INDEX WORDSTriticum aestivum, wheat, glutenin, SDS-sedimentation test, SDS-polyacrylamidegel-electrophoresis, baking quality selection. SUMMARY Gelprotein or SDS-insoluble gel-forming glutenin was isolated from wheat flour by extraction with an aqueous 1.5% SDS solution. Remarkable intervarietal differences were observed both in amount and subunit composition of these proteins.The amount of gelprotein and the SDS-sedimentation volume both proved to be good parameters for the bread-making quality of wheat cultivars. A high correlation was observed between amount of gelprotein and SDS-sedimentation volume. The amount of gelprotein was therefore tentatively assumed to be the essential basis of the SDS-sedimentation test.The subunit composition of the gelprotein was studied by SDS-PAGE after reduction of SS bonds by mercaptoethanol. It was found that the average bread-making quality of wheat cultivars and progeny of the cross Atlas 66 x Atys which possessed subunits 3 and 10, coded for by chromosome lD, was significantly higher than that of wheat samples possessing subunits 2 and 11, their allelic counterparts.
Enzymatic oxidations of linoleic acid and glycerol‐1‐monolinoleate, and the products formed by these oxidations in flour‐water suspensions and doughs were studied. Oxidation of linoleic acid leads through simultaneous reactions to two isomeric hydroperoxy‐octadecadienoic acids and two isomeric hydroxy‐epoxy‐octadecenoic acids. Reduction of the former leads to hydroxyoctadecadienoic acid, while hydrolysis of the latter yields trihydroxy‐octadecenoic acids. The hydroperoxy acids are formed by the enzyme lipoxygenase (E.C. 1.13.1.13), whereas the hydroxy‐epoxy acids are formed by combined action of lipoxygenase and an unknown factor Y. This factor Y is localized in the gluten fraction. Oxidation of glycerol‐1‐monolinoleate gives a product having a hydroperoxy group and acis,trans conjugated diene bond. The oxidation of glycerol‐1‐monolinoleate is probably a lipoxygenase reaction.
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