Fisheries Science

, Volume 84, Issue 3, pp 579–587 | Cite as

pH- and temperature-dependent denaturation profiles of tuna myoglobin

  • Mala NurilmalaEmail author
  • Hideki Ushio
  • Yoshihiro Ochiai
Original Article Chemistry and Biochemistry


Attempts have been made to elucidate the denaturation profiles of tuna myoglobin (Mb) in comparison with horse Mb. Intensive absorbance characterization was carried out for derivatives (deoxy, oxy, met forms) of Mb. The wavelength of the maximum absorbance of tuna Mb was shorter only by 1 nm for deoxy and metMb, while it was 4 nm shorter for the second peak of metMb. Percentage Mb denaturation (PMD) was measured under a combination of pH (5.6, 6.5, 7.4) and temperature (70, 75, 80 °C). Tuna Mb was almost completely denatured even during the initial incubation at 75 and 80 °C at all pHs examined. During the incubation at 70 °C, the PMD values for tuna Mb were 88.5, 52.1, and 67.7% at pH 5.6, 6.5, and 7.4, respectively. The denaturation of tuna Mb proceeded even at 55 °C, but denaturation rates were very slow at pH 6.5. On the other hand, horse Mb was found to be very stable at pH 6.5 and 7.4 at all temperatures examined, except at pH 6.5 and 80 °C. At pH 5.6, the PMD values of horse Mb gradually increased, especially at 75 and 80 °C. These different Mbs showed quite different denaturation profiles.


Pacific bluefin tuna Protein structure Stability Denaturation Sodium dodecylsulfate-polyacrylamide gel electrophoresis 



The authors would like to thank Professor S. Watabe, Kitasato University and Professor S. Asakawa, the University of Tokyo, for their encouragement throughout the study.


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Copyright information

© Japanese Society of Fisheries Science 2018

Authors and Affiliations

  1. 1.Department of Aquatic Product Technology, Faculty of Fisheries and Marine SciencesBogor Agricultural UniversityBogorIndonesia
  2. 2.Department of Aquatic BioscienceThe University of TokyoTokyoJapan
  3. 3.Graduate School of Agricultural ScienceTohoku UniversitySendaiJapan

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