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

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.

Automated summary

In this study, the composition, structure, and functional properties of green wheat protein were investigated. The protein was found to be rich in essential amino acids and exhibited high thermal stability, making it a potential new source of plant-derived protein.