Exploring the conditions for the expression of low molecular weight glutenin 1D1 protein in Escherichia coli (E. coli).

摘要

Scope of study. Bread wheat (Triticum aestivum ) is one of the major cereal crops used for making flour. Wheat flour has unique rheological properties which have been attributed to its protein content. Glutens are a major class of wheat proteins contributing to the elasticity and viscosity of wheat dough. Two classes of wheat gluten proteins have been identified: High Molecular Weight Glutenins (HMW) and Low Molecular Weight Glutenins (LMW). Different allelic forms of LMW seem to play different roles in determining the different quality parameters of wheat dough.The goal of the present study is to express the gene encoding the Low Molecular Weight Glutenin 1D1 protein in a bacterial system and purify the protein. The purified protein would then be used to determine its rheological and mixographic properties which are important parameters for determining the quality of dough in the bread making industry.To this end we have tried expressing the gene in various expression vectors and in different bacterial host strains but we were unable to express and purify the protein to its homogeneity. We could express the protein with a fusion tag which was difficult to cleave and hence, we hypothesize that the future studies to express and characterize Low Molecular Weight Glutenin 1D1 protein should utilize eukaryotic systems.