Anne Kjersti Uhlen

Proteome changes in wheat subjected to different nitrogen and sulfur fertilizations.

Controlling the quality of wheat for breadmaking is a major concern for the milling and baking industry. Wheat flour quality depends on both the genetic background and environmental factors during growth and storage. Amount and timing of application of fertilizer are factors that affect wheat quality. This study investigated the effect of different levels of nitrogen and sulfur on the tris-soluble and glutenin protein fractions by 2D-electrophoresis. Multivariate analysis was performed to study changes in the proteome pattern. In the tris-soluble fraction 20 proteins were changed in abundance due to S fertilization, whereas 16 proteins were changed in the glutenin protein fraction. It was found that induced sulfur deficiency during growth resulted in the most pronounced effect on protein composition. Understanding which proteins are affected by varying levels of fertilizers may help tailor specific traits in various wheat varieties.

Influence of temperature during grain filling on gluten viscoelastic properties and gluten protein composition

BACKGROUND The aim of this study was to investigate the effects of low to moderate temperatures on gluten functionality and gluten protein composition. Four spring wheat cultivars were grown in climate chambers with three temperature regimes (day/night temperatures of 13/10, 18/15 and 23/20 °C) during grain filling. RESULTS The temperature strongly influenced grain weight and protein content. Gluten quality measured by maximum resistance to extension (Rmax ) was highest in three cultivars grown at 13 °C. Rmax was positively correlated with the proportion of sodium dodecyl sulfate-unextractable polymeric proteins (%UPP). The proportions of ω-gliadins and D-type low-molecular-weight glutenin subunits (LMW-GS) increased and the proportions of α- and γ-gliadins and B-type LMW-GS decreased with higher temperature, while the proportion of high-molecular-weight glutenin subunits (HMW-GS) was constant between temperatures. The cultivar Berserk had strong and constant Rmax between the different temperatures. CONCLUSION Constant low temperature, even as low as 13 °C, had no negative effects on gluten quality. The observed variation in Rmax related to temperature could be explained more by %UPP than by changes in the proportions of HMW-GS or other gluten proteins. The four cultivars responded differently to temperature, as gluten from Berserk was stronger and more stable over a wide range of temperatures.

Gene dosage effects on storage proteins in wheat (Triticum aestivum)

The storage proteins of F 1 and F 2 seeds of wheat were characterised in terms of their high-molecular-weight (HMW) glutenin subunits by SDS-polyacrylamide gel electrophoresis. It was possible to distinguish between haploid, diploid and triploid gene dosage effects on these endosperm proteins. A novel, minor HMW subunit of glutenin associated with band 2 * was identified.

Investigating environmental factors that cause extreme gluten quality deficiency in winter wheat (Triticum aestivum L.)

ABSTRACT Unstable breadmaking quality of wheat due to environmental influence has been a problem for Norwegian milling industries. Large variation in gluten quality was observed from field trials with Norwegian winter wheat conducted in several locations between 2005 and 2013. Moreover, extremely poor gluten quality was observed in several locations in the 2007 and 2011 season, and indicated almost complete loss of breadmaking quality. To investigate the environmental factors which cause extremely weak gluten, gluten proteins were characterized in samples selected within the 2011 season. The results revealed that the proportion of large glutenin polymers decreased in wheat samples with extremely weak gluten. Moreover, re-polymerization of large glutenin polymers, which normally occur during the resting period of a dough, did not take place in gluten prepared from these samples. Incubation of total proteins extracted from these samples in an in vitro system showed a drastic degradation of gluten proteins indicating protease activities. The origin of the proteases remains unclear; however, exogenous proteases derived from Fusarium spp. seem to play a key role for protein degradation, and thus causing severe quality deficiency. A genotypic difference was found between the two cultivars and one of them had higher resistance against the factors influencing gluten quality in negative way.