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Study on Protein Structures of Eight Mung Bean Varieties and Freeze-Thaw Stability of Protein-Stabilized Emulsions

文献类型： 外文期刊

作者： Sun, Hongrui 1 ; Fan, Jieying 1 ; Sun, Hongjiao 2 ; Jiang, Guochuan 3 ; Meng, Yue 1 ; Zeng, Xianpeng 1 ; Yang, Zhiqiang 1 ; Nan, Xiping 1 ; Kang, Lining 1 ; Liu, Xiangying 1 ;

作者机构： 1.Jilin Acad Agr Sci, Inst Agrofood Technol, Changchun 130033, Peoples R China

2.Jilin Jinong Hitech Inc Ltd, Gongzhuling 136100, Peoples R China

3.Jilin Agr Univ, Coll Food Sci & Engn, Changchun 130118, Peoples R China

关键词： mung bean protein isolate; freeze-thaw stability; protein structure; albumin and globulin content; emulsion parameters; flexibility measurement; functional properties; fourier-transform infrared spectroscopy; circular dichroism

期刊名称：FOODS （ 影响因子：5.561； 五年影响因子：5.94 ）

ISSN：

年卷期： 2022 年 11 卷 21 期

页码：

收录情况： SCI

摘要： In order to evaluate the freeze-thaw stability of mung bean protein isolate (MPI)-stabilized emulsions and its relationship with protein structure, proteins of eight mung bean varieties were compared. The results revealed that MPIs prepared from all eight varieties were mainly composed of five subunit bands, with albumin and globulin content ranges of 188.4-310.3 and 301.1-492.7 mg/g total protein, respectively. Protein structural analysis revealed that random coil structure (32.34-33.51%) accounted for greater than 30% of MPI secondary structure. Meanwhile, analysis of protein properties revealed emulsifying activity index (EAI), emulsifying stability index (ESI) and flexibility value ranges of 6.735-8.598 m(2)/g, 20.13-34.25% and 0.125-0.182, respectively. Measurements of freezethaw stability of MPI emulsions demonstrated that exposures of emulsions to multiple freeze-thaw cycles resulted in significantly different emulsion creaming index, oiling-off, particle size and zeta potential values for the various emulsions. Moreover, the stabilities of all eight protein emulsions decreased with each freeze-thaw cycle, as demonstrated using optical micrographs. The correlation analysis method was used to study the correlation between the original structures, emulsifying properties of proteins and the freeze-thaw stability of MPI emulsions. Correlation analysis results revealed significant relationships between albumin content, subunit bands with a molecular weight of 26.9 kDa and emulsifying properties were significantly related to the freeze-thaw stability of MPI emulsion. Thus, by determining these indicator values, we can predict the freeze-thaw stability of MPI-stabilized emulsions.

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