Abstract
AbstractThe amino acid analyser has been used to determine which amino acid side chains (except that of tryptophan) in wheat proteins are attacked by three reagents. Glutaraldehyde crosslinks gliadin by reacting with lysine and tyrosine residues so that it gives an electrophoretic pattern resembling that of glutenin. Wheat gliadin after treatment with nitrous acid suffers an overall reduction in electrophoretic mobility due to deamination of lysine side chains. Chlorine oxidises part of the cystine and methionine of wheat flour protein to cysteic acid and the sulphone respectively, destroys a fraction of the tyrosine and histidine, and causes some deamidation probably as a result of hydrolysis by hydrochloric acid. The results suggest that there may be buried lysine and tyrosine residues in, and some degrees of structural similarity among, the gliadin proteins. Additional support for the crosslinked nature of glutenin is provided.
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