Glutelin

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Glutelins are a class of prolamin-like 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 form of energy storage in the endosperm of rice grains.

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.[2] 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.

An HMW 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.[3]

References[edit]

  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. doi:10.1097/00042737-200605000-00005. PMID 16607142.

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