Glutelin

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Glutelin
Identifiers
SymbolGlutelin
InterPro IPR000480

Glutelins are a class of prolamin proteins found in the endosperm of certain seeds of the grass family. They constitute a major component of the protein composite collectively referred to as gluten. 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. The glutelins of barley and rye [1] have also been identified. Glutelins are the primary protein form of energy storage in the endosperm of rice grains. [2]

This class was originally differentiated from prolamins by Thomas Burr Osborne according to its low solubility. Modern analysis now considers glutelins as a low-solubility subclass of prolamins.

Glutelins are soluble in dilute acids or bases, detergents, chaotropic agents, or reducing agents. They are also rich in hydrophobic amino acids, with a content of phenylalanine, valine, tyrosine, proline and leucine corresponding to approximately 45% of the amino acid sequence with access code P04706.1, though that specific amino acid profile is not characteristic of all glutelins. [3] There are typically both high-molecular-weight (HMW) and low-molecular-weight (LMW) glutelins in most grass species. These proteins cross-link with themselves and other proteins during baking via disulfide bonds. The LMW ones are similar to Gliadin.

A high-molecular weight glutelin (glutenin) of the grass tribe Triticeae has been implicated as a sensitizing agent for coeliac disease in individuals possessing the HLA-DQ8 class II antigen receptor gene. [4] [ verification needed ]

Related Research Articles

<span class="mw-page-title-main">Gluten</span> Group of cereal grain proteins

Gluten is a structural protein naturally found in certain cereal grains. Although "gluten" often only refers to wheat proteins, in medical literature it refers to the combination of prolamin and glutelin proteins naturally occurring in all grains that have been proven capable of triggering celiac disease. These include any species of wheat, barley, rye and some oat cultivars, as well as any cross hybrids of these grains. Gluten makes up 75–85% of the total protein in bread wheat.

<span class="mw-page-title-main">Bread</span> Food made of flour and water

Bread is a staple food prepared from a dough of flour and water, usually by baking. Throughout recorded history and around the world, it has been an important part of many cultures' diet. It is one of the oldest human-made foods, having been of significance since the dawn of agriculture, and plays an essential role in both religious rituals and secular culture.

<span class="mw-page-title-main">Oat</span> Cool weather staple grain, animal feed

The oat, sometimes called the common oat, is a species of cereal grain grown for its seed, which is known by the same name. While oats are suitable for human consumption as oatmeal and rolled oats, one of the most common uses is as livestock feed. Oats are a nutrient-rich food associated with lower blood cholesterol when consumed regularly.

<span class="mw-page-title-main">Flour</span> Cereal grains ground into powder

Flour is a powder made by grinding raw grains, roots, beans, nuts, or seeds. Flours are used to make many different foods. Cereal flour, particularly wheat flour, is the main ingredient of bread, which is a staple food for many cultures. Corn flour has been important in Mesoamerican cuisine since ancient times and remains a staple in the Americas. Rye flour is a constituent of bread in both Central Europe and Northern Europe.

<span class="mw-page-title-main">Coeliac disease</span> Autoimmune disorder that results in a reaction to gluten

Coeliac disease or celiac disease is a long-term autoimmune disorder, primarily affecting the small intestine, where individuals develop intolerance to gluten, present in foods such as wheat, rye and barley. Classic symptoms include gastrointestinal problems such as chronic diarrhoea, abdominal distention, malabsorption, loss of appetite, and among children failure to grow normally. This often begins between six months and two years of age. Non-classic symptoms are more common, especially in people older than two years. There may be mild or absent gastrointestinal symptoms, a wide number of symptoms involving any part of the body, or no obvious symptoms. Coeliac disease was first described in childhood; however, it may develop at any age. It is associated with other autoimmune diseases, such as Type 1 diabetes mellitus and Hashimoto's thyroiditis, among others.

<span class="mw-page-title-main">Spelt</span> Species of grain

Spelt, also known as dinkel wheat or hulled wheat, is a species of wheat that has been cultivated since approximately 5000 BCE.

Glutenin is a major protein within wheat flour, making up 47% of the total protein content. The glutenins are protein aggregates of high-molecular-mass (HMW) and low-molecular-mass (LMW) subunits with molar masses from about 200,000 to a few million, which are stabilized by intermolecular disulfide bonds, hydrophobic interactions and other forces. Glutenin is responsible for the strength and elasticity of dough.

<span class="mw-page-title-main">Gliadin</span>

Gliadin is a class of proteins present in wheat and several other cereals within the grass genus Triticum. Gliadins, which are a component of gluten, are essential for giving bread the ability to rise properly during baking. Gliadins and glutenins are the two main components of the gluten fraction of the wheat seed. This gluten is found in products such as wheat flour. Gluten is split about evenly between the gliadins and glutenins, although there are variations found in different sources.

<span class="mw-page-title-main">Whole grain</span> Cereal containing endosperm, germ, and bran

A whole grain is a grain of any cereal and pseudocereal that contains the endosperm, germ, and bran, in contrast to refined grains, which retain only the endosperm.

Hordein is a prolamin glycoprotein, present in barley and some other cereals, together with gliadin and other glycoproteins coming under the general name of gluten. Hordeins are found in the endosperm where one of their functions is to act as a storage unit.

Prolamins are a group of plant storage proteins having a high proline amino acid content. They are found in plants, mainly in the seeds of cereal grains such as wheat (gliadin), barley (hordein), rye (secalin), corn (zein), sorghum (kafirin), and oats (avenin). They are characterised by a high glutamine and proline content, and have poor solubility in water. They solubilise best in strong alcohol [70-80%], light acid, and alkaline solutions. The prolamins of the tribe Triticeae, such as wheat gliadin, and related proteins are known to trigger coeliac disease, an autoimmune condition, in genetically predisposed individuals.

<span class="mw-page-title-main">Wheat allergy</span> Medical condition

Wheat allergy is an allergy to wheat which typically presents itself as a food allergy, but can also be a contact allergy resulting from occupational exposure. Like all allergies, wheat allergy involves immunoglobulin E and mast cell response. Typically the allergy is limited to the seed storage proteins of wheat. Some reactions are restricted to wheat proteins, while others can react across many varieties of seeds and other plant tissues. Wheat allergy is rare. Prevalence in adults was found to be 0.21% in a 2012 study in Japan.

<span class="mw-page-title-main">Triticeae glutens</span> Seed storage protein in mature wheat seeds

Gluten is the seed storage protein in mature wheat seeds. It is the sticky substance in bread wheat which allows dough to rise and retain its shape during baking. The same, or very similar, proteins are also found in related grasses within the tribe Triticeae. Seed glutens of some non-Triticeae plants have similar properties, but none can perform on a par with those of the Triticeae taxa, particularly the Triticum species. What distinguishes bread wheat from these other grass seeds is the quantity of these proteins and the level of subcomponents, with bread wheat having the highest protein content and a complex mixture of proteins derived from three grass species.

<span class="mw-page-title-main">Gluten-related disorders</span> Set of diseases caused by gluten exposure

Gluten-related disorders is the term for the diseases triggered by gluten, including celiac disease (CD), non-celiac gluten sensitivity (NCGS), gluten ataxia, dermatitis herpetiformis (DH) and wheat allergy. The umbrella category has also been referred to as gluten intolerance, though a multi-disciplinary physician-led study, based in part on the 2011 International Coeliac Disease Symposium, concluded that the use of this term should be avoided due to a lack of specificity.

Anti-gliadin antibodies are produced in response to gliadin, a prolamin found in wheat. In bread wheat it is encoded by three different alleles, AA, BB, and DD. These alleles can produce slightly different gliadins, which can cause the body to produce different antibodies. Some of these antibodies can detect proteins in specific grass taxa such as Triticeae, while others react sporadically with certain species in those taxa, or over many taxonomically defined grass tribes.

Oat sensitivity represents a sensitivity to the proteins found in oats, Avena sativa. Sensitivity to oats can manifest as a result of allergy to oat seed storage proteins either inhaled or ingested. A more complex condition affects individuals who have gluten-sensitive enteropathy in which there is an autoimmune response to avenin, the glutinous protein in oats similar to the gluten within wheat. Sensitivity to oat foods can also result from their frequent contamination by wheat, barley, or rye particles.

The immunochemistry of Triticeae glutens is important in several inflammatory diseases. It can be subdivided into innate responses, class II mediated presentation, class I mediated stimulation of killer cells, and antibody recognition. The responses to gluten proteins and polypeptide regions differs according to the type of gluten sensitivity. The response is also dependent on the genetic makeup of the human leukocyte antigen genes. In gluten sensitive enteropathy, there are four types of recognition, innate immunity, HLA-DQ, and antibody recognition of gliadin and transglutaminase. With idiopathic gluten sensitivity only antibody recognition to gliadin has been resolved. In wheat allergy, the response pathways are mediated through IgE against other wheat proteins and other forms of gliadin.

Storage proteins serve as biological reserves of metal ions and amino acids, used by organisms. They are found in plant seeds, egg whites, and milk.

<span class="mw-page-title-main">Cupin superfamily</span>

The cupin superfamily is a diverse superfamily of proteins named after its conserved barrel domain. The superfamily includes a wide variety of enzymes as well as non-enzymatic seed storage proteins.

Caricain is an enzyme. This enzyme catalyses the following chemical reaction: Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain

References

  1. Shang H, Wei Y, Long H, Yan Z, Zheng Y (2005). "Identification of LMW glutenin-like genes from Secale sylvestre host". Genetika. 41 (12): 1656–64. PMID   16396452.
  2. Kei Takahashi; Hiromi Kohno; Tomomichi Kanabayashi; Masaki Okuda (2019). "Glutelin subtype-dependent protein localization in rice grain evidenced by immunodetection analyses". Plant Molecular Biology. 100 (3): 231–246. doi:10.1007/s11103-019-00855-5. PMC   6542783 . PMID   30911876.
  3. Elwart J. A. D. (1967). "Amino acid analysis of glutenins and gliadins". J. Sci. Food Agric. 10 (3): 111–117. doi:10.1002/jsfa.2740180307. PMID   6042168.
  4. Dewar D, Amato M, Ellis H, Pollock E, Gonzalez-Cinca N, Wieser H, Ciclitira P (2006). "The toxicity of high molecular weight glutenin subunits of wheat to patients with coeliac disease". Eur J Gastroenterol Hepatol. 18 (5): 483–91. doi:10.1097/00042737-200605000-00005. PMID   16607142.