glutenin

The protein content is higher than that of wheat, although the glutenin fraction is less.

Gluten is a composite of the proteins gliadin and glutenin.

Gliadins are known for their role, along with glutenin, in the formation of gluten.

True gluten, with gliadin and glutenin, is limited to certain members of the grass family.

Rye flour is high in gliadin but low in glutenin.

Gliadin and glutenin make up about 80% of the protein contained in wheat seed.

Gliadin is the soluble aspect of it while glutenin is insoluble.

"Glutenin runs off with sugar," Ms. Corriher said.

Glutenin in wheat forms long covalantly interlinked polymers of two repeating subunits.

Glutenin (wheat glutelin) is a predominant allergen in wheat.

Glutenin is 35-40% of wheat (Triticum aestivum) protein.

When flour is mixed with water, the water-soluble proteins dissolve, leaving the glutenin and gliadin to form the structure of the resulting bread.

Considerable efforts have been made to understand the relationship between gliadin and glutenin composition and rheological properties of wheat dough.

Gliadin has primarily monomeric proteins, which differs from glutenin, which has primarily polymers.

Breadmaking qualities are largely dependent on the number and composition of HMW glutenin subunits.

Glutenin (also called glutelin or glutenine) is the major protein within wheat flour, making up 47% of the total protein content.

The expression "corn gluten" is colloquial jargon that describes corn proteins that are neither gliadin nor glutenin.

Only wheat, barley, rye and oat contain true gluten which is formed by the interaction of gliadin and glutenin proteins).

Gluten is the composite of a gliadin and a glutenin, which is conjoined with starch in the endosperm of various grass-related grains.

Glutenin is the most common glutelin, as it is found in wheat and is responsible for some of the refined baking properties in bread wheat.

Gluten forms when glutenin molecules cross-link to form a sub-microscopic network attached to gliadin, which contributes viscosity (thickness) and extensibility to the mix.

Gluten is composed of a gliadin fraction (alcohol soluble) and a glutenin fraction (only soluble in dilute acids or alkali).

The orthologous protein sequences match very well at the region where the high molecular weight Glutenin domain and ATPase involved domain is.

T-cell responses to the high molecular weight glutenin may be more important with DQ8 mediated than DQ2.5 mediated celiac disease.

Before the glutenin and gliadin proteins can clump together as gluten, they must first partly unwind and unfold, and acidity in the batter induces that unwinding.