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Wheat flour proteins: The selectivity of solvents and the stability of gliadin and glutenin fractions of stored flours
Author(s) -
Shearer George,
Patey Alan L.,
McWeeny David J.
Publication year - 1975
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740260314
Subject(s) - glutenin , gliadin , chemistry , chromatography , size exclusion chromatography , gluten , polyacrylamide gel electrophoresis , starch , wheat flour , gel electrophoresis , storage protein , extraction (chemistry) , polyacrylamide , food science , biochemistry , enzyme , polymer chemistry , protein subunit , gene
A gel‐filtration study of extraction of wheat proteins by eight separate solvent systems is presented and the nature of the protein classes extracted by each solvent has been quantified. As judged by carboxymethylcellulose ion‐exchange chromatography, gel‐filtration and starch‐gel electrophoresis, no storage changes have occurred in wheat flour gliadin and glutenin proteins extracted from flours kept at 25, 12 and ‐20 °C for 18 months. SDS‐polyacrylamide‐gel electrophoresis shows minimal change in the gluten molecular weight distribution on storage. Six and twenty‐year‐old flours were also tested.