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Characterization of protein isolates from green wheat: structure, thermal and rheological properties

文献类型： 外文期刊

作者： Wen, Qingyu 1 ; Zhang, Kangyi 1 ; Zhang, Yu 4 ; Liu, Benguo 6 ; Xu, Guozhen 7 ; Sun, Dongxian 4 ; Li, Tianqi 4 ; Zhao, Di 1 ;

作者机构： 1.Henan Acad Agr Sci, Ctr Agr Prod Proc, Zhengzhou 450002, Peoples R China

2.Henan Int Joint Lab Whole Grain Wheat Prod Proc, Zhengzhou 450002, Peoples R China

3.Henan Whole Grain Fresh Food Proc Engn Technol Res, Zhengzhou 450002, Peoples R China

4.Henan Ankang Food Sci & Technol Res Inst, Zhengzhou 450001, Peoples R China

5.Henan Ankang Future Food Technol Co Ltd, Zhengzhou 450040, Peoples R China

6.Henan Inst Sci & Technol, Xinxiang 453003, Peoples R China

7.Puyang Acad Agr Sci, Puyang 457001, Peoples R China

关键词： Green wheat; Protein isolates; Functional properties

期刊名称：JOURNAL OF FOOD MEASUREMENT AND CHARACTERIZATION （ 影响因子：3.4； 五年影响因子：3.2 ）

ISSN： 2193-4126

年卷期： 2023 年 17 卷 3 期

页码：

收录情况： SCI

摘要： Green wheat protein is rich in nutritional value and is a high-quality vegetable protein. In this paper, the composition, structure and functional properties of green wheat protein were investigated. Albumin (60.1%), globulin (3.7%), gliadin (2.9%) and glutenin (33.3%) were isolated from green wheat. The content of essential amino acids in all four proteins was hig her than the Food and Agriculture Organization of the United Nations (FAO) recommended value for adults. The results of circular dichroism spectroscopy indicated that beta-sheet was the main ordered structure in green wheat protein isolates, gliadin had the highest content of ordered structure. In addition, albumin and gliadin had relatively compact structures and high thermal stability. The glutenin and globulin had poor thermal stability due to their loose and porous structure, but the cross-linking and aggregation between glutenins were beneficial to improve thermal stability. The rheological results showed that the four protein isolate solutions exhibited typical shear thinning behavior in the shear rate range, the apparent viscosity was lower at high shear rate and low temperature (< 40 degrees C), while shear rate and temperature had relatively weak effects on the fluidity of gliadin solution. This study provided a theoretical basis for the development of green wheat protein as a new type of plant-derived protein.

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