Low frequency magnetic fields modification on hydrogen peroxide oxidized myoglobin-isolate and mechanisms underlying the chain reaction process
文献类型： 外文期刊
作者： Xia, Minquan 1 ; Chen, Yinxia 2 ; Ma, Jing 1 ; Yin, Xiaoli 1 ; Li, Zhenshun 1 ; Xiong, Guangquan 3 ; Wang, Lan 3 ; Wu, We 1 ;
作者机构： 1.Yangtze Univ, Coll Life Sci, Jingzhou 434023, Hubei, Peoples R China
2.Huazhong Agr Univ, Coll Food Sci & Technol, Wuhan 430070, Hubei, Peoples R China
3.Hubei Acad Agr Sci, Inst Farm Prod Proc & Nucl Agr Technol, Wuhan 430064, Hubei, Peoples R China
4.Yangtze Univ, Sch Mech Engn, Jingzhou 434023, Hubei, Peoples R China
关键词： Low frequency magnetic field; Myoglobin-isolate; Hydrogen peroxide oxidation; Circular dichroism (CD) spectroscopy
期刊名称：FOOD CHEMISTRY （ 影响因子：7.514； 五年影响因子：7.516 ）
ISSN： 0308-8146
年卷期： 2020 年 312 卷
页码：
收录情况： SCI
摘要： The effects of low frequency magnetic field (0-12 mT) on hydrogen peroxide oxidized myoglobin-isolate (MbI) were investigated. The results indicate that the primary target of the hydrogen peroxide oxidation was Met(Fe-III) Mb, leading to the fall off of iron ions from the porphyrin ring. Additionally, the increased magnetic field (>= 9 mT) enhanced the release of more iron ions to react with H2O2, giving rise to the production of more hydroxyl radicals and the shift of oxidation site from porphyrin ring to Mb skeleton. Moreover, the directional movement of iron ions induced by magnetic field caused the generation of local micro-electric field and the rearrangement of charged groups on the protein surface or near-surface, thus affecting Mb aggregation. Overall, the magnetic field interfered with the hydrogen peroxide chain reaction process, changed the redox equivalents of Mb, and shifted the oxidation sites of Mb.
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