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Journal of Food Science and Technology

, Volume 56, Issue 12, pp 5354–5361 | Cite as

A simple but quantitative method for non-destructive monitoring of myoglobin redox forms inside the meat

  • Thien Nguyen
  • Jae Gwan KimEmail author
Original Article
  • 26 Downloads

Abstract

This study aims at exploring a simple and quantitative method for non-destructive monitoring of the myoglobin redox forms inside of beef. The modified Beer–Lambert law was employed to derive an equation that delineates a relationship between attenuance differences and oxy-, deoxy-, and met-myoglobin proportions. An experiment with forty-three well-bled muscle beef samples during 7 days of storage was performed to validate the equation. Firstly, the reflection spectra were collected from the beef samples using a probe consisting of a light source and a light detector. Secondly, the attenuance differences, A630-615 and A578-567, were calculated from the measured spectra. Finally, these attenuance differences were placed into the derived equation to determine the proportions of the three myoglobin redox forms. Both the met-myoglobin proportion and meat oxygenation computed via the attenuance differences established a strong correlation with the ones estimated using the whole spectrum (R2 > 0.88). The experimental results suggest the potential of using the attenuance at five wavelengths (524, 567, 578, 615, and 630 nm) to monitor oxy-, deoxy-, and met-myoglobin inside of beef in a simple and fast manner with little to no sample preparation.

Keywords

Oxy-myoglobin Deoxy-myoglobin Met-myoglobin Meat oxygenation Attenuance difference Modified Beer–Lambert law 

Notes

Acknowledgements

This work was supported by GIST Research Institute (GRI), and “Biomedical Integrated Technology Research” Project through a grant provided by GIST in 2019.

References

  1. Boles JA, Pegg R (2010) Meat color. Montana State University and Saskatchewan Food Product Innovation Program, University of Saskatchewan, Saskatoon, SaskatchewanGoogle Scholar
  2. Bowen WJ (1949) The absorption spectra and extinction coefficients of myoglobin. J Biol Chem 179(1):235–245PubMedGoogle Scholar
  3. Chen L, Zhang H, Liu Q, Pang X, Zhao X, Yang H (2019) Sanitising efficacy of lactic acid combined with low-concentration sodium hypochlorite on Listeria innocua in organic broccoli sprouts. Int J Food Microbiol 295:41–48.  https://doi.org/10.1016/j.ijfoodmicro.2019.02.014 CrossRefPubMedGoogle Scholar
  4. Du M, McCormick RJ (2009) Applied muscle biology and meat science. CRC Press, Boca RatonCrossRefGoogle Scholar
  5. Einstein G, Udayakumar K, Aruna PR, Koteeswaran D, Ganesan S (2016) Diffuse reflectance spectroscopy for monitoring physiological and morphological changes in oral cancer. Opt Int J Light Electron Opt 127(3):1479–1485.  https://doi.org/10.1016/j.ijleo.2015.11.045 CrossRefGoogle Scholar
  6. Franke WC, Solberg M (1971) Quantitative determination of metmyoglobin and total pigment in an intact meat sample using reflectance spectrophotometry. J Food Sci 36:515–519.  https://doi.org/10.1111/j.1365-2621.1971.tb06404.x CrossRefGoogle Scholar
  7. Hamm R (1960) Biochemistry of meat hydration. Adv Food Res 10:355–463.  https://doi.org/10.1016/S0065-2628(08)60141-X CrossRefPubMedGoogle Scholar
  8. Hernández B, Sáenz C, Alberdi C, Diñeiro JM (2015) Comparison between two different methods to obtain the proportions of myoglobin redox forms on fresh meat from reflectance measurements. J Food Sci Technol 52(12):8212–8219.  https://doi.org/10.1007/s13197-015-1917-x CrossRefPubMedPubMedCentralGoogle Scholar
  9. Hui YH, Nip WK, Rogers R (2001) Meat science and applications. CRC Press, Boca RatonGoogle Scholar
  10. Hunt MC, Acton JC, Benedict RC, Calkins CR, Cornforth DP, Jeremiah LE, Olson DG, Salm CP, Savell JW, Shivas SD (1991) Guidelines for meat color evaluation. In: 44th Annual reciprocal meat conference, American Meat Science Association, Savoy, IllinoisGoogle Scholar
  11. Jacques SL (2013) Optical properties of biological tissues: a review. Phys Med Biol 58:R37.  https://doi.org/10.1088/0031-9155/58/14/5007 CrossRefPubMedGoogle Scholar
  12. Krzywicki K (1979) Assessment of relative content of myoglobin, oxymyoglobin and metmyoglobin at the surface of beef. Meat Sci 3(1):1–10.  https://doi.org/10.1016/0309-1740(79)90019-6 CrossRefPubMedGoogle Scholar
  13. Mancini RA, Hunt MC (2005) Current research in meat color. Meat Sci 71(1):100–121.  https://doi.org/10.1016/j.meatsci.2005.03.003 CrossRefPubMedGoogle Scholar
  14. Mancini R, Hunt M, Kropf D (2003) Reflectance at 610 nanometers estimates oxymyoglobin content on the surface of ground beef. Meat Sci 64(2):157–162.  https://doi.org/10.1016/S0309-1740(02)00174-2 CrossRefPubMedGoogle Scholar
  15. Nachabé R, Hendriks BH, Mvd V, Desjardins AE, Sterenborg HJ (2010) Estimation of biological chromophores using diffuse optical spectroscopy: benefit of extending the UV–Vis wavelength range to include 1000–1600 nm. Biomed Opt Express 1(5):1432–1442.  https://doi.org/10.1364/BOE.1.001432 CrossRefPubMedPubMedCentralGoogle Scholar
  16. Nachabé R, Evers DJ, Hendriks BH, Lucassen GW, Van der Voort M, Rutgers EJ, Peeters MJV, Van der Hage JA, Oldenburg HS, Wesseling J (2011) Diagnosis of breast cancer using diffuse optical spectroscopy from 500 to 1600 nm: comparison of classification methods. J Biomed Opt 16(8):087010.  https://doi.org/10.1117/1.3611010 CrossRefPubMedGoogle Scholar
  17. Nguyen T, Nguyen KP, Lee JB, Kim JG (2016a) Met-myoglobin formation, accumulation, degradation, and myoglobin oxygenation monitoring based on multiwavelength attenuance measurement in porcine meat. J Biomed Opt 21(5):57002.  https://doi.org/10.1117/1.JBO.21.5.057002 CrossRefPubMedGoogle Scholar
  18. Nguyen T, Nguyen KP, Kim JG (2016b) Assessment of beef freshness by monitoring oxy-, deoxy-, and met-myoglobin concentration change during storage time. In: Biomedical engineering conference (BME-HUST), IEEE, pp 65–69Google Scholar
  19. Nguyen T, Kim S, Kim JG (2019) Diffuse reflectance spectroscopy to quantify the met-myoglobin proportion and meat oxygenation inside of pork and beef. Food Chem 275:369–376.  https://doi.org/10.1016/j.foodchem.2018.09.121 CrossRefPubMedGoogle Scholar
  20. Nighswander-Rempel SP, Kupriyanov VV, Shaw RA (2005) Relative contributions of hemoglobin and myoglobin to near-infrared spectroscopic images of cardiac tissue. Appl Spectrosc 59(2):190–193.  https://doi.org/10.1366/0003702053085106 CrossRefPubMedGoogle Scholar
  21. Scholkmann F, Wolf M (2013) General equation for the differential pathlength factor of the frontal human head depending on wavelength and age. J Biomed Opt 18(10):105004.  https://doi.org/10.1117/1.JBO.18.10.105004 CrossRefPubMedGoogle Scholar
  22. Sen C, Packer L, Hänninen O (2000) Handbook of oxidants and antioxidants. Exercise. Elsevier, PhiladelphiaGoogle Scholar
  23. Stewart MR, Zipser MW, Watts BM (1965) The use of reflectance spectrophotometry for the assay of raw meat pigments. J Food Sci 30:464–469.  https://doi.org/10.1111/j.1365-2621.1965.tb01787.x CrossRefGoogle Scholar
  24. Zhao L, Zhao MY, Phey CP, Yang H (2019) Efficacy of low concentration acidic electrolysed water and levulinic acid combination on fresh organic lettuce (Lactuca sativa Var. Crispa L.) and its antimicrobial mechanism. Food Control 101:241–250.  https://doi.org/10.1016/j.foodcont.2019.02.039 CrossRefGoogle Scholar
  25. Zijlstra WG, Buursma A, Meeuwsen-Van der Roest WP (1991) Absorption spectra of human fetal and adult oxyhemoglobin, de-oxyhemoglobin, carboxyhemoglobin, and methemoglobin. Clin Chem 37(9):1633–1638PubMedGoogle Scholar

Copyright information

© Association of Food Scientists & Technologists (India) 2019

Authors and Affiliations

  1. 1.Department of Biomedical Science and EngineeringGwangju Institute of Science and TechnologyGwangjuRepublic of Korea

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