Advertisement

Journal of Food Science and Technology

, Volume 55, Issue 5, pp 1641–1647 | Cite as

A streamlined isolation method and the autoxidation profiles of tuna myoglobin

  • Mala Nurilmala
  • Hideki Ushio
  • Shugo Watabe
  • Yoshihiro Ochiai
Original Article

Abstract

Determination of the redox state of myoglobin (Mb) gives useful information for evaluating the quality of tuna meat. To attain this purpose, a fast streamlined method has been established basically based on preparative native gel electrophoresis to isolate Mb from the dark muscle of Pacific bluefin tuna. Crude Mb fraction was prepared from dark muscle by ammonium sulfate saturation fractionation and subsequently Mb was purified by preparative native gel electrophoresis under the isoelectric pH of the Mb, resulting in absorption (or trapping) of all the contaminating proteins in the gel. Purified Mb was converted to oxy form with a trace amount of sodium hydrosulfite, and subsequently dialyzed against 50 mM sodium citrate (pH 5.6) or 50 mM sodium phosphate (pH 6.5). The purified tuna Mb was examined for the temperature and pH dependencies of autoxidation using horse Mb as a reference. Tuna Mb was oxidized 2.5–3 times faster than horse Mb irrespective of the pH conditions examined. The highest autoxidation rates both at 0 and 37 °C were observed at pH 5.6. These data were comparable to those obtained for Mbs isolated by conventional chromatographic methods.

Keywords

Myoglobin Streamlined isolation Preparative electrophoresis Autoxidation Tuna 

Notes

Acknowledgements

The authors are grateful for the assistance of Dr. Hina Satone in the electrophoretic analysis. This work was financially supported in part by the a grant-in-aid from the Fisheries Agency of Japan to the author YO.

Compliance with ethical standards

Conflict of interest

The authors declare no conflict of interest.

Supplementary material

13197_2018_3068_MOESM1_ESM.doc (105 kb)
Supplementary material 1 (DOC 105 kb)

References

  1. Alderton AL, Faustman C, Liebler DC, Hill DW (2003) Induction of redox instability of bovine myoglobin by adduction with 4-hydroxy-2-nonenal. Biochem 42:4398–4405CrossRefGoogle Scholar
  2. Birnbaum GI, Evans SV, Przybylska M, Rose DR (1994) 1.70 Å resolution structure of myoglobin from yellowfin tuna. An example of a myoglobin lacking the D helix. Acta Cryst D 50:283–289CrossRefGoogle Scholar
  3. Chaijan M (2008) Review: lipid and myoglobin oxidations in muscle foods. Songklanakarin J Sci Technol 30:47–53Google Scholar
  4. Chen WL, Chow CJ (2001) Studies on the physicochemical properties of milkfish myoglobin. J Food Biochem 25:157–174CrossRefGoogle Scholar
  5. Chow CJ, Ochiai Y, Hashimoto K (1985) Effect of freezing and thawing on the autoxidation of bluefin tuna myoglobin. Bull Jpn Soc Sci Fish 51:2073–2078CrossRefGoogle Scholar
  6. Chow CJ, Ochiai Y, Watabe S (2004) Effect of frozen temperature on autoxidation and aggregation of bluefin tuna myoglobin in solution. J Food Biochem 28:123–134CrossRefGoogle Scholar
  7. Chow CJ, Ochiai Y, Watabe S, Hashimoto K (1987) Autoxidation of bluefin tuna myoglobin associated with freezing and thawing. J Food Sci 52:589–591CrossRefGoogle Scholar
  8. Chow CJ, Ochiai Y, Watabe S, Hashimoto K (1989) Reduced stability and accelerated autoxidation of tuna myoglobin in association with freezing and thawing. J Agric Food Chem 37:1391–1395CrossRefGoogle Scholar
  9. Chow CJ, Yang JI, Lee PF, Ochiai Y (2009) Effect of acid and alkaline pretreatment on the discoloration rates of dark muscle and myoglobin extract of skinned tilapia fillet during iced storage. Fish Sci 75:1481–1488CrossRefGoogle Scholar
  10. Faustman C, Sun Q, Mancini R, Suman SP (2010) Myoglobin and lipid oxidation interactions: mechanistic bases and control. Meat Sci 86:86–94CrossRefGoogle Scholar
  11. Flögel U, Fago A, Rassaf T (2010) Keeping the heart in balance: the functional interactions of myoglobin with nitrogen oxides. J Exp Biol 213:2726–2733CrossRefGoogle Scholar
  12. Joseph P, Suman SP, Li S, Beach CM, Steinke L, Fontaine M (2010) Characterization of bison (Bison bison) myoglobin. Meat Sci 84:71–78CrossRefGoogle Scholar
  13. Kitahara Y, Matsuoka A, Kobayashi N, Shikama K (1990) Autoxidation of myoglobin from bigeye tuna fish (Thunnus obesus). Biochim Biophys Acta 1038:23–28CrossRefGoogle Scholar
  14. Kobayashi G, Mizuguchi T, Matsuoka A (2014) Isolation and autooxidation profile of fish myoglobin from hoki (Macruronus magellanicus). Fukushima J Med Sci 60:31–34CrossRefGoogle Scholar
  15. Livingston DJ, Brown WD (1981) The chemistry of myoglobin and its reactions. Food Technol 35:244–252Google Scholar
  16. Madden PW, Babcock MJ, Vayda ME, Cashon RE (2004) Structural and kinetic characterization of myoglobins from eurythermal and stenothermal fish species. Comp Biochem Physiol B Biochem Mol Biol 137:341–350CrossRefGoogle Scholar
  17. Margolis J, Corthals G, Horvath ZS (1995) Preparative reflux electrophoresis. Electrophoresis 16:98–100CrossRefGoogle Scholar
  18. Nurilmala M, Ushio H, Kaneko G, Ochiai Y (2013) Assessment of commercial quality evaluation of yellowfin tuna Thunnus albacares meat based on myoglobin properties. Food Sci Technol Res 19:237–243CrossRefGoogle Scholar
  19. Ochiai Y, Ueki N, Watabe S (2009) Effects of point mutations on the structural stability of tuna myoglobins. Comp Biochem Physiol B Biochem Mol Biol 153:223–228CrossRefGoogle Scholar
  20. Ochiai Y, Watanabe Y, Ozawa H, Ikegami S, Uchida N, Watabe S (2010) Thermal denaturation profiles of tuna myoglobin. Biosci Biotech Biochem 74:1673–1679CrossRefGoogle Scholar
  21. Rumbo M, Chirdo FG, Giorgieri SE, Fossati CA, Anon MC (1999) Preparative fractionation of gliadins by electrophoresis at pH 3.1 (A-PAGE). J Agric Food Chem 47:3243–3247CrossRefGoogle Scholar
  22. Sandri M, Rizzi C, Rossini K, Catani C, Cantini M, Spina M (1999) Purification of myosin heavy chain isoforms by electroendosmosis preparative gel electrophoresis: characterization of embryonic slow myosin heavy chain. Basic Appl Myol 9:71–78Google Scholar
  23. Seelert H, Krause F (2008) Preparative isolation of protein complexes and other bioparticles by elution from polyacrylamide gels. J Electrophor 29:2617–2636CrossRefGoogle Scholar
  24. Sen AR, Naveena BM, Muthukumar M, Vaithiyanathan S (2014) Colour, myoglobin denaturation and storage stability of raw and cooked mutton chops at different end point cooking temperature. J Food Sci Technol 51:970–975CrossRefGoogle Scholar
  25. Tang J, Faustman C, Hoagland TA (2004) Krzywicki revisited: equations for spectrophotometric determination of myoglobin redox forms in aqueous meat extract. J Food Sci 69:C717–C720CrossRefGoogle Scholar
  26. Thiansilakul Y, Benjakul S, Richards MP (2011) Isolation, characterization, and stability of myoglobin from eastern little tuna (Euthynnus affinis) dark muscle. Food Chem 124:254–261CrossRefGoogle Scholar
  27. Ueki N, Ochiai Y (2004) Primary structure and thermostability of bigeye tuna myoglobin in relation to those from other scombridae fish. Fish Sci 70:875–884CrossRefGoogle Scholar
  28. Ueki N, Ochiai Y (2006) Effect of amino acid replacement on the structural stability of fish myoglobin. J Biochem 140:649–656CrossRefGoogle Scholar
  29. Ueki N, Chow CJ, Ochiai Y (2005) Characterization of bullet tuna myoglobin with reference to thermostability–structure relationship. J Agric Food Chem 53:4968–4975CrossRefGoogle Scholar
  30. Yin S, Faustman C, Tatiyaborworntham N, Ramanathan R, Maheswarappa NB, Mancini RA, Joseph P, Suman SP, Sun Q (2011) Species-specific myoglobin oxidation. J Agric Food Chem 59:12198–12203CrossRefGoogle Scholar

Copyright information

© Association of Food Scientists & Technologists (India) 2018

Authors and Affiliations

  • Mala Nurilmala
    • 1
  • Hideki Ushio
    • 2
  • Shugo Watabe
    • 3
  • Yoshihiro Ochiai
    • 4
  1. 1.Department of Aquatic Product Technology, Faculty of Fisheries and Marine SciencesBogor Agricultural UniversityBogorIndonesia
  2. 2.Department of Aquatic BioscienceThe University of TokyoBunkyoJapan
  3. 3.School of Marine BioscienceKitasato UniversityMinami, SagamiharaJapan
  4. 4.Graduate School of Agricultural ScienceTohoku UniversitySendaiJapan

Personalised recommendations