Advertisement

Fisheries Science

, 75:1481 | Cite as

Effects of acid and alkaline pretreatment on the discoloration rates of dark muscle and myoglobin extract of skinned tilapia fillet during iced storage

  • Chau-Jen Chow
  • Jing-Iong Yang
  • Pei-Fen Lee
  • Yoshihiro Ochiai
Original Article Food Science and Technology

Abstract

Discoloration profiles of dark muscle of skinned tilapia fillets were examined during iced storage after pretreatment with lactic acid (LA) or sodium carbonate (SC). During the subsequent storage, the a* values decreased gradually, and changed more rapidly when the pH was lower than 6.3. The fillet pretreated with 10% (v/v) LA exhibited the highest metmyoglobin formation ratio (MetMb%), followed by the fillet pretreated with 5% (v/v) LA, the control fillet, and the fillet pretreated with 10% (w/v) SC. The sample pretreated with 10% LA showed a marked decrease in the a* value. Discoloration of the control was not observed until the ninth day of iced storage, and no discoloration was observed up to the 11th day for the fillet pretreated with 10% SC. These fillet discoloration profiles were subsequently verified using the myoglobin (Mb) fraction prepared from the dark muscle. MetMb% of the Mb fraction gradually increased during storage, and this increase accelerated at pH values of <6.3. Discoloration of the Mb fraction also showed a similar tendency, and no significant discoloration was observed at pH values of >6.5. These results suggest that pH greatly affects the discoloration rate of the dark muscle of skinned fillet, and the critical pH for the accelerated autooxidation of tilapia Mb is in the range 6.3–6.5.

Keywords

Dark muscle Discoloration Iced storage Lactic acid Myoglobin Sodium carbonate Tilapia 

Notes

Acknowledgments

The authors would like to express their heartfelt thanks to Mr. Hon-Jen Chiou for making live tilapia specimens available. The authors also wish to thank Professor Yuh-Jwo Chu for her valuable comments and support.

References

  1. 1.
    Brown WD (1962) The concentration of myoglobin and hemoglobin in tuna flesh. J Food Sci 27:26–28CrossRefGoogle Scholar
  2. 2.
    Matsuura F, Hashimoto K (1954) Chemical studies on the red muscle (“chiai”) of fishes—II. Determinations of the content of hemoglobin, myoglobin and cytochrome c in the muscles of fishes. Nippon Suisan Gakkaishi 20:308–312Google Scholar
  3. 3.
    Matsuura F, Hashimoto K (1959) Chemical studies on the red muscle (“chiai”) of fishes—X. A new method for determination of myoglobin. Nippon Suisan Gakkaishi 24:809–815Google Scholar
  4. 4.
    Vojtechovsky J, Chu K, Berendzen J, Sweet RM, Schlichting I (1999) Crystal structures of myoglobin-ligand complexes at near-atomic resolution. Biophys J 77:2153–2174CrossRefPubMedGoogle Scholar
  5. 5.
    Suzuki N, Hashimoto K, Matsuura F (1973) Studies on the color of skipjack meat. Nippon Suisan Gakkaishi 39:35–41Google Scholar
  6. 6.
    Ochiai Y, Chow CJ, Watabe S, Hashimoto K (1988) Evaluation of tuna meat discoloration by Hunter color difference scale. Nippon Suisan Gakkaishi 54:649–653Google Scholar
  7. 7.
    Chow CJ, Ochiai Y, Watabe S (2004) Effect of frozen temperature on autooxidation of bluefin tuna Mb in solution. J Food Biochem 28:123–134CrossRefGoogle Scholar
  8. 8.
    Chow CJ, Ochiai Y, Watabe S, Hashimoto K (1988) Effect of freezing and thawing on the discoloration of tuna meat. Nippon Suisan Gakkaishi 54:639–648Google Scholar
  9. 9.
    Chow CJ, Ochiai Y, Watabe S, Hashimoto K (1987) Autooxidation of bluefin tuna myoglobin associated with freezing and thawing. J Food Sci 52:589–591CrossRefGoogle Scholar
  10. 10.
    Chow CJ, Ochiai Y, Watabe S, Hashimoto K (1988) Autooxidation of bluefin tuna myoglobin at around freezing point. Nippon Suisan Gakkaishi 54:476–478Google Scholar
  11. 11.
    Chow CJ, Ochiai Y, Watabe S, Hashimoto K (1989) Reduced stability and accelerated autooxidation of tuna myoglobin in association with freezing and thawing. J Agric Food Chem 37:1391–1395CrossRefGoogle Scholar
  12. 12.
    Ko WC, Hsu KC (2001) Changes in K value and microorganisms of tilapia fillet during storage at high-pressure, normal temperature. J Food Prot 64:94–98PubMedGoogle Scholar
  13. 13.
    Chen WL, Chow CJ, Ochiai Y (1996) Effects of washing media and storage condition on the color of milkfish meat paste. Fish Sci 62:938–944Google Scholar
  14. 14.
    Robb DHF, Kestin SC, Warriss PD (2000) Muscle activity at slaughter: I. Changes in flesh colour and gaping in rainbow trout. Aquaculture 182:261–269CrossRefGoogle Scholar
  15. 15.
    Chaijan M, Benjakul S, Visessanguan W, Faustman C (2005) Changes of pigments and color in sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) muscle during iced storage. Food Chem 93:607–617CrossRefGoogle Scholar
  16. 16.
    Fosmire GJ, Brown WD (1976) Yellowfin tuna (Thunnus albacares) myoglobin: characterization and comparative stability. Comp Biochem Physiol 55B:293–299Google Scholar
  17. 17.
    Chauvet JP, Acher R (1972) Isolation of coelacanth (Latimeria chalumnae) myoglobin. FEBS Lett 28:16–18CrossRefPubMedGoogle Scholar
  18. 18.
    Chen WL, Chow CJ (2001) Studies on the physicochemical properties of milkfish myoglobin. J Food Biochem 25:157–174CrossRefGoogle Scholar
  19. 19.
    Chow CJ (1991) Relationship between the stability and autooxidation of myoglobin. J Agric Food Chem 39:22–26CrossRefGoogle Scholar
  20. 20.
    Chanthai S, Ogawa M, Tamiya T, Tsuchiya T (1996) Studies on thermal denaturation of fish myoglobins using differential scanning calorimetry, circular dichroism, and tryptophan fluorescence. Fish Sci 62:927–932Google Scholar
  21. 21.
    Chanthai S, Ogawa M, Tamiya T, Tsuchiya T (1996) Studies on thermal denaturation of fish apomyoglobins using differential scanning calorimetry, circular dichroism, and tryptophan fluorescence. Fish Sci 62:933–937Google Scholar
  22. 22.
    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
  23. 23.
    Ueki N, Chow CJ, Ochiai Y (2005) Characterization of bullet tuna myoglobin with reference to thermostability–structure relationship. J Agric Food Chem 53:4968–4975CrossRefPubMedGoogle Scholar
  24. 24.
    Ueki N, Ochiai Y (2005) Structural stabilities of recombinant scombridae fish myoglobins. Biosci Biotechnol Biochem 69:1935–1943CrossRefPubMedGoogle Scholar
  25. 25.
    Ueki N, Ochiai Y (2006) Effect of amino acid replacement on the stability of fish myoglobin. J Biochem 140:649–656CrossRefPubMedGoogle Scholar
  26. 26.
    Kitahara Y, Matsuoka A, Kobayashi N, Shikama K (1990) Autooxidation of myoglobin from bigeye tuna fish (Thunnus obesus). Biochim Biophys Acta 1038:23–28PubMedGoogle Scholar
  27. 27.
    Marcinek DJ, Bonaventura J, Wittenberg JB, Block BA (2001) Oxygen affinity and amino acid sequence of myoglobins from endothermic and ectothermic fish. Am J Physiol Regul Integr Comp Physiol 280:R1123–R1133PubMedGoogle Scholar
  28. 28.
    Suzuki T, Muramatsu R, Kisamori T, Furukohri T (1988) Myoglobin of the shark Galeus nipponensis: identification of the exceptional amino acid replacement at the distal (E7) position and autooxidation of its oxy-form. Zool Sci 5:69–76Google Scholar
  29. 29.
    Madden PW, Babcock MJ, Vayda ME, Cashon RE (2004) Structural and kinetic characterization of myoglobins from eurythermal and stenothermal fish species. Comp Biochem Physiol 137B:341–350Google Scholar
  30. 30.
    Cashon RE, Vayda ME, Sidell BD (1997) Kinetic characterization of myoglobins from vertebrates with vastly different body temperatures. Comp Biochem Physiol 117B:613–620Google Scholar
  31. 31.
    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 Crystallogr D50:283–289Google Scholar
  32. 32.
    Colonna G, Irace G, Bismuto E, Servillo L, Balestrieri C (1983) Structural and functional aspects of the heart ventricle myoglobin of bluefin tuna. Comp Biochem Physiol 76A:481–485CrossRefGoogle Scholar
  33. 33.
    Aojula HS, Wilson MT, Morrison IEG (1987) Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins. Biochem J 243:205–210PubMedGoogle Scholar
  34. 34.
    Bismuto E, Gratton E, Lamb DC (2001) Dynamics of ANS binding to tuna apomyoglobin measured with fluorescence correlation spectroscopy. Biophys J 81:3510–3521CrossRefPubMedGoogle Scholar
  35. 35.
    Chow CJ, Wu JC, Lee PF, Ochiai Y (2009) Structural and autooxidation profiles of myoglobin from three species and one hybrid of tilapia (Cichlidae, Perciformes). Comp Biochem Physiol 154:274–281Google Scholar
  36. 36.
    Schreiter RE, Rodriguez MM, Weichsel A, Monfort RW, Bonaventura J (2007) S-Nitrosylation-induced conformational change in blackfin tuna myoglobin. J Biol Chem 282:19773–19780CrossRefPubMedGoogle Scholar
  37. 37.
    Gutzke D, Trout G (2002) Temperature and pH dependence of the autooxidation rate of bovine, ovine, porcine, and corvine oxymyoglobin isolated from three different muscles—longissimus dorsi, gluteus medius, and biceps femoris. J Agric Food Chem 50:2673–2678CrossRefPubMedGoogle Scholar
  38. 38.
    Murozuka T, Takashi R, Arai K (1974) Relative thermo-stabilities of Ca2+-ATPase of myosin and actomyosin from tilapia and rabbit. Nippon Suisan Gakkaishi 42:57–63Google Scholar
  39. 39.
    Strange ED, Benedict RC, Gugger RE, Metzger VG, Swift CE (1974) Simplified methodology for measuring meat color. J Food Sci 39:988–992CrossRefGoogle Scholar
  40. 40.
    Grigorakis K, Taylor KDA, Alexis MN (2003) Seasonal patterns of spoilage of ice-stored cultured gilthead sea bream (Sparus aurata). Food Chem 81:263–268CrossRefGoogle Scholar
  41. 41.
    Abril M, Campo MM, Önenç A, Sañudo C, Albertí P, Negueruela AI (2001) Beef colour evolution as a function of ultimate pH. Meat Sci 58:69–78CrossRefGoogle Scholar
  42. 42.
    Dyuysekina AE, Dolgikh DA, Samatova Baryshnikova EN, Tiktopulo EI, Balobanov VA, Bychkova VE (2008) pH-induced equilibrium unfolding of apomyoglobin: substitutions at conserved Trp14 and Met131 and non-conserved Val17 positions. Biochemistry (Mosc) 73:693–701CrossRefGoogle Scholar
  43. 43.
    Cornforth DP, Egbert WR (1985) Effect of rotenone and pH on the color of pre-rigor muscle. J Food Sci 50:34–35CrossRefGoogle Scholar
  44. 44.
    Mendenhall VT (1989) Effect of pH and total pigment concentration on the internal color of cooked ground beef patties. J Food Sci 54:1–2CrossRefGoogle Scholar
  45. 45.
    Trout GR (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 54:536–540CrossRefGoogle Scholar
  46. 46.
    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–C772Google Scholar
  47. 47.
    Chajian M, Benjakul S, Visessanguan W, Lee S, Faustman C (2008) Interaction of fish myoglobin and myofibrillar proteins. J Food Sci 73:292–298CrossRefGoogle Scholar
  48. 48.
    Kauffman RG, van Laack RLJM, Russell RL, Pospiech E, Cornelius CA, Suckow CE, Greaser ML (1998) Can pale, soft, exudative pork be prevented by postmortem sodium bicarbonate injection? J Anim Sci 76:3010–3015PubMedGoogle Scholar

Copyright information

© The Japanese Society of Fisheries Science 2009

Authors and Affiliations

  • Chau-Jen Chow
    • 1
  • Jing-Iong Yang
    • 1
  • Pei-Fen Lee
    • 1
  • Yoshihiro Ochiai
    • 2
  1. 1.Department of Seafood ScienceNational Kaohsiung Marine UniversityKaohsiungTaiwan, ROC
  2. 2.Laboratory of Aquatic Molecular Biology and Biotechnology, Graduate School of Agricultural and Life SciencesThe University of TokyoBunkyoJapan

Personalised recommendations