The effect of Fenton’s reactants and aldehydes on the changes of myoglobin from Eastern little tuna (Euthynnus affinis) dark muscle
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The influences of Fenton’s reactants (H2O2 and FeCl2) and aldehydes (hexanal and hexenal) on changes of oxymyoglobin and metmyoglobin from Eastern little tuna (Euthynnus affinis) dark muscle were studied. In the presence of H2O2, both oxymyoglobin and metmyoglobin were rapidly oxidized into ferrylmyoglobin based on spectra patterns. In the presence of Fe2+ and/or H2O2, the changes in fluorescent intensity of myoglobin were noticeable, but there were no changes in aggregation ratio. Release of non-heme iron from myoglobin was mainly governed by H2O2. When aldehydes were incorporated, the oxidation of oxymyoglobin and conformational changes of globin were more pronounced. No release of non-heme iron was noticeable, suggesting the stability of heme moiety toward aldehydes. Hexenal had a great impact on cross-linking of oxymyoglobin and metmyoglobin via covalent modification. Alteration of myoglobin redox state might be enhanced by conformational changes of globin induced by both Fenton’s reactants and aldehydes.
KeywordsMyoglobin Ferrylmyoglobin H2O2 Cross-linking Hexanal Hexenal
This research was supported by the Thailand Research Fund under the Royal Golden Jubilee PhD Program to Yaowapa Thiansilakul (PHD/0101/2550) and TRF senior research scholar.
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