文献类型： 外文期刊
作者： Xia, Minquan 1 ; Chen, Yinxia 2 ; Ma, Jing 1 ; Yin, Xiaoli 1 ; Wang, Lan 3 ; Wu, Wenjin 3 ; Xiong, Guangquan 3 ; Sun, Wei 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： Myoglobin oxidation; Polyacrylamide gel electrophoresis (PAGE); Intrinsic fluorescence; Circular dichroism (CD) spectroscopy
期刊名称：FOOD CHEMISTRY （ 2020影响因子：7.514； 五年影响因子：7.516 ）
ISSN： 0308-8146
年卷期： 2020 年 309 卷
收录情况： SCI
摘要： The effects of low frequency magnetic field on myoglobin (Mb) oxidation stability were evaluated by treatments at 0, 3, 6, 9, 12 mT and storage for 10 h. The results showed that Mb oxidation was inhibited under all magnetic field treatments, due to the increase of total sulfhydryl and free amino groups (9 or 12 mT) from unfolding of Mb clusters (3, 9, 12 mT) as well as beta-turn and beta-sheet structures (9 or 12 mT). The unfolding also induced (i) the destruction or burial of iron porphyrin and tyrosine residues; (ii) the exposure of tryptophan; (iii) more uniform Mb particle size distribution (3, 9, 12 mT) and increased zeta potential (3, 6, 12 mT). Overall, magnetic field promoted exposed active groups as the preferred oxidation target, thus decreasing the oxidation rate of central iron atoms. It also promoted Mb stability by redistributing particle size and increasing zeta potential.
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