ABSTRACT
The content and composition of the disulfide-bonded glutenin macropolymer has been shown to influence dough properties, although its structural organization is poorly characterized. The structure of the glutenin macropolymer in dough was studied using an immunolocalization transmission electron microscopy (TEM) technique by localizing gliadins, low molecular weight glutenin subunits (LMW-GS), and high molecular weight glutenin subunits (HMW-GS) in sections of dough using antibody probes selective for each of the three classes of gluten polypeptides. Distinct differences in the distribution patterns of gliadins, LMW-GS, and HMW-GS were observed, which suggests that proteins have different roles in the structural organization of the gluten matrix. On the basis of the observed distribution of the proteins in dough, it is speculated that gliadins, which are randomly distributed as individual particles, fill space within the glutenin macropolymer; LMW-GS, which are present as clusters, are speculated to form aggregated branch structures; and HMW-GS, which are present as chains, are speculated to form a network from which the LMW-GS branches are formed. Changes in the distribution of gliadins, LMW-GS, and HMW-GS in dough during mixing were also noted. Such an arrangement supports previous biochemical evidence which has established that gliadins, LMW-GS, and HMW-GS have specific roles in the structural organization of the glutenin macropolymer in doughs.
