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Improving wheat to remove coeliac epitopes but retain functionality

by luciano

An interesting study that explores the possibilities of obtaining low toxicity grains by investigating the quality, quantity and distribution of the toxic fractions (for celiacs) of whea

“…..omissis. Wheat gluten proteins are traditionally classified into two groups based on their solubility. The gliadins are readily extracted from flour with alcohol:water mixtures, such as 60% (v/v) ethanol or 50% (v/v) propan-1- ol, while the glutenins were traditionally extracted with dilute acid or alkali. However, these fractions contain related proteins and the differences in solubility are determined by their presence as monomers or polymers. Thus, the gliadin fraction comprises mainly proteins which are present as monomers, with small amounts of polymeric components, while the glutenins comprise “subunits” assembled into high molecular mass polymers stabilized principally by inter-chain disulphide bonds. When these disulphide bonds are reduced the monomeric glutenin subunits resemble the gliadins in being soluble in alcohol: water mixtures. Hence, the protein subunits present in both fractions correspond to alcohol-soluble prolamin proteins as defined in the classic studies of Osborne (1924). more in full text”. Improving wheat to remove coeliac epitopes but retain functionality. Peter R. Shewry and Arthur S. Tatham. Journal of Cereal Science 2016 Jan

Extract from the study:
1.2. Wheat gluten protein
1.3. Wheat gluten protein genes and expressed proteins
2.2. Identification of coeliac disease epitopes
2.3. Distribution of coeliac disease epitopes
3.1. Genetic diversity of wheat
3.2. Exploiting genetic diversity in gluten proteins to reduce coeliac toxicity
3.3. Developing coeliac-safe wheat