Influence of High Molecular Weight (HMW) and Low Molecular Weight (LMW) Glutenin Subunits Controlled byGlu-1andGlu-3Loci on Durum Wheat Quality

2001 ◽  
Vol 78 (1) ◽  
pp. 59-63 ◽  
Author(s):  
C. Brites ◽  
J. M. Carrillo
Keyword(s):  
Molecular Weight ◽  
Durum Wheat ◽  
High Molecular Weight ◽  
Low Molecular Weight ◽  
Wheat Quality ◽  
Glutenin Subunits ◽  
Lmw Glutenin Subunits

scholarly journals Genetic diversity of high and low molecular weight glutenin subunits in Saharan bread and durum wheats from Algerian oases

2012 ◽  
Vol 48 (No. 1) ◽  
pp. 23-32 ◽  
Author(s):  
I. Bellil ◽  
M. Chekara Bouziani ◽  
D. Khelifi
Keyword(s):  
Genetic Diversity ◽  
Molecular Weight ◽  
Durum Wheat ◽  
Bread Wheat ◽  
Allelic Variation ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Lmw Glutenin Subunits ◽  
Genotypic Identification ◽  
Diversity Studies

Saharan wheats have been studied particularly from a botanical viewpoint. Genotypic identification, classification and genetic diversity studies to date were essentially based on the morphology of the spike and grain. For this, the allelic variation at the glutenin loci was studied in a set of Saharan bread and durum wheats from Algerian oases where this crop has been traditionally cultivated. The high molecular weight and low molecular weight glutenin subunit composition of 40 Saharan bread and 30 durum wheats was determined by SDS-PAGE. In Saharan bread wheats 32 alleles at the six glutenin loci were detected, which in combination resulted in 36 different patterns including 17 for HMW and 23 for LMW glutenin subunits. For the Saharan durum wheats, 29 different alleles were identified for the five glutenin loci studied. Altogether, 29 glutenin patterns were detected, including 13 for HMW-GS and 20 for LMW-GS. Three new alleles were found in Saharan wheats, two in durum wheat at the Glu-B1 and Glu-B3 loci, and one in bread wheat at the Glu-B1 locus. The mean indices of genetic variation at the six loci in bread wheat and at the five loci in durum wheat were 0.59 and 0.63, respectively, showing that Saharan wheats were more diverse. This information could be useful to select Saharan varieties with improved quality and also as a source of genes to develop new lines when breeding for quality.

Composition of and variation in high- and low-molecular weight glutenin subunits, and omega gliadins in Ethiopian tetraploid wheat germplasm

2006 ◽  
Vol 4 (2) ◽  
pp. 134-143 ◽  
Author(s):  
Faris Hailu ◽  
Eva Johansson ◽  
Arnulf Merker ◽  
Getachew Belay ◽  
Harjit-Singh ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Tetraploid Wheat ◽  
Glutenin Subunit ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Hmw Glutenin Subunits ◽  
Lmw Glutenin Subunits ◽  
Hmw Glutenin ◽  
Omega Gliadins ◽  
High Degree

A collection of 120 Ethiopian tetraploid wheat accessions was analysed for high-molecular weight (HMW) glutenin subunit, low-molecular weight (LMW) glutenin subunit and omega gliadin composition by SDS–PAGE. For the HMW glutenin subunits, a new allelic variant, 2****, was detected which has not been previously described at the Glu-A1 locus. A high proportion of Glu-A1x banding pattern was observed in durum wheat. For the Glu-B1 locus four different banding patterns were detected. Among those HMW glutenin subunits, 7+8 were the most common, while subunits 14+15 and 6+8 were found to be rare. A high degree of variation was evident for the LMW glutenin subunits and D-zone omega gliadins. The association of the composition of the gluten with quality has been discussed. This wide variation can be used in improving the quality of wheat and to widen its genetic base.

Simultaneous Isolation of Wheat High Molecular Weight and Low Molecular Weight Glutenin Subunits

1998 ◽  
Vol 28 (1) ◽  
pp. 25-32 ◽  
Author(s):  
I.M. Verbruggen ◽  
W.S. Veraverbeke ◽  
A. Vandamme ◽  
J.A. Delcour
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Low Molecular Weight ◽  
Glutenin Subunits

scholarly journals Evaluation of winter wheat collection in terms of HMW- and LMW-glutenin subunits

2010 ◽  
Vol 46 (Special Issue) ◽  
pp. S96-S99 ◽  
Author(s):  
J. Bradová ◽  
L. Štočková
Keyword(s):  
Molecular Weight ◽  
Winter Wheat ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Bread Making ◽  
Wheat Varieties ◽  
Lmw Glutenin Subunits ◽  
Winter Wheat Varieties

The composition of high molecular weight (HMW-GS) and low molecular weight (LMW-GS) glutenin subunits was examined in a collection of 86 Czech registered winter wheat varieties. These proteins were analyzed by sodium dodecyl sulphate polyacrylamide gel electrophoresis. An inter-varietal polymorphism of the HMW and LMW glutenin subunits was detected. Twenty-one different patterns for HMW were identified, and eighteen for the LMW-glutenins. The different alleles encoded at the six glutenin loci were determined. Three, six, and four alleles were observed, respectively at the <I>Glu-A1, Glu-</I>B1, and <I>Glu-D1 </I>loci (encoding high HMW-GS). Three, eight, and three alleles of LMW-GS were found, respectively, at the <I>Glu-A3, Glu- B3</I>, and <I>Glu-D3 </I>loci. The evaluated varieties were split into four categories of baking quality, and these variety groups were analyzed for the presence of different HMW-GS and LMW-GS alleles. While the alleles <I>Glu-B1c </I>(7+9), and <I>Glu-D1d </I>(5+10) were detected exclusively in bread wheat varieties, the alleles <I>Glu-B1d </I>(6+8), <I>Glu-D1a </I>(2+12), and <I>Glu-A3e/f </I>only occurred in those varieties that are not suitable for bread-making. &nbsp;

Development of 1AS.1AL-1DL durum wheat chromosome carrying Glu-D1a locus encoding high molecular weight glutenin subunits 2 + 12

2019 ◽  
Vol 39 (3) ◽  
Author(s):  
Olivier Coriton ◽  
Annie Faye ◽  
Etienne Paux ◽  
Jocelyne Lemoine ◽  
Virginie Huteau ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Durum Wheat ◽  
High Molecular Weight ◽  
Wheat Chromosome ◽  
Glutenin Subunits

Isolation of Wheat High Molecular Weight Glutenin Subunits from Durum Wheat

2000 ◽  
Vol 77 (2) ◽  
pp. 105-106 ◽  
Author(s):  
Antonella Capocchi ◽  
Luciano Galleschi ◽  
Franco Saviozzi
Keyword(s):  
Molecular Weight ◽  
Durum Wheat ◽  
High Molecular Weight ◽  
Glutenin Subunits

scholarly journals The composition of gluten proteins and their effect on the rheological properties of gluten

2006 ◽  
pp. 124-129
Author(s):  
Csilla Uri ◽  
Árpád Tóth ◽  
Péter Sipos ◽  
Mária Borbélyné Varga ◽  
Zoltán Győri
Keyword(s):  
Molecular Weight ◽  
Rheological Properties ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Wheat Varieties ◽  
Gluten Proteins ◽  
Two Factors ◽  
Protein Components

Wheat is the major cereal component of bread in the world and is grown worldwide. Of the cereals only the bread wheats – and less the triticale – includes storage proteins that play an important role in the performance of gluten. Proteins of gluten complex may be present in two classes:− low molecular weight (gliadin-) components, and− high molecular weight (glutenin-) components.Gliadins shown appreciable heterogenity and can be separated into 40-50 components with gel electrophoresis. The composition of gliadins is employable for the identification the wheat varieties and to investigate the varieties. In the decreasing electrophoretic mobility sequence may be distinguish α-, β-, γ- and ω-gliadins. A glutenin subunits may be include in two classes:− high molecular weight glutenin subunits (HMW-GS),− low molecular weight glutenin subunits (LMW-GS).Wheat varieties can be identified by glutenin and their quality selection is also possible. The gliadin’s polypeptides encoding genes are located on the short arm of chromosomes 1A, 1B and 1D, 6A, 6B and 6D. Genetic coding for HMW subunits is located on the long arms of chromosomes 1A, 1B and 1D, the LMW-GS are also located on chromosomes 1A, 1B and 1D (Glu-3 loci) near the gliadin-coding loci.Storage proteins affect the rheological properties of gluten by two factors:1. The quality and quantity of the protein components of the gluten complex,2. The interactions between the protein fractions.

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