Recent results in the investigation of the structure of the gluten complex

Abstract

AbstractIt is generally accepted that gluten complex is composed from different groups of proteins bound by covalent and non covalent system of bonds resp. interactions. The two main groups of those are low molecular weight (LMW)‐ and high molecular weight (HMW)‐storage proteins of wheat. Probably a third group of proteins (membrane proteins, residue proteins) play a definition role.The LMW‐storage proteins are characterized by globular shape and intramolecular disulphide bonds. The most commonly held view of the structure of the HMW‐storage proteins (glutenins) of wheat is that it consists of a mixture of polypeptide subunits crosslinked by intermolecular disulphide bonds in such a way as to yield a broad spectrum of molecular weights ranging up to higher polymers with molecular weights in the millions. According to the model proposed more recently (GRAVELAND) glutenins are composed from three types of clusters consisting from different types of subunits. According to an alternative model of the glutenin structure (KASARDA et al.) there are no interpolypeptide disulphide bonds in HMW‐storage proteins. They aggregate strongly through secondary bonding forces such as hydrogen bonds, ionic bonds and hydrophobic interactions.The third group of proteins is till now poorely characterized. Further studies are needed to know the exact place of the interacting non protein components (especially lipids and carbohydrates) of the gluten complex.