A set
of high-molecular-weight glutenin subunit (HMW-GS)
deletion
lines were used to investigate the influences of HMW-GS on wheat gluten,
and dough properties were investigated using a set of HMW-GS deletion
lines. Results showed that HMW-GS deletion significantly decreased
the dough stability time, as well as viscoelastic moduli (G′ and G″), compared with
the wild type, where the deletion of x-type HMW-GSs (Ax1d, Bx7d, and
Dy12d) decreased more than y-type HMW-GSs (By8d and Dy12d). The deletion
of HMW-GS significantly decreased HMW-GS contents and increased α-/γ-gliadin
contents. A proteomic study showed that the HMW-GS deletion down-regulated
the HMW-GS, β-amylase, serpins, and protein disulfide isomerase
and up-regulated the LMW-GS, α/γ-gliadin, and α-amylase
inhibitor. Meanwhile, HMW-GS deletion significantly decreased contents
of β-turn and β-sheet. In addition, less energetically
stable disulfide conformations (trans–gauche–gauche
and trans–gauche–trans) were abundant in HMW-GS deletion
lines. Furthermore, analysis of five HMW-GSs based on amino acid sequences
proved that Dx2 and Bx7 had a more stable structure, followed by Ax1,
then Dy12, and finally By8.