Skip to main content
Log in

Effect of postmortem time on the metmyoglobin reductase activity, oxygen consumption, and colour stability of different lamb muscles

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

Abstract

The aim of this research was to characterize the lamb M. longissimus dorsi (LD), M. semitendinosus (ST), and M. psoas major (PM) muscles for differences in instrumental colour, tissue oxygen consumption rate (OCR), mitochondrial respiration control ratio (RCR), metmyoglobin reductase activity (MRA), and the relative proportions of myoglobin (Mb) redox forms. LD, ST, and PM muscles were stored for 6 days at 4 °C. Changes in the instrumental colour (CIE L*-value, a*-value, b*-value, Chroma-value, and Hue-value), OCR, RCR, MRA, and relative proportions of Mb redox forms during storage were evaluated. LD revealed the lowest MetMb accumulation and highest colour stability. Muscles with higher colour stability had lower levels of OCR, higher MRA, and less MetMb accumulation. Colour stability and MRA for the lamb muscles were LD > ST > PM. The correlation coefficients among the main parameters were also investigated in this research. The correlation coefficients between a*-value and OxyMb within the same muscle were highly significant (r = 0.951, 0.974, 0.828; P < 0.05). MRA of the muscles was negatively correlated (r = −0.810, −0.942, −0.971, P < 0.05) with the relative percentage of MetMb. The results of the present study suggested that OCR, RCR and MRA contribute to variation in colour stability of different lamb muscles.

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.

Institutional subscriptions

Fig. 1

Similar content being viewed by others

References

  1. Arihara K, Cassens RG, Greaser ML, Luchansky JB, Mozdziak PE (1995) Localization of metmyoglobin-reducing enzyme (NADH-cytochrome b5 reductase) system components in bovine skeletal muscle. Meat Sci 39:205–213

    Article  CAS  Google Scholar 

  2. Ledward DA (1985) Post-slaughter influences on the formation of metmyoglobin in beef muscles. Meat Sci 15:149–171

    Article  CAS  Google Scholar 

  3. Faustman C, Cassens RG (1990) The biochemical basis for meat discoloration in fresh meat: a review. J Muscle Foods 1:217–243

    Article  Google Scholar 

  4. Bekhit AE, Faustman C (2005) Metmyoglobin reducing activity: a review. Meat Sci 71:407–439

    Article  CAS  Google Scholar 

  5. Luciano G, Monahan FJ, Vasta V, Pennisi P, Bella M, Priolo A (2009) Lipid and colour stability of meat from lambs fed fresh herbage or concentrate. Meat Sci 82:193–199

    Article  CAS  Google Scholar 

  6. Wittenberg JB (1970) Myoglobin-facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle. Physiol Rev 50:559

    CAS  Google Scholar 

  7. Lanari MC, Cassens RG (1991) Mitochondrial activity and beef muscle color stability. J Food Sci 56:1476–1479

    Article  CAS  Google Scholar 

  8. Tang J, Faustman C, Mancini RA, Seyfert M, Hunt MC (2005) Mitochondrial reduction of metmyoglobin: dependence on the electron transport chain. J Agric Food Chem 53:5449–5455

    Article  CAS  Google Scholar 

  9. Madhavi DL, Carpenter CH (1993) Aging and processing affect color, metmyoglobin reductase and oxygen consumption of beef muscles. J Food Sci 58:939–942

    Article  CAS  Google Scholar 

  10. Tang J, Faustman C, Hoagland TA, Mancini RA, Seyfert M, Hunt MC (2005) Postmortem oxygen consumption by mitochondria and its effects on myoglobin form and stability. J Agric Food Chem 53:1223–1230

    Article  CAS  Google Scholar 

  11. Watts BM, Kendrick J, Zipser MW, Hutchins B, Saleh B (1966) Enzymatic reducing pathways in meat. J Food Sci 31:855–862

    Article  CAS  Google Scholar 

  12. Reddy LM, Carpenter CH (1991) Determination of metmyoglobin reductase activity in bovine skeletal muscles. J Food Sci 56:1161–1164

    Article  CAS  Google Scholar 

  13. Mclaren K (1987) Colour space, colour scales and colour difference. In: McDonald R (ed) Colour physics for industry, 2nd edn. Dyers Company Publications Trust, Bradford

    Google Scholar 

  14. Smith AL (1967) Preparation, properties, and conditions for assay of mitochondria: slaughterhouse material, small-scale. Method Enzymol 10:81–86

    Article  CAS  Google Scholar 

  15. Estabrook RW (1967) Mitochondrial respiratory control and the polarographic measurement of ADP: O ratios. Methods Enzymol 10:41–47

    Article  CAS  Google Scholar 

  16. Mikkelsen A, Juncher D, Skibsted LH (1999) Metmyoglobin reductase activity in porcine m. longissimus dorsi muscle. Meat Sci 51:155–161

    Article  CAS  Google Scholar 

  17. Tang J, Faustman C, Hoagland TA (2004) Krzywicki revisited: equations for spectrophotometric determination of myoglobin redox forms in aqueous meat extracts. J Food Sci 69:C717–C720

    Article  CAS  Google Scholar 

  18. Kim YHB, Frandsen M, Rosenvold K (2011) Effect of ageing prior to freezing on colour stability of ovine longissimus muscle. Meat Sci 88:332–337

    Article  Google Scholar 

  19. Mckenna DR, Mies PD, Baird BE, Pfeiffer KD, Ellebracht JW, Savell JW (2005) Biochemical and physical factors affecting discoloration characteristics of 19 bovine muscles. Meat Sci 70:665–682

    Article  CAS  Google Scholar 

  20. Renerre M, Labas R (1987) Biochemical factors influencing metmyoglobin formation in beef muscles. Meat Sci 19:151–165

    Article  CAS  Google Scholar 

  21. Echevarne C, Renerre M, Labas R (1990) Metmyoglobin reductase activity in bovine muscles. Meat Sci 27:161–172

    Article  CAS  Google Scholar 

  22. Kim YH, Keeton JT, Smith SB, Berghman LR, Savell JW (2009) Role of lactate dehydrogenase in metmyoglobin reduction and color stability of different bovine muscles. Meat Sci 83:376–382

    Article  CAS  Google Scholar 

  23. King DA, Shackelford SD, Rodriguez AB, Wheeler TL (2011) Effect of time of measurement on the relationship between metmyoglobin reducing activity and oxygen consumption to instrumental measures of beef longissimus color stability. Meat Sci 87:26–32

    Article  CAS  Google Scholar 

  24. Hood DE (1980) Factors affecting the rate of metmyoglobin accumulation in pre-packaged beef. Meat Sci 4:247–265

    Article  CAS  Google Scholar 

  25. Briand M, Talmant A, Briand Y, Monin G, Durand R (1981) Metabolic types of muscle in the sheep: I. Myosin ATPase, gloycolytic, and mitochondrial enzyme activities. Eur J Appl Physiol Occup Physiol 46:347–358

    Article  CAS  Google Scholar 

  26. O’Keeffe M, Hood DE (1982) Biochemical factors influencing metmyoglobin formation on beef from muscles of differing colour stability. Meat Sci 7:209–228

    Article  Google Scholar 

  27. Hunt MC, Hedrick HB (1977) Profile of fiber types and related properties of five bovine muscles. J Food Sci 42:513–517

    Article  CAS  Google Scholar 

  28. Richards MP, Modra AM, Li R (2002) Role of deoxyhemoglobin in lipid oxidation of washed cod muscle mediated by trout, poultry and beef hemoglobins. Meat Sci 62:157–163

    Article  CAS  Google Scholar 

  29. Seyfert M, Mancini RA, Hunt MC, Tang J, Faustman C (2007) Influence of carbon monoxide in package atmospheres containing oxygen on colour, reducing activity, and oxygen consumption of five bovine muscles. Meat Sci 75:432–442

    Article  CAS  Google Scholar 

  30. Guderley H, Pierre JS, Couture P, Hulbert AJ (1997) Plasticity of the properties of mitochondria from rainbow trout red muscle with seasonal acclimatization. Fish Physiol Biochem 16:531–541

    Article  CAS  Google Scholar 

  31. Raw I, Petragnani N, Nogueira OC (1960) Studies of electron transport enzymes. IV. Oxidation and reduction of cytochrome b 5 by rat liver mitochondria. J Biol Chem 235:1517–1520

    CAS  Google Scholar 

  32. Atkinson JL, Follett MJ, Ratcliff PW (1969) Post-mortem changes in the oxygen uptake and NAD content of lamb muscularis semimembranosus. Nature 223:1372–1373

    Article  CAS  Google Scholar 

  33. Feldhusen F, Warnatz A, Erdmann R, Wenzel S (1995) Influence of storage time on parameters of colour stability of beef. Meat Sci 40:235–243

    Article  CAS  Google Scholar 

  34. Bekhit AE, Geesink GH, Ilian MA, Morton JD, Sedcole R, Bickerstaffe R (2003) Particulate metmyoglobin reducing activity and its relationship with meat color. J Agric Food Chem 51:6026–6035

    Article  CAS  Google Scholar 

  35. Bekhit AE, Geesink GH, Morton JD, Bickerstaffe R (2001) Metmyoglobin reducing activity and colour stability of ovine longissimus muscle. Meat Sci 57:427–435

    Article  CAS  Google Scholar 

  36. Rady OG, Monahan FJ, Mooney MT (2001) Oxymyoglobin in bovine muscle systems as affected by oxidizing lipids, vitamin E and metmyoglobin reductase activity. J Muscle Foods 12:19–35

    Article  Google Scholar 

  37. Renerre M (1984) Variabilité entre muscles et entre animaux de lastabilité de la couleur des viandes bovines. Sci Aliment 4:567–584

    Google Scholar 

  38. Ramanathan R, Mancini RA, Joseph P, Yin S, Tatiyaborworntham N, Petersson KH, Sun Q, Konda MR (2011) Effects of lactate on ground lamb colour stability and mitochondria-mediated metmyoglobin reduction. Food Chem 126:166–171

    Article  CAS  Google Scholar 

  39. Strittmatter CF, Ball EG (1952) A hemochromogen component of liver microsomes. Proc Natl Acad Sci USA 38:19–25

    Article  CAS  Google Scholar 

  40. Saleh BA, Watts BE (1968) Substrates and intermediates in the enzymatic reduction of metmyoglobin in ground beef. J Food Sci 33:353–358

    Article  CAS  Google Scholar 

  41. Atkinson JL, Follett MJ (1973) Biochemical studies on the discoloration of fresh meat. Int J Food Sci Tech 8:51–58

    Article  CAS  Google Scholar 

Download references

Acknowledgments

We gratefully acknowledge the financial support by Nature Science Foundation of China (Project No: 31071624) and the Ministry of Agriculture of China (China Agriculture Research System-39, CARS-39).

Conflict of interest

Ruitong Dai has received research grants from Nature Science Foundation of China (Project No: 31071624) and the Ministry of Agriculture of China (China Agriculture Research System-39, CARS-39). Li Xie, Zhenyu Wang, Xingmin Li, Hailing Luo, Changwei Ma, Ruitong Dai declare no conflict of interest.

Compliance with Ethics Requirements

All institutional and national guidelines for the care and use of laboratory animals were followed.

Author information

Authors and Affiliations

Authors

Corresponding authors

Correspondence to Changwei Ma or Ruitong Dai.

Additional information

Ruitong Dai and Changwei Ma have equally contributed to this manuscript.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Gao, X., Xie, L., Wang, Z. et al. Effect of postmortem time on the metmyoglobin reductase activity, oxygen consumption, and colour stability of different lamb muscles. Eur Food Res Technol 236, 579–587 (2013). https://doi.org/10.1007/s00217-012-1903-8

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00217-012-1903-8

Keywords

Navigation