Irreversible unfolding of myoglobin in an aqueous solution by supercritical carbon dioxide

H. Ishikawa, M. Shimoda, A. Yonekura, K. Mishima, K. Matsumoto, Y. Osajima

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23 Citations (Scopus)


The conformational changes in myoglobin, treated by microbubbling of supercritical carbon dioxide (SC-CO2), were investigated by measuring the circular dichroism spectra in the ultraviolet range and compared with those in other proteins (ovoalbumin, bovine serum albumin, and β-lactoglobulin). Irreversible unfoldings were observed after the microbubbling of SC-CO2 at 35 °C and 30 MPa for 30 min. The degree of unfolding depended on the number of intramolecular S-S bonds. α-Helix contents of myoglobin decreased with increasing density of SC-CO2. Unfoldings of myoglobin induced by heating, pH-lowering, and the addition of a denaturant were reversible. The irreversible unfolding of myoglobin was also observed by the bubbling of gaseous CO2 under atmospheric pressure, but heating was required.

Original languageEnglish
Pages (from-to)4535-4539
Number of pages5
JournalJournal of Agricultural and Food Chemistry
Issue number10
Publication statusPublished - 2000

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)


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