Gliadin

Gliadin is an alcohol-soluble protein obtained from wheat. Gliadin is one of the components of gluten.

Gliadin belongs to prolamins, a group of storage proteins characteristic of cereal crops. Together with glutenin, gliadin forms gluten, a complex of proteins that gives the viscoelastic structure to dough and bread.

Gliadin has an unusually high solubility in 70-80% ethyl alcohol. This property is used to isolate gliadin from wheat flour. When flour is treated with alcohol, gliadin goes into solution, and insoluble glutenin remains in the sediment.

Gliadin does not contain all the essential amino acids and is therefore an incomplete protein. However, in the composition of gluten, together with glutenin, gliadin provides a balanced amino acid composition.

In people with a genetically determined intolerance to gliadin (celiac disease), its consumption causes damage to the villi of the small intestine and impairs the absorption of nutrients. A diet without gliadin is the only treatment method for celiac disease today.

Gliadin is an alcohol-soluble protein obtained from wheat. Gliadin is one of the components of gluten.

Gliadin is a mixture of proteins that dissolve in 70-80% ethyl alcohol. It is obtained from wheat flour by extraction with alcohol. Gliadin is a component of gluten along with glutenin.

Gliadin gives the dough extensibility and elasticity. Thanks to the presence of gliadin, the dough can rise during kneading and baking. With a lack of gliadin, the dough becomes tough and inelastic.

Excess gliadin is also undesirable, as it can lead to excessive stickiness and stickiness of the dough, making it difficult to shape products. Therefore, an optimal ratio of gliadin and glutenin is important for a good dough.

When you eat foods containing wheat, your stomach encounters gliadins, soluble proteins obtained from wheat grains. These proteins provide texture and the ability to bind other ingredients together, such as flour and eggs for breads and cakes. Like all proteins, gliadins are the main structural components of our body and exist to create strength and integrity in our body.

Gliadins are fairly small proteins that are secreted by special enzymes called glutenolinosins. These enzymes break down gluten and enable other proteins to do the same. Gliadins are responsible for obtaining the required form of products: for example, gluten makes it possible to form such an important food group as bread, muffins or cakes. Thus, we can safely say that the texture and taste of our products depend on the ability of glutenolinases to cause an increase in protein structure and expansion of its spatial network.

However, in the case of wheat, allergies to gluten-containing proteins have several causes. First, our bodies don't produce enough glutathione transferase to eliminate toxic fractions of wheat, such as allincarotenes—molecules that can also cause inflammation and gut damage. This