Skip to main content

Advertisement

SpringerLink
Log in

In Vitro Zinc Protoporphyrin IX Formation in Different Meat Sources Related to Potentially Important Intrinsic Parameters

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

Abstract

For several years, researchers have studied the formation of zinc protoporphyrin IX in meat, as it is considered to be an important natural colouring agent in dry cured or fermented meat products in the absence of nitrite and/ or nitrate. Until now, however, mainly pork meat is used for these investigations. The goal of this research was to relate in vitro zinc protoporphyrin IX and protoporphyrin IX formation in eight meat sources (chicken, turkey, pork, lamb, beef, veal, horse and porcine liver) to eight intrinsic parameters using partial least squares regression (PLS) analysis. Significant differences in pH, initial metmyoglobin formation, metmyoglobin reduction ability, total heme, zinc chelatase activity, and total iron and zinc concentration between meat sources were found. Water activity, however, was not significantly different between meat sources. Liver tissue and horse meat showed the best ability to form zinc protoporphyrin IX. Formation of protoporphyrin IX was limited in all meat sources. PLS analysis revealed that mainly zinc chelatase activity, followed by total heme, total iron and zinc content, were predominant intrinsic parameters to explain variations in zinc protoporphyrin IX formation. These findings could be important for meat industry in order to establish the production of red coloured nitrite-free meat products.

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

Access this article

Log in via an institution

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

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4

Similar content being viewed by others

References

  • Adamsen, C. E., Møller, J. K. S., Laursen, K., Olsen, K., & Skibsted, L. H. (2006). Zn-porphyrin formation in cured meat products: effect of added salt and nitrite. Meat Science, 72(4), 672–679.

    Article  CAS  Google Scholar 

  • Ajioka, R. S., Phillips, J. D., & Kushner, J. P. (2006). Biosynthesis of heme in mammals. Biochimica et Biophysica Acta, 1763(7), 723–736.

    Article  CAS  Google Scholar 

  • AMSA. (2012). AMSA Meat Color Measurement Guidelines Measurement.

  • Becker, E. M., Westermann, S., Hansson, M., & Skibsted, L. H. (2012). Parallel enzymatic and non-enzymatic formation of zinc protoporphyrin IX in pork. Food Chemistry, 130(4), 832–840.

    Article  CAS  Google Scholar 

  • Belgische voedingsmiddelentabel, Nubel vzw, 5e editie (2010).

  • Chan, J. T. Y., Omana, D. A., & Betti, M. (2011). Effect of ultimate pH and freezing on the biochemical properties of proteins in Turkey breast meat. Food Chemistry, 127(1), 109–117.

    Article  CAS  Google Scholar 

  • Chau, T. T., Ishigaki, M., Kataoka, T., & Taketani, S. (2010). Porcine ferrochelatase: the relationship between iron-removal reaction and the conversion of heme to Zn-protoporphyrin. Bioscience, Biotechnology, and Biochemistry, 74(7), 1415–1420.

    Article  CAS  Google Scholar 

  • Chau, T. T., Ishigaki, M., Kataoka, T., & Taketani, S. (2011). Ferrochelatase catalyzes the formation of Zn-protoporphyrin of dry-cured ham via the conversion reaction from heme in meat. Journal of Agricultural and Food Chemistry, 59(22), 12238–12245.

    Article  CAS  Google Scholar 

  • Cross, A. A. J., Harnly, J. J. M., Ferrucci, L. M. L., Risch, A., Mayne, S. T., & Sinha, R. (2012). Developing a heme iron database for meats according to meat type, cooking method and doneness level. Food and Nutrition Sciences, 3(7), 905–913.

    Article  CAS  Google Scholar 

  • Dailey, H. A., Dailey, T. A., Wu, C., Medlock, A. E., Wang, K., Rose, J. P., & Wang, B. (2000). Ferrochelatase at the millennium: structures , mechanisms and [ 2Fe-2S ] clusters. Cellular and Molecular Life Sciences, 57, 1909–1926.

    Article  CAS  Google Scholar 

  • De Maere, H., Fraeye, I., De Mey, E., Dewulf, L., Michiels, C., Paelinck, H., & Chollet, S. (2016). Formation of naturally occurring pigments during the production of nitrite-free dry fermented sausages. Meat Science, 114, 1–7.

    Article  CAS  Google Scholar 

  • Devine, C., & Dikeman, M. (2004). Encyclopedia of Meat Sciences ed. Elsevier Acad: Press, Oxford.

    Google Scholar 

  • Durek, J., Bolling, J. S., Knorr, D., Schwägele, F., & Schlüter, O. (2012). Effects of different storage conditions on quality related porphyrin fluorescence signatures of pork slices. Meat Science, 90(1), 252–258.

    Article  CAS  Google Scholar 

  • Elroy, N. N., Rogers, J., Mafi, G. G., Van Overbeke, D. L., Hartson, S. D., & Ramanathan, R. (2015). Species-specific effects on non-enzymatic metmyoglobin reduction in vitro. Meat Science, 105, 108–113.

    Article  CAS  Google Scholar 

  • Estévez, M., & Cava, R. (2004). Lipid and protein oxidation, release of iron from heme molecule and colour deterioration during refrigerated storage of liver pâté. Meat Science, 68(4), 551–558.

    Article  Google Scholar 

  • Ferreira, G. C. (1999). Ferrochelatase. The International Journal of Biochemistry & Cell Biology, 31(10), 995–1000.

    Article  CAS  Google Scholar 

  • Gill, C. O. (2005). Safety and storage stability of horse meat for human consumption. Meat Science, 71(3), 506–513.

    Article  CAS  Google Scholar 

  • Grossi, A. B., do Nascimento, E. S. P., Cardoso, D. R., & Skibsted, L. H. (2014). Proteolysis involvement in zinc–protoporphyrin IX formation during Parma ham maturation. Food Research International, 56, 252–259.

    Article  CAS  Google Scholar 

  • Gurtler, J. B., Doyle, M. P., & Kornacki, J. L. (2014). The microbiological safety of spices and low-water activity foods and spices. Food microbiology and food safety. New York: Springer Science.

    Google Scholar 

  • Hunter, G. A., Sampson, M. P., & Ferreira, G. C. (2008). Metal ion substrate inhibition of ferrochelatase. The Journal of Biological Chemistry, 283(35), 23685–23691.

    Article  CAS  Google Scholar 

  • International Organization for Standardization (1997). Determination of moisture content, ISO 1442:1997 standard.

  • Ishikawa, H., Yoshihara, M., Baba, A., Kawabuchi, T., Sato, M., Numata, M., & Matsumoto, K. (2006). Formation of zinc protoporphyrin IX from myoglobin with pork loin extract. Journal of the Faculty of Agriculture, 51(1), 93–97.

    CAS  Google Scholar 

  • Ishikawa, H., Kawabuchi, T., Kawakami, Y., Sato, M., Numata, M., & Matsumoto, K. (2007). Formation of zinc protoporphyrin IX and protoporphyrin IX from oxymyoglobin in porcine heart mitochondria. Food Science and Technology Research, 13(1), 85–88.

    Article  CAS  Google Scholar 

  • Jacobs, J. M., Sinclair, P. R., Sinclair, J. F., Gorman, N., Walton, H. S., Wood, S. G., & Nichols, C. (1998). Formation of zinc protoporphyrin in cultured hepatocytes: effects of ferrochelatase inhibition, iron chelation or lead. Toxicology, 125(2–3), 95–105.

    Article  CAS  Google Scholar 

  • Jay, J. M., Loessner, M. J., & Golden, D. A. (2005). Modern food microbiology (7th ed.). New York: Springer Science.

    Google Scholar 

  • Klont, R. E., Barnier, V. M. H., Van Dijk, A., Smulders, F. J. M., Hoving-Bolink, A. H., Hulsegge, B., & Eikelenboom, G. (2000). Effects of rate of pH fall, time of deboning, aging period, and their interaction on veal quality characteristics. Journal of Animal Science, 78(7), 1845–1851.

    Article  CAS  Google Scholar 

  • Labbé, R. F., Vreman, H. J., & Stevenson, D. K. (1999). Zinc protoporphyrin: a metabolite with a mission. Clinical Chemistry, 45(12), 2060–2072.

    Google Scholar 

  • Lammens, V., Peeters, E., De Maere, H., De Mey, E., Paelinck, H., Leyten, J., & Geers, R. (2007). A survey of pork quality in relation to pre-slaughter conditions, slaughterhouse facilities, and quality assurance. Meat Science, 75(3), 381–387.

    Article  CAS  Google Scholar 

  • Lindahl, G. (2005). Colour Characteristics of Fresh Pork. Doctor’s dissertation.

  • Litwinczuk, A., Florek, M., Skalecki, P., & Litwinczuk, Z. (2008). Chemical composition and physicochemical properties of horse meat from the longissimus. Journal of Muscle Foods, 19(3), 223–236.

    Article  CAS  Google Scholar 

  • Lombardi-Boccia, G., Martinez-Dominguez, B., & Aguzzi, A. (2002). Total heme and non-heme iron in raw and cooked meats. Journal of Food Chemistry and Toxicology, 67(5), 1738–1741.

    CAS  Google Scholar 

  • Mancini, R. A., Seyfert, M., & Hunt, M. C. (2008). Effects of data expression, sample location, and oxygen partial pressure on initial nitric oxide metmyoglobin formation and metmyoglobin-reducing-activity measurement in beef muscle. Meat Science, 79(2), 244–251.

    Article  CAS  Google Scholar 

  • Mikkelsen, A., Juncher, D., & Skibsted, L. H. (1999). Metmyoglobin reductase activity in porcine M. longissimus dorsi muscle. Meat Science, 51(2), 155–161.

    Article  CAS  Google Scholar 

  • Parolari, G., Benedini, R., & Toscani, T. (2009). Color formation in nitrite-free dried hams as related to Zn-protoporphyrin IX and Zn-chelatase activity. Journal of Food Science, 74(6), 413–418.

    Article  Google Scholar 

  • Samel, L. M., Hunt, M. C., Kropf, D. H., Hachmeister, K. A., & Johnson, D. E. (2002). Comparison of assays for metmyoglobin reducing ability in beef inside and outside. Food Chemistry and Toxicology, 67(3), 978–984.

    Google Scholar 

  • Schneider, J., Wulf, J., Surowsky, B., Schmidt, H., Schwägele, F., & Schlüter, O. (2008). Fluorimetric detection of protoporphyrins as an indicator for quality monitoring of fresh intact pork meat. Meat Science, 80(4), 1320–1325.

    Article  CAS  Google Scholar 

  • Wakamatsu, J., Nishimura, T., & Hattori, A. (2004a). A Zn-porphyrin complex contributes to bright red color in Parma ham. Meat Science, 67(1), 95–100.

    Article  CAS  Google Scholar 

  • Wakamatsu, J., Okui, J., Ikeda, Y., Nishimura, T., & Hattori, A. (2004b). Establishment of a model experiment system to elucidate the mechanism by which Zn-protoporphyrin IX is formed in nitrite-free dry-cured ham. Meat Science, 68(2), 313–317.

    Article  CAS  Google Scholar 

  • Wakamatsu, J., Okui, J., Hayashi, N., Nishimura, T., & Hattori, A. (2007). Zn protoporphyrin IX is formed not from heme but from protoporphyrin IX. Meat Science, 77(4), 580–586.

    Article  CAS  Google Scholar 

  • Wakamatsu, J., Odagiri, H., Nishimura, T., & Hattori, A. (2009). Quantitative determination of Zn protoporphyrin IX, heme and protoporphyrin IX in Parma ham by HPLC. Meat Science, 82(1), 139–142.

    Article  CAS  Google Scholar 

  • Wakamatsu, J., Murakami, N., & Nishimura, T. (2015). A comparative study of zinc protoporphyrin IX-forming properties of animal by-products as sources for improving the color of meat products. Animal Science Journal, 86, 547–552.

    Article  CAS  Google Scholar 

  • Warriss, P. D., Brown, S. N., Adams, S. J., & Lowe, D. B. (1990). Variation in haem pigment concentration and colour in meat from British pigs. Meat Science, 28(4), 321–329.

    Article  CAS  Google Scholar 

  • Zhu, L. G., & Brewer, M. S. (1998). Metmyoglobin reducing capacity of fresh normal, PSE, and DFD pork during retail display. Journal of Food Science, 63(3), 390–393.

    Article  CAS  Google Scholar 

Download references

Acknowledgments

This work was performed with financial support of internal funding of KU Leuven.

Author information

Authors and Affiliations

  1. Research Group for Technology and Quality of Animal Products, Department M2S, member of Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven Technology Campus Ghent, Gebroeders De Smetstraat 1, B-9000, Ghent, Belgium

    Hannelore De Maere, Marlies Govaert, Eveline De Mey, Hubert Paelinck & Ilse Fraeye

  2. IICV – Institut Charles Viollette, EA 7394, USC 1281, ISA Lille, F-59000, Lille, France

    Sylvie Chollet

  3. UGent - Lanupro Laboratory for Animal Nutrition and Animal Product Quality, Faculty of Bioscience Engineering, Ghent University, Proefhoevestraat 10, 9090, Melle, Belgium

    Erik Claeys

  4. Centre for Food and Microbial Technology, Department M2S, member of Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 23 box 2457, B-3001, Leuven, Belgium

    Chris Michiels

Authors
  1. Hannelore De Maere
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Sylvie Chollet
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Erik Claeys
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Chris Michiels
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Marlies Govaert
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Eveline De Mey
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Hubert Paelinck
    View author publications

    You can also search for this author in PubMed Google Scholar

  8. Ilse Fraeye
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Ilse Fraeye.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

De Maere, H., Chollet, S., Claeys, E. et al. In Vitro Zinc Protoporphyrin IX Formation in Different Meat Sources Related to Potentially Important Intrinsic Parameters. Food Bioprocess Technol 10, 131–142 (2017). https://doi.org/10.1007/s11947-016-1804-0

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11947-016-1804-0

Keywords

Search

Navigation