Gluten is a mixture of different proteins. Gluten is responsible for ensuring that liquid mixed with flour gets a sticky consistency.
The dough of bread or other pastry has a cohesion due to the protein mixture and forms a homogeneous mass. The change in consistency is due to the fact that the egg whites in the dough assume a three-dimensional structure. This is not reversible (irreversible). Gluten is an adhesive white, but no glue. In contrast to gluten, adhesives are not just proteins, but proteins, fats and carbohydrates.
Gluten in its entirety has no significance for the health or the human body. An exception is only the gluten intolerance or celiac disease. However, gluten is composed of different proteins. The proteins consist of long chains of amino acids. The cleavage of proteins releases energy that the body can use for its metabolic processes. At the end of this processing, the amino acids are free or fragmented into shorter chains.
The body needs the amino acids as building blocks for other molecules that serve as the source material for all cells, hormones, transmitters, tissue types, etc. In total, there are 23 known proteinogenic amino acids, from which almost infinitely many proteins can be composed. Of these amino acids eight are essential for humans, that is essential for life. These include isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan and valine. In addition, the organism needs semi-essential amino acids: For example, an injury requires that certain amino acids be present to assist the body in coping with this injury. If there is no injury, they are not so important to the functioning of the human body.
The number and order of the amino acids as well as the spatial structure of the folded chain determine the properties of the proteins - comparable to letters that string together into words. In addition to the proteinogenic amino acids, there are numerous other amino acids that are not used as building materials in proteins. Biology calls them nonproteinogenic amino acids. They influence, for example, the enzymatic reaction. Researchers have identified around 400 different nonproteinogenic amino acids.
Gluten is present in different cereals, but not all. Spelled has one of the highest proportions of gluten with 10.3 g gluten per 100 g flour. Oats, on the other hand, have about 5.6 grams of gluten per 100 grams of flour. The gluten in the wheat forms the basis for the so-called wheat meat, the seitan. It is an increasingly popular alternative to meat and, like this, is very rich in protein. The gluten-free cereals include millet, corn, rice and teff.
Teff or dwarf millet is a sweetgrass that is found mainly in Ethiopia and is very widespread there. Buckwheat, amaranth and quinoa are not gluten-free in addition to these cereals. From a biological point of view, however, they are not crops; botany therefore also calls it pseudo-grain.
The two components of the gluten are prolamine and gluteline. Prolamins do not serve as building materials and are not enzymes either: they are storage proteins that the plant forms in the seeds. During germination, these proteins are available to the new plant. That is why biology calls them reserve substances. Prolamins are not single-origin proteins, but are also composed of different proteins.
Gluten intolerance is a common gluten disorder. It is also referred to as celiac disease or gluten-sensitive or gluten-induced enteropathy. This disease is a cross between allergy and autoimmune disease. It is thus significantly different from the wheat allergy, but can show similar symptoms.
People who do not tolerate gluten are hypersensitive to the components of the gluten. As a result, a chronic inflammation of the intestinal mucosa manifests. Without dietary measures, it leads in many cases to a destruction of the epithelial cells in the intestine. As a result, the body can no longer absorb nutrients correctly. The digestion remains incomplete.
This disorder causes various symptoms. Disturbances such as diarrhea, but also vomiting, loss of appetite, weight loss, depressive symptoms, tiredness and concentration problems are characteristic. In children, celiac disease can also interfere with physical development. Affected children develop physiologically more slowly than healthy peers. Medicine describes this disease as a failure to thrive. The extent of the symptoms depends on how severe the gluten intolerance is in the individual case. Some sufferers experience only mild digestive discomfort, while others have to accept heavy loss of function.
Gluten intolerance can be hereditary. People with celiac disease suffer the symptoms of their entire life when they take gluten; there is no cure. Those affected can control the disease by changing their diet and avoiding gluten-containing foods. Not only do you have to stop eating gluten-containing cereals, but you may also need to consider contaminants in other foods. People with uncontrolled celiac disease are at an increased risk for certain cancers and diabetes.