Cereal Chem 51:288 - 299.  |  VIEW ARTICLE
Submicroscopic Structure of Wheat Flour and Gluten Lipoprotein Components.

N. Crozet, B. Godon, L. Petit, and A. Guilbot. Copyright 1974 by the American Association of Cereal Chemists, Inc. 

Protein fractions of gluten, obtained either by the Osborne separation method or by acetic acid solubilization followed by chromatography on Sephadex G-100, were observed by electron microscopy. Gliadin and fractions with a high gliadin content have a smooth, compact, and nearly electron-lucent structure; glutenin and fractions with a high glutenin content present a granular and fibrillar structure. The fibrils have a diameter of 100 to 200 Angstroms and form compact networks. Albumins and globulins have a structure which is more like glutenin than gliadin. In gluten there is a smooth, compact matrix similar to gliadin which, however, encloses zones of structure similar to glutenin, albumins, and globulins. Flour proteins also present two kinds of structure: fragments of relatively compact and nearly electron-lucent proteins, and granular zones and fibrillar felting which adhere to both starch granules and protein fragments.