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

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

doi:10.1021/jf000081i

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

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

Food Science and Biotechnology

Research output: Contribution to journal › Article › peer-review

23 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	4535-4539
Number of pages	5
Journal	Journal of Agricultural and Food Chemistry
Volume	48
Issue number	10
DOIs	https://doi.org/10.1021/jf000081i
Publication status	Published - 2000

All Science Journal Classification (ASJC) codes

Chemistry(all)
Agricultural and Biological Sciences(all)

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10.1021/jf000081i

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abstract = "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.",

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T1 - Irreversible unfolding of myoglobin in an aqueous solution by supercritical carbon dioxide

AU - Ishikawa, H.

AU - Shimoda, M.

AU - Yonekura, A.

AU - Mishima, K.

AU - Matsumoto, K.

AU - Osajima, Y.

PY - 2000

Y1 - 2000

N2 - 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.

AB - 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.

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

Abstract

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