Genetics of Wheat Storage Proteins and the Effect of Allelic Variation on Bread-Making Quality

1987 ◽  
Vol 38 (1) ◽  
pp. 141-153 ◽  
Author(s):  
P I Payne
Catalysts ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 923
Author(s):  
Bartosz Brzozowski ◽  
Katarzyna Stasiewicz ◽  
Mateusz Ostolski ◽  
Marek Adamczak

Wheat storage proteins and products of their hydrolysis may cause coeliac sprue in genetically predisposed individuals with high expression of main histocompatibility complex HLA-DQ2 or DQ8, since by consuming wheat, they become exposed to proline- (P) and glutamine (Q)-rich gluten. In bread-making, the hydrolysis of gliadins and coeliac-toxic peptides occurs with varied efficiency depending on the fermentation pH and temperature. Degradation of gliadins catalysed by Lactobacillus acidophilus 5e2 peptidases and a commercial prolyl endopeptidase synthesised by A. niger, carried out at pH 4.0 and 37 °C, reduces the gliadin concentration over 110-fold and decreases the relative immunoreactivity of the hydrolysate to 0.9% of its initial value. Hydrolysis of coeliac-toxic peptides: LGQQQPFPPQQPY (P1) and PQPQLPYPQPQLP (P2) under the same conditions occurs with the highest efficiency, reaching 99.8 ± 0.0% and 97.5 ± 0.1%, respectively. The relative immunoreactivity of peptides P1 and P2 was 0.8 ± 0.0% and 3.2 ± 0.0%, respectively. A mixture of peptidases from L. acidophilus 5e2 and A. niger may be used in wheat sourdough fermentation to reduce the time needed for degradation of proteins and products of their hydrolysis.


The genes that code for endosperm storage proteins occur at nine complex loci on six different chromosomes. Glu-A1 , Glu-B1 and Glu-D1 contain the genes for high molecular mass subunits of glutenin and are close to the centromere on the long arms of chromosomes 1A, 1B and 1D respectively. On the short arms of the same chromosomes, but distant from the centromere, are Gli-A1 , Gli-B1 and Gli-D1 . Each of these loci carry three major gene families coding for ω-gliadins, γ-gliadins and low molecular mass glutenin subunits. The remaining loci, Gli-A2 , Gli-B2 and Gli-D2 occur near the ends of the short arms of chromosomes 6A, 6B and 6D respectively and each code for α- and β-gliadins. Recombination of genes within a locus is very rare and has so far been detected only at Glu-B1 , at the rate of about one recombinant in 1000 progeny. Each locus displays allelic variation and this is responsible for differences among varieties in protein quality for making bread. The protein variants that are associated with good quality are being identified, firstly by analysing segregating populations and secondly from the development of near-isogenic lines. Current, incomplete, information on the relative qualities of different alleles at each locus indicates the following order of im portance: Glu-1 > Gli-1 > Gli-2 . Landraces of primitive agriculture are being screened for novel proteins. The genes for some of them are being incorporated into the genomes of commercial wheats.


Genome ◽  
2002 ◽  
Vol 45 (4) ◽  
pp. 661-669 ◽  
Author(s):  
Ali Masoudi-Nejad ◽  
Shuhei Nasuda ◽  
Akira Kawabe ◽  
Takashi R Endo

Gliadins are the most abundant component of the seed storage proteins in cereals and, in combination with glutenins, are important for the bread-making quality of wheat. They are divided into four subfamilies, the α-, β-, γ-, and ω-gliadins, depending on their electrophoresis pattern, chromosomal location, and DNA and protein structures. Using a PCR-based strategy we isolated and sequenced an ω-gliadin sequence. We also determined the chromosomal subarm location of this sequence using wheat aneuploids and deletion lines. The gene is 1858 bp long and contains a coding sequence 1248 bp in length. Like all other gliadin gene families characterized in cereals, the ω-gliadin gene described here had characteristic features including two repeated sequences 300 bp upstream of the start codon. At the DNA level, the gene had a high degree of similarity to the ω-secalin and C-hordein genes of rye and barley, but exhibited much less homology to the α- and β-gliadin gene families. In terms of the deduced amino acid sequence, this gene has about 80 and 70% similarity to the ω-secalin and C-hordein genes, respectively, and possesses all the features reported for other gliadin gene families. The ω-gliadin gene has about 30 repeats of the core consensus sequences PQQPX and XQQPQQX, twice as many as other gliadin gene families. Southern blotting and PCR analysis with aneuploid and deletion lines for the short arm of chromosome 1A showed that the ω-gliadin was located on the distal 25% of the short arm of chromosome 1A. By comparison of PCR and A-PAGE profiles for deletion stocks, its genomic location must be at a different locus from gli-A1a in 'Chinese Spring'.Key words: glutenin, omega gliadin, storage protein, Triticum aestivum, secalin.


Genetika ◽  
2018 ◽  
Vol 50 (2) ◽  
pp. 503-517 ◽  
Author(s):  
Wanqing Wang ◽  
Ke Wang ◽  
Xi Chen ◽  
Slaven Prodanovic ◽  
Xiaohui Li ◽  
...  

Gliadins, as the major components of wheat storage proteins, determine the extensibility properties of dough and have important effects on flour processing quality. Wheat related species carries potential storage protein gene resources for quality improvement. In this study, we isolated and characterized the first complete ?-gliadin gene Omega-AS from Aegilops speltoides L. (2n = 2x = 14, SS) by allelic-specific PCR and investigated its phylogenetic relationships among Triticum and Aegilopsspecies. Molecular structure showed that Omega-AS gene consisted of 1122 bp encoding 373 amino acid residues with deduced molecular mass 41379.21 Da. Omega-AS gene was exceptionally rich in prolines and glutamines with fewer methionine and no cysteine. Sequence characterization and epitope analysis showed that three epitopes QQPIPVQPQQ, TQPQQPTPIQ and IQPQQPFPQQ were absent in Omega-AS gene encoded protein, indicating its potential value for wheat quality improvement with less toxic, or no toxic peptides. Phylogenetic analysis revealed that Omega-AS was closely related to gliadin genes of wheat and related species and its divergence from bread wheat was more recently (less than 1.243 MYA). Heterologous expression showed that Omega-AS gene could successfully express with a high level in E. coli under the control of T7promoter. The transcription expression pattern of Omega-AS gene during grain development detected by qRT-PCR revealed that the highest expression level occurred at 17 days post an thesis.


1996 ◽  
Vol 25 (4) ◽  
pp. 243-251
Author(s):  
Jean-Claude Autran

A four-year coordinated wheat research programme was recently conducted with the aim of advancing understanding of wheat processing and quality under the specific conditions of the European Union. The main areas examined included milling quality, starch/gluten separation, the basis of breadmaking quality, the basis of biscuit quality, flour composition, dough development, the genetics of wheat storage proteins and sprouting resistance. The programme produced a range of results which will contribute to developments In the processing industry, wheat breeding and trade.


2020 ◽  
Vol 21 (3) ◽  
pp. 1012
Author(s):  
Fusheng Sun ◽  
Xiaoxue Xie ◽  
Yufan Zhang ◽  
Jiangwei Duan ◽  
Mingyu Ma ◽  
...  

The present research reported the effects of structural properties and immunoreactivity of celiac-toxic peptides and wheat storage proteins modified by cold jet atmospheric pressure (CJAP) plasma. It could generate numerous high-energy excited atoms, photons, electrons, and reactive oxygen and nitrogen species, including O3, H2O2, •OH, NO2− and NO3− etc., to modify two model peptides and wheat storage proteins. The Orbitrap HR-LC-MS/MS was utilized to identify and quantify CJAP plasma-modified model peptide products. Backbone cleavage of QQPFP and PQPQLPY at specific proline and glutamine residues, accompanied by hydroxylation at the aromatic ring of phenylalanine and tyrosine residues, contributed to the reduction and modification of celiac-toxic peptides. Apart from fragmentation, oxidation, and agglomeration states were evaluated, including carbonyl formation and the decline of γ-gliadin. The immunoreactivity of gliadin extract declined over time, demonstrating a significant decrease by 51.95% after 60 min of CJAP plasma treatment in vitro. The CJAP plasma could initiate depolymerization of gluten polymer, thereby reducing the amounts of large-sized polymers. In conclusion, CJAP plasma could be employed as a potential technique in the modification and reduction of celiac-toxic peptides and wheat storage proteins.


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