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Gel properties of grass carp myofibrillar protein modified by low-frequency magnetic field during two-stage water bath heating

文献类型： 外文期刊

作者： Wang, Limei 1 ; Xia, Minquan 1 ; Zhou, Yuanhua 2 ; Wang, Xian 1 ; Ma, Jing 1 ; Xiong, Guangquan 3 ; Wang, Lan 3 ; Wang, S 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

4.Northwest A&F Univ, Coll Mech & Elect Engn, Yangling 712100, Shaanxi, Peoples R China

关键词： Myofibrillar protein; Low-frequency magnetic field; Two-stage water bath heating; Raman spectroscopy; Low-field nuclear magnetic resonance

期刊名称：FOOD HYDROCOLLOIDS （ 影响因子：9.147； 五年影响因子：9.169 ）

ISSN： 0268-005X

年卷期： 2020 年 107 卷

页码：

收录情况： SCI

摘要： The effects of low-frequency magnetic field (LF-MF) on the gel properties of grass carp myofibrillar proteins (GCMPs) and the underlying mechanisms were investigated to explore a better processing method for surimi gel products. GCMPs were untreated or treated with LF-MF of 9.5 mT in the first stage (40 degrees C heating for 50 min) or the second stage (85 degrees C heating for 40 min) of two-stage water bath heating. Results indicated that in the first stage, LF-MF induction may be detrimental to GCMPs unfolding and possibly resulted in a poor and unstable the GCMPs gels network structure, which had a negative effect on gel strength. Hence, water easily leaked from the GCMPs gel, leading to a decrease in WHC. Inversely, the unfolding of a-helix and the formation of random coil of LF-MF treatment in the second stage resulted in more exposure of internal groups, leading to the reduction of ionic bonds and increase of hydrogen bonds. These changed bonds further affected the T-21 relaxation time, increased in PT2b and decreased in PT22, and mainly impacted the bind between water and protein, thus resulting in the improved gel strength and WHC.

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