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Temperature-dependent Structural Perturbation of Tuna Myoglobin
Authors: Yoshihiro Ochiai
Abstract:To unveil the mechanism of fast autooxidation of fish myoglobins, the effect of temperature on the structural change of tuna myoglobin was investigated. Purified myoglobin was subjected to preincubation at 5, 20, 50 and 40oC. Overall helical structural decay through thermal treatment up to 95oC was monitored by circular dichroism spectrometry, while the structural changes around the heme pocket was measured by ultraviolet/visible absorption spectrophotometry. As a result, no essential structural change of myoglobin was observed under 30oC, roughly equivalent to their body temperature, but the structure was clearly damaged at 40oC. The Soret band absorption hardly differed irrespective of preincubation temperature, suggesting that the structure around the heme pocket was not perturbed even after thermal treatment.
Digital Object Identifier (DOI): doi.org/10.5281/zenodo.1331401Procedia APA BibTeX Chicago EndNote Harvard JSON MLA RIS XML ISO 690 PDF Downloads 1669
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