Influence of high-molecular-weight glutenin subunit composition at Glu-A1 and Glu-D1 loci on secondary and micro structures of gluten in wheat (Triticum aestivum L.)

Food Chem. 2016 Dec 15:213:728-734. doi: 10.1016/j.foodchem.2016.07.043. Epub 2016 Jul 6.

Abstract

As one of critical gluten proteins, high-molecular-weight glutenin subunits (HMW-GS) mainly affect the rheological behaviour of wheat dough. The influence of HMW-GS variations at the Glu-A1 and Glu-D1 loci on both secondary and micro structures of gluten and rheological properties of wheat dough was investigated in this study. Results showed that the Amide I bands of the three near-isogenic lines (NILs) shifted slightly, but the secondary structures differed significantly. The micro structure of gluten in NIL 4 (Ax null) showed bigger apertures and less connection, compared to that in Xinong 1330 (Ax1). The micro structure of gluten in NIL 5 (Dx5+Dy10) showed more compact than that in Xinong 1330 (Dx2+Dy12). Correlation analysis demonstrated that the content of β-sheets and disulfide bonds in gluten has a significant relationship with dough properties. The secondary structures of native gluten are suggested to be used as predictors of wheat quality.

Keywords: Dough rheological behaviour; Glu-A1 and Glu-D1; Micro structure; Secondary structure of gluten; Wheat glutenin subunits.

MeSH terms

  • Genetic Loci
  • Gliadin / chemistry
  • Gliadin / genetics
  • Glutens / chemistry
  • Glutens / genetics*
  • Molecular Weight
  • Protein Conformation, beta-Strand
  • Protein Structure, Secondary
  • Spectroscopy, Near-Infrared
  • Triticum / chemistry
  • Triticum / genetics*

Substances

  • Glutens
  • Gliadin
  • glutenin