Glutelin

Glutelin proteins are soluble in dilute acids or bases, detergents, chaotropic agents, or reducing agents. In general, they are prolamin-like proteins in certain grass seeds. 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 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.[2]

Glutelins are the primary energy storage in the endosperm of rice.

There are typically high-molecular-weight (HMW) and low-molecular-weight (LMW) glutelins in these species. They crosslink with themselves and other proteins during baking via disulfide bonds.

A HMW glutelin (glutenin) of the grass tribe Triticeae can be sensitizing agents for coeliac disease in individuals possessing the HLA-DQ8 class II antigen receptor gene.[3] (not yet characterized to the epitope level)

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. ↑ Elwart J. A. D. (1967). "Amino acid analysis of glutenins and gliadins". J. Sci. Food Agric. 10: 111–117.
  3. ↑ 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. PMID 16607142. doi:10.1097/00042737-200605000-00005.
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