Abstract

Investigations of the submicroscopic structure of gluten protein fractions by means of SEM have revealed significant changes in the structure of glutenins due to the removal of flour lipids by extraction with petroleum ether and chloroform-methanol resp. Defatting of the flour caused a rupture of the sheetlike structure observed in the glutenin of untreated flour and an increase of the amount of fibrillar components. The number of spherical particles arising from delipidation with petroleum ether decreases considerably in the glutenin from chloroform-methanol defatted flour. It has been concluded that these spherical particles may consist mainly of chloroform-methanol soluble lipoproteids originally existing in wheat flour. Furthermore it could be shown that the gliadin fraction also is very heterogenous and consists of sheetlike, fibrillar, and spherical aggregates.

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