Low frequency magnetic fields modification on hydrogen peroxide oxidized myoglobin-isolate and mechanisms underlying the chain reaction process

•Increased magnetic field promoted H2O2 oxidation of myoglobin (Mb).•Magnetic fields of ≥ 9 mT changed the redox equivalents of Mb.•≥ 9 mT magnetic field shifted oxidation site from porphyrin ring to Mb skeleton.•Mb aggregation was affected by magnetic field-induced iron ion movement. The effects of...

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Veröffentlicht in:	Food chemistry 2020-05, Vol.312, p.126069-126069, Article 126069
Hauptverfasser:	Xia, Minquan, Chen, Yinxia, Ma, Jing, Yin, Xiaoli, Li, Zhenshun, Xiong, Guangquan, Wang, Lan, Wu, Wenjin, Sun, Weiqing, Zhou, Yuanhua
Format:	Artikel
Sprache:	eng
Schlagworte:	Circular dichroism (CD) spectroscopy Ferric Compounds - chemistry Hydrogen Peroxide - chemistry Hydrogen peroxide oxidation Hydroxyl Radical - chemistry Iron - chemistry Low frequency magnetic field Magnetic Fields Myoglobin - chemistry Myoglobin-isolate Oxidation-Reduction Porphyrins - chemistry
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