeability in the spoilage of vacuum-packaged beef. J. Food Sci. 47, 1119.CrossRefGoogle Scholar
  79. Egbert, W.R. and Cornforth, D.P. (1986) Factors affecting color of dark cutting beef muscle. J. Food Sci. 51, 57.CrossRefGoogle Scholar
  80. Enfors, S.O., Molin, G. and Ternstrom, A. (1979) Effect of packaging under carbon dioxide, nitrogen or air on the microbial flora of pork stored at 4°C. J. Appl. Bact. 47, 197.CrossRefGoogle Scholar
  81. Faustman, C. and Cassens, R.G. (1990) The biochemical basis for discoloration in fresh meat. A review. J. Muscle Foods 1, 217.CrossRefGoogle Scholar
  82. Faustman, C., Cassens, R.G. and Greaser, M.L. (1988) Reduction of metmyoglobin by extracts of bovine liver and cardiac muscle. J. Food Sci. 53, 1065.CrossRefGoogle Scholar
  83. Faustman, C., Cassens, R.G., Schaefer, D.M., Buege, D.R. and Sheller, K.K. (1989a) Vitamin E supplementation of Holstein steer diets improves sirloin steak color. J. Food Sci. 54, 485.CrossRefGoogle Scholar
  84. Faustman, C., Cassens, R.G., Schaefer, D.M., Buege, D.R., Williams, S.N. and Sheller, K.K. (1989b) Improvement of pigment and lipid stability in Holstein steer beef by dietary supplementation of vitamin E. J. Food Sci. 54, 858.CrossRefGoogle Scholar
  85. Faustman, C., Johnson, J.L., Cassens, R.G. and Doyle, M.P. (1990) Color reversion in beef. Influence of psychrotropic bacteria. Fleischwirtsch. 70, 676.Google Scholar
  86. Fife, D.J. and Moore, W.M. (1979) The reduction and quenching of photoexcited flavins by EDTA. Photochem. Photobiol. 29, 43.CrossRefGoogle Scholar
  87. Finne, G. (1982) Modified- and controlled-atmosphere storage of muscle foods. Food Technol. 36(2), 128.Google Scholar
  88. Fischer, K. (1981) Influence of temperature, fasting and transportation, in The Problem of Dark-Cutting in Beef (eds D.E. Hood and P.V. Tarrant), Martinus Nijhoff, Hague, Netherlands, pp. 395–403.CrossRefGoogle Scholar
  89. Fox, J.B. (1966) The chemistry of meat pigments. J. Agric. Food Chem. 14, 207.CrossRefGoogle Scholar
  90. Fox, J.B., Jr. and Ackerman, S.A. (1968) Formation of nitric oxide myoglobin: Mechanisms of the reaction with various reductants. J. Food Sci. 33, 364CrossRefGoogle Scholar
  91. Fox, J.B., Jr., Dymicky, M. and Wasserman, A.E. (1974) Heme-protein-ligand interactions, in Proc. Symp. Protein-Metal Interactions (ed. M. Friedman), Plenum Publishing, New York, p. 97.CrossRefGoogle Scholar
  92. Fox, J.B., Jr. and Thompson, J.S. (1963) Formation of bovine nitrosylmyoglobin. I. pH 4.5–6.5. Biochemistry 2, 465.CrossRefGoogle Scholar
  93. Fredeen, H.T., Martin, A.H. and Weiss, G.M. (1974) Changes in tenderness of beef M. longissimus dor si as related to muscle colour and pH. J. Food Sci. 39, 532.CrossRefGoogle Scholar
  94. Fujii, J., Otsu, K., Zorzato, F., DeLeon, S., Khanna, V.J., Weiler, J.E., O’Brien, P.J. and MacLennan, D.H. (1991) Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia. Science 253, 448.CrossRefGoogle Scholar
  95. Gardner, G.A., Carson, A.W. and Patton, J. (1967) Bacteriology of pre-packed pork with reference to the gas composition within the pack. J. Appl. Bact. 30, 321.CrossRefGoogle Scholar
  96. Gee, D.L. and Brown, W.D. (1978a) Stability of carboxymyoglobin in refrigerated ground beef. J. Agric. Food Chem. 26, 273.CrossRefGoogle Scholar
  97. Gee, D.L. and Brown, W.D. (1978b) Extension of shelf-life in refrigerated ground beef stored under an atmosphere containing carbon dioxide and carbon monoxide. J. Agric. Food Chem. 26, 274.CrossRefGoogle Scholar
  98. George, P. and Stratmann, C.J. (1952) The oxidation of myoglobin to metmyoglobin by oxygen. 2. The relation between the first order rate constant and the partial pressure of oxygen. Biochem. J. 51, 418.Google Scholar
  99. Giddings, G.G. (1974) Reduction of ferrimyoglobin in meat. CRC Crit. Rev. Food Technol. 5, 143.Google Scholar
  100. Giddings, G.G. (1977) The basis of color in muscle foods. J. Food Sci. 42, 288.CrossRefGoogle Scholar
  101. Gill, C.O. (1983) Meat spoilage and evaluation of the potential storage life of fresh meat. J. Food Prot. 46, 444.Google Scholar
  102. Gill, C.O. and Harrison, J.C.L. (1989) The storage life of chilled pork packaged under carbon dioxide. Meat Sci. 26, 313.CrossRefGoogle Scholar
  103. Gill, C.O. and Newton, K.G. (1979) Spoilage of vacuum-packaged dark, firm, dry meat at chill temperatures. Appl. Environ. Microbiol. 37, 362.Google Scholar
  104. Ginger, I.D., Lewis, U.J. and Schweigert, B.S. (1955) Changes associated with irradiating meat and meat extracts with gamma rays. J. Agric. Food Chem. 3, 156.CrossRefGoogle Scholar
  105. Girard, B., Vanderstoep, J. and Richards, J.F. (1990) Characterization of the residual pink color in cooked turkey breast and pork loin. Food Sci. 55, 1249.CrossRefGoogle Scholar
  106. Ghorpade, V.M. and Cornforth, D.P. (1993) Spectral characterization of pigments responsible for pink color in pork roasts cooked to 65 or 82°C. J. Food Sci. 58, 51.CrossRefGoogle Scholar
  107. Ghorpade, V.M., Cornforth, D.P. and Sisson, D.V. (1992) Inhibition of red discoloration in cooked, vacuum packaged bratwurst. J. Food Sci. 57, 1053.CrossRefGoogle Scholar
  108. Gotoh, T. and Shikama, K. (1974) Autoxidation of oxymyoglobin from bovine heart muscle. Arch. Biochem. Biophys. 163, 476.CrossRefGoogle Scholar
  109. Govindarajan, S. (1973) Fresh meat color. CRC Crit. Rev. Food Technol. 4, 117.Google Scholar
  110. Govindarajan, S., Hultin, H.O. and Kotula, A.W. (1977) Myoglobin oxidation in ground beef, mechanistic studies. J. Food Sci. 42, 571.CrossRefGoogle Scholar
  111. Grandin, T. (1992) Dark cutters. Meat & Poultry 38(7), 78.Google Scholar
  112. Greene, B.E., Hsin, I. and Zipser, M.W. (1971) Retardation of oxidative color changes in raw ground beef. J. Food Sci. 36, 940.CrossRefGoogle Scholar
  113. Greer, G.G. and Murray, A.C. (1989) Effects of pork muscle quality on bacterial growth and retail case life. Meat Sci. 24, 61.CrossRefGoogle Scholar
  114. Guilbert, H.R. (1937) What causes ‘black cutter’ beef? A historical basis for the hypothesis that the condition known as ‘black cutter’ in beef is caused by hereditary factors. J. Heredity 28, 213.Google Scholar
  115. Gupta, L.K., Garg, V. and Tiwari, R.P. (1988) Evaluation of ammonium hydroxide as a preservative for ground meat. J. Appl. Microbiol. Biotechnol. 4(4), 431.CrossRefGoogle Scholar
  116. Hagler, L., Coppes, R.I. and Herman, R.H. (1979) Metmyoglobin reductase. Identification and purification of a reduced nicotinamide adenine dinucleotide-dependent enzyme from bovine heart which reduces metmyoglobin. J. Biol. Chem. 254, 6505.Google Scholar
  117. Haldane, J. (1901) The red colour of salted meat. J. Hyg. Camb. 1, 115.CrossRefGoogle Scholar
  118. Hall, J.L., Latschar, C.E. and Mackintosh, D.L. (1944) Studies on dark-cutting beef. Part IV. Characteristics of dark-cutting beef survey and preliminary investigation. Kansas Agric. Expt. Sta. Tech. Bull. 58, 55.Google Scholar
  119. Halleck, F.E., Ball, C.O. and Stier, E.F. (1958a) Factors affecting quality of pre-packaged meat. IV. Microbial studies. A. Cultural studies on bacterial flora of fresh meat, classification by genera. Food Technol. 12, 197.Google Scholar
  120. Halleck, F.E., Ball, C.O. and Stier, E.F. (1958b) Factors affecting quality of pre-packaged meat. IV. Microbial studies. B. Effect of packaging characteristics and atmospheric pressure in package upon bacterial flora of meat. Food Technol. 12, 301.Google Scholar
  121. Hanenian, R., Mittal, G.S. and Usborne, W.R. (1989) Effects of pre-chilling, freezing rate, and storage time on beef patty quality. J. Food Sci. 54, 532.CrossRefGoogle Scholar
  122. Hanna, M.O., Savell, J.W., Smith, G.C., Purser, D.E., Gardner, F.A. and Vanderzant, C. (1983) Effect of growth of individual meat bacteria on pH, color and odor of aseptically prepared vacuum-packaged round steaks. J. Food Prot. 46, 216.Google Scholar
  123. Hanson, H.L., Brushway, M.J., Pool, M.F. and Lineweaver, H. (1963) Factors causing color and texture differences in radiation-sterilized chicken. Food Technol. 17, 108.Google Scholar
  124. Harbers, C.A.Z., Harrison, D.L. and Kropf, D.H. (1981) Ascorbic acid effects on bovine muscle pigments in the presence of radiant energy. J. Food Sci. 46, 7.CrossRefGoogle Scholar
  125. Harel, S. and Kanner, J. (1985) Hydrogen peroxide generation in ground muscle tissues. J. Agric. Food. Chem. 33, 5178.Google Scholar
  126. Hedrick, H.B. (1981) Preventive treatments during the pre-slaughter period, in The Problem of Dark-Cutting in Beef (eds D.E. Hood and P.V. Tarrant), Martinus Nijhoff, Hague, Netherlands, pp. 213–28.CrossRefGoogle Scholar
  127. Hedrick, H.B., Boillot, J.B., Brady, D.E. and Naumann, H.D. (1959) Etiology of darkcutting beef. Missouri Agric. Expt. Sta. Res. Bull. 717.Google Scholar
  128. Heinze, P.H. and Mitchell, G. (1991) A comparison of some muscle metabolites in stress susceptible and resistant Landrace gilts after halothane exposure or exercise stress. Meat Sci. 30, 337.CrossRefGoogle Scholar
  129. Hoagland, R. (1908) The action of saltpeter upon the color of meat. USDA, Bureau of Animal Industry, 25th annual report, Washington DC, p. 301.Google Scholar
  130. Hood, D.E. (1975) Pre-slaughter injection of sodium ascorbate as a method of inhibiting metmyoglobin formation in fresh beef. J. Sci. Food Agric. 26, 85.CrossRefGoogle Scholar
  131. Hood, D.E. (1980) Factors affecting the rate of metmyoglobin accumulation in pre-packaged beef. Meat Sci. 4, 247.CrossRefGoogle Scholar
  132. Hornsey, H.C. (1956) The colour of cooked cured pork. I. Estimation of the nitric oxidehaem pigments. J. Sci. Food Agric. 7, 534.CrossRefGoogle Scholar
  133. Howard, A., Duffy, P., Else, K. and Brown, W.D. (1973) Possible substitutes for nitrite for pigment formation in cured meat products. J. Agric. Food Chem. 21, 894.CrossRefGoogle Scholar
  134. Huffman, D.L., Davis, K.A., Marple, D.N. and McGuire, J.A. (1975) Effect ot of gas atmospheres on microbial growth, color and pH of beef. J. Food Sci. 40, 1229.CrossRefGoogle Scholar
  135. Hunt, M.C. and Hedrick, B. (1977) Chemical, physical and sensory characteristics of bovine muscle from four quality groups. J. Food Sci. 42, 716.CrossRefGoogle Scholar
  136. IFT (1986) Sulfites as food ingredients. Food Technol. 40(6), 47.Google Scholar
  137. Ingram, M. (1962) Microbiological principles in prepacking meats. J. Appl. Bacteriol. 25, 259.CrossRefGoogle Scholar
  138. Ito, T., Cassens, R.G., Greaser, M.L., Lee, M. and Izumi, K. (1983) Lability and reactivity of non-heme protein-bound nitrite. J. Food Sci. 48, 1204.CrossRefGoogle Scholar
  139. Izumi, K., Cassens, R.G. and Greaser, M.L. (1989) Reaction of nitrite with ascorbic acid and its significant role in nitrite-cured foods. Meat Sci. 26, 141.CrossRefGoogle Scholar
  140. James, N.T. (1968) Histochemical demonstration of myoglobin in skeletal muscle fibers and muscle spindles. Nature 219, 1174.CrossRefGoogle Scholar
  141. James, S.J., Gigiel, A.J. and Hudson, W.R. (1983) The ultra rapid chilling of pork. Meat Sci. 9, 63.CrossRefGoogle Scholar
  142. Jaye, M., Kittaka, R.S. and Ordal, Z.J. (1962) The effect of temperature and packaging material on the storage life and bacterial flora of ground beef. Food Technol. 16(5), 95.Google Scholar
  143. Jensen, L.B. (1945) Microbiology of Meats, 3rd edn., Garrard Press, Champaign, Illinois.Google Scholar
  144. Jensen, L.B. and Urbain, W.M. (1936a) Bacteriology of green discoloration in meats and spectrophotometric characteristics of the pigments involved. Food Res. 1, 263.CrossRefGoogle Scholar
  145. Jensen, L.B. and Urbain, W.M. (1936b) A delicate test for blood pigments. Food Res. 1, 275.CrossRefGoogle Scholar
  146. Kalchayanand, N., Ray, B., Field, R.A. and Johnson, M.C. (1989) Spoilage of vacuum-packaged refrigerated beef by Clostridium. J. Food Prot. 52, 424.Google Scholar
  147. Kanner, J. and Juven, B.J. (1980) S-nitrosocysteine as an antioxidant, color-developing and anticlostridial agent in comminuted turkey meat. J. Food Sci. 45, 1105.CrossRefGoogle Scholar
  148. Kauffman, R.G., Cassens, R.G., Scherer, A. and Meeker, D.L. (1992) Variations in Pork Quality. National Pork Producers Council, Des Moines, Iowa.Google Scholar
  149. Kastenschmidt, L.L., Briskey, E.J. and Hoekstra, W.G. (1964) Prevention of pale, soft, exudative porcine muscle through regulation of ante-mortem environmental temperature. J. Food Sci. 29, 210.CrossRefGoogle Scholar
  150. Keeton, J.T., Leu, R., Vanderzant, C., Bohac, J.J., Griffin, D.B., Savell, J.W. and Cross, H.R. (1988) Evaluation of fresh vacuum-packaged beef steaks coated with an acetylated monoglyceride. Food Sci. 53, 701.CrossRefGoogle Scholar
  151. Keilin, J. (1955) Reactions of free haematins and haemoproteins with nitric oxide and certain other substances. Biochem. J. 59, 571.Google Scholar
  152. Kendrew, J.C., Dickerson, R.E., Stranberg, B.E., Hart, R.G., Davies, D.R., Phillips, D.C. and Shore, V.C. (1960) Structure of myoglobin. A three-dimensional Fourier synthesis at 2 A° resolution. Nature 185, 422.CrossRefGoogle Scholar
  153. Kenny, J.F. and Tarrant, P.V. (1987).Dark-cutting beef in bulls prevented by modified abattoir pens. Farm and Food Res. 18, 7.Google Scholar
  154. Killday, B.K., Tempesta, M.S., Bailey, M.E. and Metral, C.J. (1988) Structural characterization of nitrosylhemochromogen of cooked cured meat: Implications in the meat-curing reaction. J. Agric. Food Chem. 36, 909.CrossRefGoogle Scholar
  155. Koizumi, C. and Brown, W.D. (1971) Formation of nitric oxide myoglobin by nicotinamide adenine dinucleotides and flavins. J. Food Sci. 36, 1105.CrossRefGoogle Scholar
  156. Kraft, A.A. and Ayres, J.C. (1952) Post-mortem changes in stored meats. IV. Effect of packaging materials on keeping quality of self-service meats. Food Technol. 6, 8.Google Scholar
  157. Kropf, D.H. (1980) Effects of retail display conditions on meat color. Proc. Recip. Meat Conf. 33. 15.Google Scholar
  158. Krzywicki, K. (1982) The determination of heam pigments in meat. Meat Sci. 7, 29.CrossRefGoogle Scholar
  159. Lanari, M.C., Bevilacqua, A.E. and Zaritzky, N.E. (1989) Pigments modifications during freezing and frozen storage of packaged beef. J. Food Proc. Engr. 12, 49.CrossRefGoogle Scholar
  160. Lanari, M.C. and Cassens, R.G. (1991) Mitochondrial activity and beef muscle color stability. J. Food Sci. 56, 1476.CrossRefGoogle Scholar
  161. Landrock, A.H. and Wallace, G.A. (1955) Discoloration of fresh red meat and its relationship to film oxygen permeability. Food Technol. 9, 194.Google Scholar
  162. Lanier, T.C., Carpenter, J.A. and Toledo, R.T. (1977) Effects of cold storage environment on color of exposed lean beef surfaces. J. Food Sci. 42, 860.CrossRefGoogle Scholar
  163. Lawrie, R.A. (1958) Physiological stress in relation to dark-cutting beef. J. Sci. Food Agric. 9,721.CrossRefGoogle Scholar
  164. Lawrie, R.A. (1960) Post-mortem glycolysis in normal and exudative longissimus dor si muscles of the pig in relation to so-called white muscle disease. J. Comp. Pathol. Therap. 70, 273.Google Scholar
  165. Ledward, D.A. (1970) Metmyoglobin formation in beef stored in carbon dioxide enriched and oxygen depleted atmospheres. J. Food Sci. 35, 33.CrossRefGoogle Scholar
  166. Ledward, D.A. (1971) Metmyoglobin formation in beef muscles as influenced by water content and anatomical location. Food Sci. 36, 138.CrossRefGoogle Scholar
  167. Ledward, D.A. (1972) Metmyoglobin reduction and formation in beef during aerobic storage at 1°C. J. Food Sci. 37, 634.CrossRefGoogle Scholar
  168. Ledward, D.A. (1985) Post-slaughter influences on the formation of metmyoglobin in beef muscles. Meat Sci. 15, 149.CrossRefGoogle Scholar
  169. Ledward, D.A. and Shorthose, W.R. (1971) A note on the haem pigment concentration of lamb as influenced by age and sex. Anim. Prod. 13, 193.CrossRefGoogle Scholar
  170. Ledward, D.A., Smith, C.G., Clarke, H.M. and Nicholson, M. (1977) Relative role of catalysts and reductants in the formation of metmyoglobin in aerobically stored beef. Meat Sci. 1, 149.CrossRefGoogle Scholar
  171. Lee, M. and Cassens, R.G. (1976) Nitrite binding sites on myoglobin. J. Food Sci. 41, 969.CrossRefGoogle Scholar
  172. Lehninger, A.L. (1975) Biochemistry, 2nd edn., Worth Publishers, New York.Google Scholar
  173. Lin, T.S., Levin, R.E. and Hultin, H.O. (1977) Myoglobin oxidation in ground beef: Microorganisms and food additives. J. Food Sci. 42, 151.CrossRefGoogle Scholar
  174. Livingston, D.J. and Brown, W.D. (1981) The chemistry of myoglobin and its reactions. Food Technol. 35(5), 244.Google Scholar
  175. Livingston, D.J., Lamar, G.N. and Brown, W.D. (1983) Myoglobin diffusion in bovine heart muscle. Science 220, 71.CrossRefGoogle Scholar
  176. Ludvigsen, J. (1954) Undersogelser over den sakaldte ‘muskeldegeneration’ hos svin 1. 272 beretning fra forsogslaboratoriet. Statens husdyrbrugsudvalg, Kobenhavn.Google Scholar
  177. MacDougall, D.B. (1982) Changes in the colour and opacity of meat. Food Chem. 9, 75.CrossRefGoogle Scholar
  178. MacDougall, D.B. and Jones, S.J. (1981) Translucency and colour defects of dark-cutting meat and their detection, in The Problem of Dark-Cutting in Beef (eds D.E. Hood and PV. Tarrant), Martinus Nijhoff Publishers, Hague, Netherlands, pp. 328–39.CrossRefGoogle Scholar
  179. MacDougall, D.B. and Taylor, A.A. (1975) Colour retention in fresh meat stored in oxygen -a commercial scale trial. J. Food Technol. 10, 339.CrossRefGoogle Scholar
  180. MacDougall, D.B., Shaw, B.G., Nute, G.R. and Rhodes, D.N. (1979) Effect of pre-slaughter handling on the quality and microbiology of venison from farmed young red deer. J. Sci. Food Agric. 30,1160.CrossRefGoogle Scholar
  181. Mallinson, E.T., Curry, K.A. and Corrao, P.A. (1985) Re-evaluation of selectivity of malachite green test for presence of sulfite in mechanically deboned poultry. J. Assoc. Offic. Anal. Chem. 68, 1231.Google Scholar
  182. Manu-Tawiah, W., Ammann, L.L., Sebranek, J.G. and Molins, R.A. (1991) Extending the color stability and shelf life of fresh meat. Food Technol. 45(3), 94.Google Scholar
  183. Marriott, N.G., Naumann, H.D., Stringer, W.C. and Hedrick, H.B. (1967) Color stability of pre-packaged fresh beef as influenced by pre-display environments. Food Technol. 21, 104.Google Scholar
  184. McBrady, W.J. (1968) Curing apparatus. US Patent 3 393 629.Google Scholar
  185. McKeith, F.K., Smith, G.C., Savell, J.W., Dutson, T.R., Carpenter, Z.L. and Hammons, D.R. (1981) Effects of certain electrical stimulation parameters on quality and palatability of beef. J. Food Sci. 46, 13.CrossRefGoogle Scholar
  186. McVeigh, J.M. and Tarrant, P.V. (1981) The breakdown of muscle glycogen during behavioural stress in normal and beta-adrenoreceptor blocked young bulls, in The Problem of Dark-Cutting in Beef (eds D.E. Hood and P.V. Tarrant), Martinus Nijhoff, Hague, Netherlands, pp. 430–39.CrossRefGoogle Scholar
  187. Meischen, H.W., Huffman, D.L. and Davis, G.W. (1987) Branded beef-product of tomorrow today. Proc. Recip. Meat Conf. 40, 37.Google Scholar
  188. Mendenhall, V.T. (1989) Effect of pH and total pigment concentration on the internal color of cooked ground beef patties. J. Food Sci. 54, 1.CrossRefGoogle Scholar
  189. Mendonca, A.F., Molins, R.A., Kraft, A.A. and Walker, H.W. (1989) Microbial, chemical, and physical changes in fresh, vacuum-packaged pork treated with organic acids and salts. J. Food Sci. 54, 18.CrossRefGoogle Scholar
  190. Mitsumoto, M., Faustman, C., Cassens, R.G., Arnold, R.N., Schaefer, D.M. and Scheller, K.K. (1991a) Vitamins E and C improve pigment and lipid stability in ground beef. J. Food Sci. 56, 194.CrossRefGoogle Scholar
  191. Mitsumoto, M., Cassens, R.G., Schaefer, D.M. and Scheller, K.K. (1991b) Pigment stability improvement in beef steak by ascorbic acid application. J. Food Sci. 56, 857.CrossRefGoogle Scholar
  192. Mitsumoto, M., Cassens, R.G., Schaefer, D.M., Arnold, R.N. and Scheller, K.K. (1991c) Improvement of color and lipid stability in beef longissimus with dietary vitamin E and vitamin C dip treatment. J. Food Sci. 56, 1489.CrossRefGoogle Scholar
  193. Mocker, J. (1991) USD A Won’t Visit Sulfite Man. Lean Trimmings. Western States Meat Assn., Oakland, California.Google Scholar
  194. Morita, S., Cassens, R.G. and Briskey, E.J. (1969) Localization of myoglobin in striated muscle of the domestic pig. Benzidine and NADH2-TR reactions. Stain Technol. 44, 283.Google Scholar
  195. Mortimer, C.E. (1977) Introduction to Chemistry. Van Nostrand Reinhold, New York.Google Scholar
  196. Munns, W.O. and Burrell, D.E. (1966) The incidence of dark-cutting beef. Food Technol. 20, 1601.Google Scholar
  197. Nachlas, M.M., Walker, D.G. and Seligman, A.M. (1958) A histochemical method for the demonstration of diphosphopyridine nucleotide diaphorase. J. Biophysic. Biochem. Cytol. 4, 29.CrossRefGoogle Scholar
  198. Newton, K.G. and Gill, C.O. (1978) Storage quality of dark, firm, dry meat. Appl. Environ. Microbiol. 36, 375.Google Scholar
  199. Newton, K.G. and Gill, C.O. (1981) The microbiology of DFD fresh meats. A review. Meat Sci. 5, 223.CrossRefGoogle Scholar
  200. Nicol, D.J., Shaw, M.K. and Ledward, D.A. (1970) Hydrogen sulfide production by bacteria and sulfmyoglobin formation in prepacked chilled beef. Appl. Microbiol. 19, 937.Google Scholar
  201. Nishida, J. (1976) Changes in myoglobin content during development and growth of chicken. Jpn. J. Vet. Sci. 38, 299.CrossRefGoogle Scholar
  202. Nunes, K. (1992) Quality and beef. Meat and Poultry 38(6), 38.Google Scholar
  203. O’Boyle, A.R., Rubin, L.J., Diosady, L.L., Aladin-Kassam, N., Comer, F. and Brightwell, W. (1990) A nitrite-free curing system and its application to the production of weiners. Food Technol. 44(5), 88.Google Scholar
  204. O’Boyle, A.R., Aladin-Kassam, N., Rubin, L.J. and Diosady, L.L. (1992) Encapsulated cured-meat pigment and its application in nitrite-free ham. J. Food Sci. 57, 807.CrossRefGoogle Scholar
  205. Oellingrath, I.M., Iversen, A. and Skrede, G. (1990) Quantitative determination of myoglobin and haemoglobin in beef by high-performance liquid chromatography. Meat Sci. 28, 313.CrossRefGoogle Scholar
  206. Ogilvy, W.A. and Ayres, J.C. (1951) Post-mortem changes in stored meats. 11. The effect of atmospheres containing carbon dioxide in prolonging the storage life of cut-up chicken. Food Technol. 5, 97.Google Scholar
  207. Okayama, T., Imai, T. and Yamanoue, M. (1987) Effect of ascorbic acid and alpha-tocopherol on storage stability of beef steaks. Meat Sci. 21, 267.CrossRefGoogle Scholar
  208. O’Keefe, M. and Hood, D.E. (1982) Biochemical factors influencing metmyoglobin formation in beef from muscles of differing colour stability. Meat Sci. 7, 209.CrossRefGoogle Scholar
  209. Orcutt, M.W., Dutson, T.R., Cornforth, D.P. and Smith, G.C. (1984) Factors affecting the formation of a dark, coarse band (‘heat-ring’) in bovine longissimus muscle. J. Anim. Sci. 58, 1366.Google Scholar
  210. Pasteur, R.L. and Joubert, J. (1877) Etude sur la maladie charbonneuse. Comptes Rendus Hebdomadaires des Seances de I’Academie des Sciences, 84, 900.Google Scholar
  211. Patterson, J.T. and Gibbs, P.A. (1977) Incidence and spoilage potential of isolates from vacuum-packaged meat of high pH value. J. Appl. Bacteriol. 43, 25.CrossRefGoogle Scholar
  212. Pierson, M.D., Collins-Thompson, D.L. and Ordal, Z.J. (1970) Microbiological, sensory, and pigment changes of aerobically and anaerobically packaged beef. Food Technol. 24, 1171.Google Scholar
  213. Pietraszek, G. (1989) If they can do it, we can — and must. National Provisioner, May 20, pp. 8–11.Google Scholar
  214. Pirko, P.C. and Ayres, J.C. (1957) Pigment changes in packaged beef during storage. Food Technol 11, 461.Google Scholar
  215. Pool, M.F. (1956) Why does some cooked turkey turn pink? Turkey World, Jan, p. 68.Google Scholar
  216. Ramsbottom, J.M., Goeser, P.A. and Schultz, H.W. (1951) How light discolors meat: What to do about it. Food Ind. 23(2), 120.Google Scholar
  217. Rankin, M.D. (1973) A new method of curing. Proc. Inter. Food Sci. Technol. 6, 157.Google Scholar
  218. Reagan, J.O., Smith, G.C. and Carpenter, Z.L. (1973) Use of ultraviolet light for extending the retail caselife of beef. J. Food Sci. 38, 929.CrossRefGoogle Scholar
  219. Reddy, I.M. and Carpenter, C.E. (1991) Determination of metmyoglobin reductase activity in bovine skeletal muscles. J. Food Sci. 56, 1161.CrossRefGoogle Scholar
  220. Reddy, S.G., Hendrickson, R.L. and Olson, H.C. (1970) The influence of lactic cultures on ground beef quality. Food Sci. 35, 787.CrossRefGoogle Scholar
  221. Reith, J.F. and Szakaly, M. (1967a) Formation and stability of nitric oxide myoglobin. I. Studies with model systems. J. Food Sci. 32, 188.CrossRefGoogle Scholar
  222. Reith, J.F. and Szakaly, M. (1967b) Formation and stability of nitric oxide myoglobin. II. Studies on meat. J. Food Sci. 32, 194.CrossRefGoogle Scholar
  223. Renerre, M. and Labas, R. (1987) Biochemical factors influencing metmyoglobin formation in beef muscles. Meat Sci. 19, 151.CrossRefGoogle Scholar
  224. Renerre, M., Anton, M. and Gatellier, P. (1992) Autoxidation of purified myoglobin from two bovine muscles. Meat Sci. 32, 331.CrossRefGoogle Scholar
  225. Rey, C.R., Kraft, A.A., Topel, D.G., Parrish, F.C., Jr. and Hotchkiss, D.K. (1976) Microbiology of pale, dark and normal pork. J. Food Sci. 41, 111.CrossRefGoogle Scholar
  226. Rhee, K.S. and Ziprin, Y.A. (1987) Lipid oxidation in retail beef, pork and chicken muscles as affected by concentrations of heme pigments and non-heme iron and microsomal enzymic lipid peroxidation activity. J. Food Biochem. 11, 1.CrossRefGoogle Scholar
  227. Rickansrud, D.A. and Henrickson, R.L. (1967) Total pigments and myoglobin concentration in four bovine muscles. J. Food Sci. 32, 57.CrossRefGoogle Scholar
  228. Rikert, J.A., Bressler, L., Ball, C.O. and Stier, E.F. (1957) Factors affecting quality of prepackaged meat. II. Color studies. B. Effects of storage time, storage temperature, antioxidants, bacteria, light, freezing and fat upon color of product. Food Technol. 11(ii), 567.Google Scholar
  229. Robach, D.L. and Costilow, R.N. (1961) Role of bacteria in the oxidation of myoglobin. Appl. Microbiol. 9, 529.Google Scholar
  230. Romero-Herrera, A.E., Lehmann, H., Joysey, K.A. and Friday, A.E. (1978) On the evolution of myoglobin. Phil. Trans. Royal Soc. London Series B, 283, 61.CrossRefGoogle Scholar
  231. Roth, L.A. and Clark, D.S. (1972) Studies on the bacterial flora of vacuum-packaged fresh beef. Can. J. Microbiol. 18, 1761.CrossRefGoogle Scholar
  232. Rust, R.E. (1977) Sausage and Processed Meats Manufacturing, American Meat Institute, Chicago, Illinois, p. 24.Google Scholar
  233. Saleh, B. and Watts, B.M. (1968) Substrates and intermediates in the enzymatic reduction of metmyoglobin in ground beef. J. Food Sci. 33, 353.CrossRefGoogle Scholar
  234. Satterlee, L.D. and Hansmeyer, W. (1974) The role of light and surface bacteria in the color stability of prepackaged beef. J. Food Sci. 39, 305.CrossRefGoogle Scholar
  235. Satterlee, L.D., Wilhelm, M.S. and Barnhart, H.M. (1971) Low-dose gamma irradiation of bovine metmyoglobin. Food Sci. 36, 549.CrossRefGoogle Scholar
  236. Savell, J.W., Smith, G.C. and Carpenter, Z.L. (1978) Effect of electrical stimulation on quality and palatability of light-weight beef carcasses. J. Anim. Sci. 46, 1221.Google Scholar
  237. Savell, J.W., Smith, G.C., Hanna, M.O. and Vanderzant, C. (1981) Packaging of beef loin steaks in 75% O2 plus 25% CO2 I. Physical and sensory properties. J. Food Prot. 44, 923.Google Scholar
  238. Savell, J.W., Griffin, D.B., Dill, C.W., Acuff, G.R. and Vanderzant, C. (1986) Effect of film oxygen transmission rate on lean color and microbiological characteristics of vacuum- packaged beef knuckles. J. Food Prot. 49, 917.Google Scholar
  239. Sayre, R.N. and Briskey, E.J. (1963) Protein solubility as influenced by physiological conditions in the muscle. J. Food Sci. 28, 675.CrossRefGoogle Scholar
  240. Sayre, R.N., Kiernat, B. and Briskey, E.J. (1964) Processing characteristics of porcine muscle related to pH and temperature during rigor mortis development and to gross morphology 24 h post-mortem. J. Food Sci. 29, 175.CrossRefGoogle Scholar
  241. Scriven, F., Sporns, P. and Wolfe, F. (1987) Investigation of nitrite and nitrate levels in paper materials used to package fresh meat. J. Agric. Food Chem. 35, 188.CrossRefGoogle Scholar
  242. Seideman, S.C. and Durland, P.R. (1983) Vacuum-packaging of fresh beef. A review. J. Food Qual. 6, 29.CrossRefGoogle Scholar
  243. Seideman, S.C., Carpenter, Z.L., Smith, G.C., Dill, C.W. and Vanderzant, C. (1979) Physical and sensory characteristics of beef packaged in modified gas atmospheres. J. Food Prot. 42, 233.Google Scholar
  244. Severin, S.E., Tseitlin, L.A. and Druzhinina, T.N. (1963) Enzymic breakdown of diphosphopyridine neucleotide in cardiac and skeletal muscle. Biochem. 28, 112.Google Scholar
  245. Shahidi, F. and Pegg, R.P. (1991) Novel synthesis of cooked cured-meat pigment. J. Food Sci. 56, 1205.CrossRefGoogle Scholar
  246. Shahidi, F., Rubin, L.J., Diosady, L.L. and Wood, D.F. (1985) Preparation of the cooked cured-meat pigment, dinitrosyl ferrohemochrome, from hemin and nitric oxide. J. Food Sci. 50, 272.CrossRefGoogle Scholar
  247. Shaw, D.E., Claus, J.R. and Stewart, K.K. (1992) Effects of ammonia exposure on fresh pork: A distinct pink color after cooking. J. Muscle Foods 3, 169.CrossRefGoogle Scholar
  248. Shikama, K. (1985) Nature of the FeO2 bonding in myoglobin. An overview from physical to clinical biochemistry. Experientia 41, 701.CrossRefGoogle Scholar
  249. Shikama, K. (1990) Autoxidation of oxymyoglobin. A meeting point of the stabilization and the activation of molecular oxygen. Biol. Rev. 65, 517.CrossRefGoogle Scholar
  250. Shimizu, C. and Matsuura, F. (1971) Occurrence of a new enzyme reducing metmyoglobin in dolphin muscle. Agric. Biol. Chem. 35, 468.CrossRefGoogle Scholar
  251. Stermer, R.A., Lasater-Smith, M. and Brasington, C.F. (1987) Ultraviolet radiation — an effective bactericide for fresh meat. J. Food Prot. 50, 108.Google Scholar
  252. Stewart, M.R., Hutchins, B.K., Zipser, M.W. and Watts, B.M. (1965) Enzymatic reduction of metmyoglobin by ground beef. J. Food Sci. 30, 1487.Google Scholar
  253. Stubbs, C.A. and Cornforth, D.P. (1980) The effects of an edible calcium pectinate film on beef carcass shrinkage and surface microbial growth. Proc. Eur. Mtg. Meat Res. Workers, 26(2) 276.Google Scholar
  254. Tappel, A.L. (1956) Regeneration and stability of oxymyoglobin in some gamma irradiated meats. Food Res. 21, 650.CrossRefGoogle Scholar
  255. Tappel, A.L. (1957a) Reflectance spectral studies of the hematin pigments of cooked beef. Food Res. 22, 404.CrossRefGoogle Scholar
  256. Tappel, A.L. (1957b) The red pigment of pre-cooked irradiated meats. Food Res. 22, 408.CrossRefGoogle Scholar
  257. Tarladgis, B.G. (1962a) Interpretation of the spectra of meat pigments. I. Cooked meats. J. Sci. Food Agric. 13, 481.CrossRefGoogle Scholar
  258. Tarladgis, B.G. (1962b) Interpretation of the spectra of meat pigments. II. Cured meats. The mechanism of color fading. Sci. Food Agric. 13, 485.CrossRefGoogle Scholar
  259. Tarrant, P.V. (1981) The occurrence, causes and economic consequences of dark-cutting in beef — A survey of current information, in The Problem of Dark-Cutting in Beef (eds D.E. Hood and P.V. Tarrant), Martinus Nijhoff, Hague, Netherlands, pp. 3–34.CrossRefGoogle Scholar
  260. Tarrant, P.V. and Sherington, J. (1980) An investigation of ultimate pH in the muscles of commercial beef carcasses. Meat Sci. 4, 287.CrossRefGoogle Scholar
  261. Topel, D.G., Merkel, R.A., Mackintosh, D.L. and Hall, J.L. (1966) Variation of some physical and biochemical properties within and among selected porcine muscles. J. Anim. Sci. 25, 277.Google Scholar
  262. Trout, G.R. (1989) Variation in myoglobin denaturation and color of cooked beef, pork and turkey meat as influenced by pH, sodium chloride, sodium tripolyphosphate and cooking temperature. J. Food Sci. 54, 536.CrossRefGoogle Scholar
  263. Trout, G.R. (1990) The rate of metmyoglobin formation in beef, pork, and turkey meat as influenced by pH, sodium chloride, and sodium tripolyphosphate. Meat Sci. 28, 203.CrossRefGoogle Scholar
  264. Unda, J.R., Molins, R.A. and Walker, H.W. (1990) Microbiological and some physical and chemical changes in vacuum-packaged beef steaks treated with combinations of potassium sorbate, phosphate, sodium chloride and sodium acetate. J. Food Sci. 55, 323.CrossRefGoogle Scholar
  265. Urbain, W.M. (1960) Protecting color of electron irradiated meat. US Patent 2 963 369.Google Scholar
  266. Urbain, W.M. (1973) The low-dose radiation preservation of retail cuts of meat. Radiation Preservation of Food. Intern. Atomic Energy Agency, SM-166/50, 505.Google Scholar
  267. Urbain, W.M. (1986) Meats and poultry, (ch. 6.), in Food Irradiation, (ed. W.M. Urbain), Academic Press, Inc., Orlando, Florida, p. 142.Google Scholar
  268. Urbain, W.M. and Greenwood, D.A. (1940) The heme pigments of cured meats. II. An application of the Van Slyke-Neill manometric gas apparatus to the determination of oxygen capacity of dilute hemoglobin solutions. Food Res. 5, 607.CrossRefGoogle Scholar
  269. Urbain, W.M. and Jensen, L.B. (1940) The heme pigments of cured meats I. Preparation of nitric oxide hemoglobin and stability of the compound. Food Res. 5, 593.CrossRefGoogle Scholar
  270. Urbain, W.M. and Ramsbottom, J.M. (1948) Controlling quality changes in cured meats by packaging. Food Res. 13, 432.CrossRefGoogle Scholar
  271. Vahabzadeh, F., Collinge, S.K., Cornforth, D.P., Mahoney, A.W. and Post, F.J. (1983) Evaluation of iron binding compounds as inhibitors of gas and toxin production by Clostridium botulinum in ground pork. J. Food Sci. 48, 1445.CrossRefGoogle Scholar
  272. Walch, K.A. and Rose, D. (1956) Factors affecting the oxidation of nitric oxide myoglobin. J. Agric. Food Chem. 4, 353.Google Scholar
  273. Wallace, W.J., Houtchens, R.A., Maxwell, J.C. and Caughey, W.S. (1982) Mechanism of autoxidation for hemoglobins and myoglobins. J. Biol. Chem. 257, 4966.Google Scholar
  274. Walters, C.L. and Taylor, A.M. (1963) Biochemical properties of pork muscle in relation to curing. Food Technol. 17, 354.Google Scholar
  275. Walters, C.L. and Taylor, A.M. (1964) Nitrite metabolism by muscle in vitro. Biochim. Biophys. Acta 86, 448.CrossRefGoogle Scholar
  276. Walters, C.L., Casselden, R.J. and Taylor, A.M. (1967) Nitrite metabolism by skeletal muscle mitochondria in relation to haem pigments. Biochim. Biophys. Acta 143, 310.CrossRefGoogle Scholar
  277. Wang, J.H. (1962) Hemoglobin and myoglobin (ch. 11.), in Oxygenases, (ed. O. Hayaishi), Academic Press, New York, p. 469.Google Scholar
  278. Warriss, P.D. (1979) The extraction of haem pigments from fresh meat. J. Food Technol. 14, 75.CrossRefGoogle Scholar
  279. Warriss, P.D. and Rhodes, D.N. (1977) Haemoglobin concentrations in beef. J. Sci. Food Agric. 28, 931.CrossRefGoogle Scholar
  280. Watts, B.M. and Lehmann, B.T. (1952) The effect of ascorbic acid on the oxidation of hemoglobin and the formation of nitric oxide hemoglobin. Food Res. 17, 100.CrossRefGoogle Scholar
  281. Watts, B.M., Kendrick, J., Zipser, M.W., Hutchins, B.K. and Saleh, B. (1966) Enzymatic reducing pathways in meat. J. Food Sci. 31, 855.CrossRefGoogle Scholar
  282. Watts, D.A., Wolfe, S.K. and Brown, W.D. (1978) Fate of [14C]carbon monoxide in cooked or stored ground beef samples. J. Agric. Food Chem. 26, 210.CrossRefGoogle Scholar
  283. Weiss, G.M., Peo, E.R., Jr., Mandigo, R.W. and Moser, B.D. (1975) Influence of exercise on performance and carcass parameters of confinement reared swine. J. Anim. Sci. 40, 457.Google Scholar
  284. Williams, R.J.P. (1956) The properties of metalloporphyrins. Chem. Rev. 56, 299.CrossRefGoogle Scholar
  285. Winkler, C.A. (1939) The colour of meat. I. Apparatus for its measurement, and relation between pH and colour. Canad. J. Res. 17, Sect. D., p. 7.Google Scholar
  286. Wittenberg, J.B. (1970) Myoglobin facilitated oxygen diffusion. Role of myoglobin in oxygen entry into muscle. Physiol. Rev., 50, 559.Google Scholar

Copyright information

© Springer Science+Business Media Dordrecht 1994

Authors and Affiliations

  • D. Cornforth

There are no affiliations available

Personalised recommendations