Modification of the Low Molecular Weight (LMW) Glutenin Composition of Transgenic Durum Wheat: Effects on Glutenin Polymer Size and Gluten Functionality

  title={Modification of the Low Molecular Weight (LMW) Glutenin Composition of Transgenic Durum Wheat: Effects on Glutenin Polymer Size and Gluten Functionality},
  author={Paola Tosi and Stefania Masci and Angela Giovangrossi and Renato D'Ovidio and Frank B{\'e}k{\'e}s and Oscar Larroque and Johnathan A. Napier and Peter R. Shewry},
  journal={Molecular Breeding},
The low-molecular weight (LMW) glutenin subunits are major determinants of the viscoelasticity of durum wheat gluten, and therefore of its technological quality, with both quantitative effects and qualitative effects. We have modified the LMW glutenin subunit composition of the durum wheat cultivar Ofanto by expression of a transgene encoding a B-type LMW glutenin subunit and have carried out detailed analyses of two independent transformed lines in order to assess the effect of the transgene… 

Coexpression of the High Molecular Weight Glutenin Subunit 1Ax1 and Puroindoline Improves Dough Mixing Properties in Durum Wheat (Triticum turgidum L. ssp. durum)

The results in this study suggest that simultaneous modulation of dough strength and grain hardness in durum wheat could significantly improve its breadmaking quality and may not even impair its pastamaking potential.

Overexpression of Avenin-Like b Proteins in Bread Wheat (Triticum aestivum L.) Improves Dough Mixing Properties by Their Incorporation into Glutenin Polymers

The hypothesis that Avenin-like b proteins could be integrated into glutenin polymers by inter-chain disulphide bonds, which could help understand the mechanism behind strengthening wheat dough strength, was confirmed.

Transformation of common wheat (Triticum aestivum L.) with avenin-like b gene improves flour mixing properties

Avenin-like b proteins may contribute to the viscoelastic properties of wheat dough via inter- chain disulphide bonds, due to their rich cysteine residues. In order to clarify the effect of the

Trafficking of storage proteins in developing grain of wheat

These studies are in agreement with previous suggestions that two trafficking pathways occur in wheat, with the proteins either being transported via the Golgi apparatus into the vacuole or accumulating directly within the lumen of the ER, and suggest that the same individual protein could be trafficked by either pathway.

Transformation of common wheat (Triticum aestivum L.) with avenin-like b gene improves flour mixing properties

The results of SE-HPLC analysis of the gluten proteins in wheat flour demonstrated that the improvement in transgenic line flour properties was associated with the increased proportion of large polymeric proteins due to the incorporation of overexpressed avenin-like b proteins into the glutenin polymers.

Co-expression of high-molecular-weight glutenin subunit 1Ax1 and Puroindoline a (Pina) genes in transgenic durum wheat (Triticum turgidum ssp. durum) improves milling and pasting quality

It is demonstrated that co-expression of Pina + 1Ax1 in durum wheat did not affect the milling performance that was enhanced by Pina expression, and Pina and 1Ax1 co- expression suggests that PINA impacts gluten aggregation via interaction with gluten protein matrix.

Effects of additional cysteine residue of Avenin-like b protein by site-directed mutagenesis on dough properties in wheat (Triticum aestivum L.).

Avenin-like b proteins were detected in glutenin macropolymers, providng further evidence for this protein to participate in the polymerization of glutenin.



Expression of epitope-tagged LMW glutenin subunits in the starchy endosperm of transgenic wheat and their incorporation into glutenin polymers

The results demonstrate that the ability to specifically epitope-tag LMW glutenin transgenes can greatly assist in the elucidation of their individual contributions to the functionality of the complex gluten system.

Prolamin aggregation, gluten viscoelasticity, and mixing properties of transgenic wheat lines expressing 1Ax and 1Dx high molecular weight glutenin subunit transgenes.

The effect of transgenes coding for subunits 1Ax1 and 1Dx5 was studied in two near-isogenic wheat lines differing in their HMW subunit compositions and mixing properties, resulting in increased cross-linking of glutenin polymers and abnormal mixing properties of dough.

Influence of High Mr Glutenin Subunits on Glutenin Polymers and Rheological Properties of Glutens and Gluten Subfractions of Near-isogenic Lines of Wheat Sicco

Abstract The gluten proteins of three near-isogenic lines of the wheat Sicco, which differed only in high Mr glutenin subunit composition, were studied. Gluten was extracted and fractionated by a

Characterization of a low-molecular-weight glutenin subunit gene from bread wheat and the corresponding protein that represents a major subunit of the glutenin polymer.

A computer-generated molecular model of the 42K LMW-GS, a major component of the glutenin polymer, was constructed on the basis of the deduced amino acid sequence and literature-based assignment of disulfide linkages and indicates correspondence between this protein and the putative corresponding gene.

Depolymerization of the Glutenin Macropolymer During Dough Mixing: I. Changes in Levels, Molecular Weight Distribution, and Overall Composition

ABSTRACT Changes in the amounts, molecular weight distributions, and levels of major groups of subunits in the glutenin macropolymer (GMP) of doughs during mixing were investigated. The GMP (gel

Characterization and quantification of low molecular weight glutenins in durum wheats.

Characterization of low molecular weight glutenin subunits in durum wheat by reversed-phase high-performance liquid chromatography and N-terminal sequencing

Low molecular weight glutenin subunits (LMW-GS) from a residue preparation were fractionated by reversed-phase high-performance liquid chromatography (RP-HPLC) of reduced subunits from two biotypes


  • 2007
Cereal Chemistry 53(2): 258-269 Properties of glutenin and other wheat proteins that may be responsible for varietal differences in wheat flour performance were investigated. The proteins from