Abstract

BackgroundThe end-use quality of wheat flour varies as a result of the growth conditions of the plant. Among the wheat gluten proteins, the omega-5 gliadins have been identified as a major source of environmental variability, increasing in proportion in grain from plants that receive fertilizer or are subjected to high temperatures during grain development. The omega-5 gliadins also have been associated with the food allergy wheat-dependent exercise-induced anaphylaxis (WDEIA). Recently, transgenic lines with reduced levels of omega-5 gliadins were developed using RNA interference (RNAi). These lines make it possible to determine whether changes in the levels of omega-5 gliadins in response to environmental conditions and agronomic inputs may be responsible for changes in flour end-use quality.ResultsTwo transgenic wheat lines and a non-transgenic control were grown under a controlled temperature regimen with or without post-anthesis fertilizer and the protein composition of the resulting flour was analyzed by quantitative two-dimensional gel electrophoresis (2-DE). In one transgenic line, all 2-DE spots identified as omega-5 gliadins were substantially reduced without effects on other proteins. In the other transgenic line, the omega-5 gliadins were absent and there was a partial reduction in the levels of the omega-1,2 gliadins and the omega-1,2 chain-terminating gliadins as well as small changes in several other proteins. With the exception of the omega gliadins, the non-transgenic control and the transgenic plants showed similar responses to the fertilizer treatment. Protein contents of flour were determined by the fertilizer regimen and were similar in control and transgenic samples produced under each regimen while both mixing time and mixing tolerance were improved in flour from transgenic lines when plants received post-anthesis fertilizer.ConclusionsThe data indicate that omega-5 gliadins have a negative effect on flour quality and suggest that changes in quality with the growth environment may be due in part to alterations in the levels of the omega gliadins. Because a known food allergen and one of the major sources of environmentally-induced variation in wheat flour protein composition has been eliminated, the transgenic lines may yield flour with both improved end-use quality and more consistent functionality when grown in different locations.Electronic supplementary materialThe online version of this article (doi:10.1186/s12870-014-0393-1) contains supplementary material, which is available to authorized users.

Highlights

  • The end-use quality of wheat flour varies as a result of the growth conditions of the plant

  • As shown in Additional file 1, samples from both the control and transgenic lines produced with post-anthesis fertilizer had uniform kernels with a vitreous appearance while those produced without post-anthesis fertilizer contained high percentages of yellow berries

  • When plants were supplied with post-anthesis fertilizer, there were increases in only alpha gliadin Bu-14, serpins Bu-3 and Bu-5, and triticin

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Summary

Introduction

The end-use quality of wheat flour varies as a result of the growth conditions of the plant. Transgenic lines with reduced levels of omega-5 gliadins were developed using RNA interference (RNAi) These lines make it possible to determine whether changes in the levels of omega-5 gliadins in response to environmental conditions and agronomic inputs may be responsible for changes in flour end-use quality. The main determinants of flour end-use quality, the gluten proteins, consist of gliadins and glutenins that together comprise about 70-80% of the flour protein Both types of proteins contain repetitive sequences and an abundance of glutamine and proline and are largely insoluble in aqueous solutions [1,2]. The gliadins are present as monomers in the flour and contribute extensibility to wheat flour dough These proteins are separated into alpha, gamma and omega gliadin subgroups, each with distinct primary sequences. They may be referred to as chain-terminating gliadins on the basis of their primary sequences

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