The accumulation of high molecular weight glutenin subunits (HMW-GS) and their relation to dough rheological quality in Chinese winter wheat

2006 ◽  
Vol 57 (1) ◽  
pp. 41 ◽  
Author(s):  
Zhiying Deng ◽  
Jichun Tian ◽  
Ruibo Hu

Six winter wheat cultivars were categorised into high gluten, medium gluten, and low gluten according to their protein content and gluten index. The object of this study was to determine the accumulation of high molecular weight glutenin subunits (HMW-GS) and their relationship to dough rheological quality. They were grown in 3 replicates on experimental plots at the Shandong Agricultural University research farm in 2001. HMW-GS compositions during grain development were investigated by SDS-PAGE procedures, followed by imaging densitometry to determine quantitative variations. Initial formation time of HMW-GS was different among cultivars. HMW-GS in cultivars with high gluten had formed completely by 10 days after anthesis, but were still only partially formed at this time in cultivars having weak gluten. Accumulation quantities of HMW-GS followed with grain development. Individual HMW-GS accumulated rapidly between 25 days after anthesis and maturity. The kinetic accumulation trend for the individual HMW-GS was similar in the same type of cultivars, but quantities were different. Strong cultivars had more kinetic accumulation quantities of HMW-GS than weak cultivars. HMW-GS kinetic accumulation quantities during grain development were significantly positively correlated with dough rheological characteristics and SDS-sedimentation volume.

Agronomy ◽  
2019 ◽  
Vol 9 (11) ◽  
pp. 755 ◽  
Author(s):  
Alvarez ◽  
Guzmán

Club wheat (Triticum aestivum L. ssp. compactum (Host) Mackey), macha wheat (T. aestivum L. ssp. macha (Dekapr. & A.M. Menabde) Mackey) and Indian dwarf wheat (T. aestivum L. ssp. sphaerococcum (Percival) Mackey) are three neglected or underutilized subspecies of hexaploid wheat. These materials were and are used to elaborate modern and traditional products, and they could be useful in the revival of traditional foods. Gluten proteins are the main grain components defining end-use quality. The high molecular weight glutenin subunit compositions of 55 accessions of club wheat, 29 accessions of macha wheat, and 26 accessions of Indian dwarf wheat were analyzed using SDS-PAGE. Three alleles for the Glu-A1 locus, 15 for Glu-B1 (four not previously described), and four for Glu-D1 were detected. Their polymorphisms could be a source of genes for quality improvement in common wheat, which would permit both their recovery as new crops and development of modern cultivars with similar quality characteristics but better agronomic traits.


2017 ◽  
Vol 94 (3) ◽  
pp. 508-512 ◽  
Author(s):  
Kimtoan Hoang ◽  
Xiangnan Li ◽  
Yun Bo ◽  
Qin Zhou ◽  
Jian Cai ◽  
...  

Genome ◽  
2006 ◽  
Vol 49 (2) ◽  
pp. 181-189 ◽  
Author(s):  
H Q Wang ◽  
X Y Zhang

High-molecular-weight glutenin subunits (HMW-GSs) play an important role in the breadmaking quality of wheat flour. In China, cultivars such as Triticum aestivum 'Xiaoyan No. 6' carrying the 1Bx14 and 1By15 glutenin subunits usually have attributes that result in high-quality bread and noodles. HMW-GS 1Bx14 and 1By15 were isolated by preparative sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and used as an antigen to immunize BALB/c mice. A resulting monoclonal antibody belonging to the IgG1 subclass was shown to bind to all HMW-GSs of Triticum aestivum cultivars, but did not bind to other storage proteins of wheat seeds in a Western blot analysis. After screening a complementary DNA expression library from immature seeds of 'Xiaoyan No. 6' using the monoclonal antibody, the HMW-GS 1By15 gene was isolated and fully sequenced. The deduced amino acid sequence showed an extra stretch of 15 amino acid repeats consisting of a hexapeptide and a nonapeptide in the repetitive domain of this y-type HMW subunit. Bacterial expression of a modified 1By15 gene, in which the coding sequence for the signal peptide was removed and a BamHI site eliminated, gave rise to a protein with mobility identical to that of HMW-GSs extracted from seeds of 'Xiaoyan No. 6' via SDS-PAGE. This approach for isolating genes using specific monoclonal antibody against HMW-GS genes is a good alternative to the extensively used polymerase chain reaction (PCR) technology based on sequence homology of HMW-GSs in wheat and its relatives.Key words: wheat, HMW-GS, monoclonal antibody, immunoscreen.


1989 ◽  
Vol 263 (3) ◽  
pp. 837-842 ◽  
Author(s):  
A P Goldsbrough ◽  
N J Bulleid ◽  
R B Freedman ◽  
R B Flavell

‘High-molecular-weight’ (HMW, high-Mr) glutenin subunits are protein constituents of wheat (Triticum aestivum) seeds and are responsible in part for the viscoelasticity of the dough used to make bread. Two subunits, numbered 10 and 12, are the products of allelic genes. Their amino acid sequences have been derived from the nucleic acid sequences of the respective genes. Subunit 10 has fewer amino acids than subunit 12, but migrates more slowly on SDS/PAGE (polyacrylamide-gel electrophoresis). This anomaly is due to between one and six of the amino acid differences between the subunits, localized towards the C-terminal end of the proteins. This has been established by making chimaeric genes between the genes for subunits 10 and 12, transcribing and translating them in vitro and analysing the products by SDS/PAGE. The postulated conformational differences between subunits 10 and 12 are discussed in relation to current hypotheses for the structure of HMW glutenin subunits.


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