glutelin


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Related to glutelin: gluten, albumin

glu·te·lin

 (glo͞o′tə-lĭn)
n.
Any of a class of simple proteins that are found in cereal grains and are soluble in dilute acids or bases. Glutelins are a major component of gluten in wheat.

[Alteration of glutenin, glutelin found in wheat (probably influenced by globulin) : gluten + -in.]
American Heritage® Dictionary of the English Language, Fifth Edition. Copyright © 2016 by Houghton Mifflin Harcourt Publishing Company. Published by Houghton Mifflin Harcourt Publishing Company. All rights reserved.

glutelin

(ˈɡluːtɪlɪn)
n
(Biochemistry) any of a group of water-insoluble plant proteins found in cereals. They are precipitated by alcohol and are not coagulated by heat. Compare gliadin
[C20: See gluten, -in]
Collins English Dictionary – Complete and Unabridged, 12th Edition 2014 © HarperCollins Publishers 1991, 1994, 1998, 2000, 2003, 2006, 2007, 2009, 2011, 2014
ThesaurusAntonymsRelated WordsSynonymsLegend:
Noun1.glutelin - a simple protein found in the seeds of cereals
simple protein - a protein that yields only amino acids when hydrolyzed
Based on WordNet 3.0, Farlex clipart collection. © 2003-2012 Princeton University, Farlex Inc.
References in periodicals archive ?
The results were similar to that for peanut protein and corn glutelin reported by Zhao et al.
Millet total protein content ranged from 11-17% dependent on variety, of which 11.3-17.2% was albumin/globulins, 6.8-11.6 prolamins, 5.9-54.4% glutelin [10,11].
The defatted barley flour was treated with 1 M NaCl solution (10 : 1 v/w) for 1 h to remove albumin, globulin, and glutelin. This step was repeated twice and then washed by deionized water 3 times (1 h each time) to eliminate the disturbance of reagents and small molecule materials, and centrifuged at 7,000 xg for 30 min at room temperature.
[56] who reported that the antioxidant properties of the barley glutelin hydrolysates had ferric-reducing power values of 24.0 pg [Fe.sup.2+]/mg, respectively.
Furthermore, the raw albumin and glutelin fractions of the bean proteins show low digestibility; in the case of albumins, this fact is also promoted by a high number of disulfide bridges and the presence of carbohydrates [2].
Nut protein sequences for analysis in silico are as follows: Glutelin (44aa, superfamily Glutelin, GenBank accession: AAC69515.1), 11S legumin (505aa, superfamily Globulin, GenBank accession: ABW86979.1), 7S vicilin (784aa, superfamily Globulin, GenBank accession: ABV49593.1), 7S vicilin (792aa, superfamily Globulin, GenBank accession: ABV49592.1), putative allergen I1 (143aa, superfamily Albumin, GenBank accession: AAO32314.1), and putative 7S vicilin (102aa, superfamily Globulin, GenBank accession: AAZ93628.1).
Immunoassays with protein fractions revealed the antibody specificity to the prolamin and glutelin fractions in the respective grains.
[15], it was concluded that the treatment increase the quantity of prolamin in all the treated cake, while the quantity of globulin, albumin and glutelin were reduced.
Although this protein content is lower than in other cereals, such as corn and wheat, rice has a relatively higher content of glutelin, the highest quality protein fraction.
The composite of the substances gliadin and glutelin, gluten is found in grass-related grains.