USE OF RECOMBINANT PEPTIDES TO EXPLORE THE MOLECULAR MECHANISM OF GLUTEN PROTEIN VISCOELASTICITY

摘要

Wheat gluten proteins are characterised by the presence of domains comprising repeated sequences based on one or more short peptide motifs. In the HMW subunits of glutenin these domains range from about 480 to 700 ammo acids, accounting for 75-85% of the whole protein1. Two motifs, based on hexapeptides (PGQGQQ) and nonapeptides (GYYPTSP/LQQ), are present in all HMW subunits while the x-type subunits also contain tripeptide motifs (GQQ). Both the nonapeptide and tripeptide are always present in tandem with a hexapeptide.