Cereal Chem 66:26-30   |  VIEW ARTICLE

The Role of Low Molecular Weight Glutenin Proteins in the Determination of Cooking Quality of Pasta Products: An Overview.

P. Feillet, O. Ait-Mouh, K. Kobrehel, and J.-C. Autran. Copyright 1989 by the American Association of Cereal Chemists, Inc. 

Low molecular weight glutenin (LMWG) proteins are those proteins that correspond to large aggregates in wheat and upon reduction yield subunits with apparent molecular weights of 12,000-60,000. Estimation of their content, by combining sequential extraction, chromatography, and electrophoresis, showed that they make up a major fraction of durum wheat gluten and that their content in durum wheat of gamma-45 type is higher (28%) than in the gamma-42 type (15%). The discovery of a recombination with the Gli-B1 locus between gamma-gliadins and LMWG indicated that gamma-gliadins 42 and 45 are only gene tic markers of pasta firmness and elasticity. LMWG strongly aggregate through heat treatments and contribute to pasta firmness and elasticity. Sulfur-rich glutenin proteins were also found associated to surface condition of cooked pasta, and a new model was proposed to explain their contribution to the aggregation of LMWG through hydrophobic and disulfide bonds.