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Irreversible unfolding of myoglobin in an aqueous solution by supercritical carbon dioxide
H Ishikawa1, M Shimoda, A Yonekura
1Laboratory of Food Biotechnology, Department of Bioscience and Biotechnology, Division of Bioresource and Bioenviromental Science, Graduate School of Kyushu University, Fukuoka 812-8581, Japan. ishikawa@agr.kyushu-u.ac.jp
Abstract:
The conformational changes in myoglobin, treated by microbubbling of supercritical carbon dioxide (SC-CO(2)), were investigated by measuring the circular dichroism spectra in the ultraviolet range and compared with those in other proteins (ovoalbumin, bovine serum albumin, and beta-lactoglobulin). Irreversible unfoldings were observed after the microbubbling of SC-CO(2) at 35 degrees C and 30 MPa for 30 min. The degree of unfolding depended on the number of intramolecular S-S bonds. alpha-Helix contents of myoglobin decreased with increasing density of SC-CO(2). 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 CO(2) under atmospheric pressure, but heating was required.
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