Thermal denaturation profiles of Tuna Myoglobin

Yoshihiro Ochiai, Yoshiaki Watanabe, Hideo Ozawa, Shigeru Ikegami, Naoyuki Uchida, Shugo Watabe

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)


Myoglobin (Mb) purified from fast skeletal muscle of bluefin tuna Thunnus thynnus orientalis was subjected to thermal treatment, and the denaturation profiles were examined by thermodynamic analysis. Based on the ellipticity or helical content obtained by circular dichroism (CD) spectrometry, it was found that denaturation of tuna Mb consisted of three steps, and that slight structural changes of Mb started below 20 °C. However, major structural changes were observed at around 58 and 72 °C. Differential scanning calorimetry (DSC) analysis revealed a similar but somewhat different thermal denaturation profile of Mb. In comparison with the denaturing profiles of whale Mb under the same conditions, the thermal stability of tuna Mb was found to be much lower. In the modeled tertiary structures of these Mbs, they were roughly similar to each other, though minor conformational differences were recognized and the total energy was found to be lower for tuna Mb.

Original languageEnglish
Pages (from-to)1673-1679
Number of pages7
JournalBioscience, Biotechnology and Biochemistry
Issue number8
Publication statusPublished - 2010
Externally publishedYes


  • Denaturation
  • Myoglobin
  • Stability
  • Temperature
  • Tuna

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry


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