The Composition, Structure, and Functionalities of Prolamins from Highland Barley

The composition, structure, and functionalities of prolamins from highland barley were investigated. These parameters were compared with those of the commonly applied prolamins (zein). There are more charged and hydrophilic amino acids in highland barely prolamins than zein. The molecular weight of highland barely prolamins was between 30 and 63 kDa, which was larger than that of zein (20 and 24 kDa). The main secondary structure of highland barely prolamins was & beta;-turn helices, while & alpha;-helical structures were the main secondary structure in zein. The water holding capacity, thermal stability, emulsifying capacity, and stability of prolamins from highland barley were significantly higher than in zein, while the opposite results were observed for oil absorption capacity between the two. The diameter of fibers prepared using highland barely prolamins was almost six times that of zein, while highland barely prolamins formed ribbon structures instead of fibers. Therefore, the results provide guidance for applications of prolamins from highland barley.

Automated summary

The composition, structure, and functionalities of prolamins from highland barley, compared to those of zein, were investigated. The highland barley prolamins contained more charged and hydrophilic amino acids. The molecular weight of highland barley prolamins was larger, and their main secondary structure was β-turn helices, while zein had α-helical structures. The prolamins from highland barley had higher water holding capacity, thermal stability, emulsifying capacity, and stability, but lower oil absorption capacity compared to zein. The fibers prepared using highland barley prolamins were larger and had ribbon structures. These findings provide guidance for the applications of highland barley prolamins.