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Gel properties of myofibrillar proteins heated at different heating rates under a low-frequency magnetic field

文献类型： 外文期刊

作者： Wang, Xian 1 ; Xia, Minquan 1 ; Zhou, Yuanhua 2 ; Wang, Limei 1 ; Feng, Xiaolong 1 ; Yang, Kun 1 ; Ma, Jing 1 ; Li, Zhens 1 ;

作者机构： 1.Yangtze Univ, Coll Life Sci, Jingzhou 434023, Hubei, Peoples R China

2.Yangtze Univ, Sch Mech Engn, Jingzhou 434023, Hubei, Peoples R China

3.Hubei Acad Agr Sci, Inst Farm Prod Proc & Nucl Agr Technol, Wuhan 430064, Hubei, Peoples R China

关键词： Myofibrillar protein gel; Low-frequency magnetic field; Heating rate; Raman spectroscopy; Low-field nuclear magnetic resonance

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 321 卷

页码：

收录情况： SCI

摘要： The effects of low-frequency magnetic field combined with different heating rates on pork myofibrillar protein (MP) gels were investigated. Samples were treated under different heating rates (1 degrees C/min and 2 degrees C/min) in the presence or absence of 9.5 mT low-frequency magnetic field. The highest levels of intermolecular and intramolecular ionic and hydrogen bonds in MP were observed at the heating rate of 2 degrees C/min under the 9.5 mT magnetic field. These bonds resulted in decreasing the alpha-helix and increasing the beta-sheet and beta-turn, which promoted the formation of a more uniform microstructure. It also increased the proportion of bound water, increasing the ability of MP to bind with water. This effect, combined with the weaker hydrophobic interactions, as confirmed by the reduced content of tryptophan and aliphatic residues, explained well the high water-holding capacity of MP induced by heating at 2 degrees C/min under the 9.5 mT magnetic field.

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