Solubility-composition Relations of Gluten Proteins

Tracey, MV

doi:10.1038/211850a0

Cited by 1 publication

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“…The presence of higher quantities of 35% ethanolsoluble proteins in the mutants and Hiproly than in NP-113 might be a reflection of the lower hydrophobic interactions due to a higher proportion of amino acids with polar side chains in the proteins, causing the proteins to remain in solution in a more polar solvent like 35% ethanol compared with 70% ethanol. The prolamin fraction was soluble in nonpolar solvents like ethanol, chloroform, and methanol, owing primarily to the presence of large proportions of amino acids with nonpolar side chains and consequent hydrophobic interactions of these proteins with the solvent (Tracey, 1966).…”

Section: Discussionmentioning

confidence: 99%

Studies on the proteins of the mutants of barley grain. 2. Fractionation and characterization of the alcohol-soluble proteins

Singh¹,

Sastry²

1977

J. Agric. Food Chem.

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Fractionation and characterization of the alcohol-soluble proteins of a barley variety, its mutants, and Hiproly, a high-protein and high-nutritive barley isolated from the world barley collection, indicate quantitative and qualitative changes in the mutants. The 35 % ethanol-soluble subfraction is higher in proportion in the mutants and Hiproly, and this could have resulted from the higher proportions of the polar amino acids in these proteins among which are also some limiting amino acids like lysine and threonine. The digestibility, as observed by the in vitro procedure, of this subfraction in all the varieties also is higher and, presumably as a result, the hordein fraction of these mutants also shows better digestibility. It appears that, in view of the presence of more polar amino acids which include lysine in this subfraction and better digestibility, its enrichment could be a nutritionally favorable index of better grain quality.

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Section: Discussionmentioning

confidence: 99%