Wheat Storage Proteins in Transgenic Rice Endosperm

2013 ◽  
Vol 61 (31) ◽  
pp. 7606-7614 ◽  
Author(s):  
Mária Oszvald ◽  
Gábor Balázs ◽  
Sára Pólya ◽  
Sándor Tömösközi ◽  
Rudi Appels ◽  
...  
Keyword(s):  
Transgenic Rice ◽  
Storage Proteins ◽  
Rice Endosperm ◽  
Wheat Storage Proteins

scholarly journals Molecular characterization and phylogenetic analysis of one Omega-gliadin gene from Aegilops speltoidesl

Genetika ◽  
2018 ◽  
Vol 50 (2) ◽  
pp. 503-517 ◽  
Author(s):  
Wanqing Wang ◽  
Ke Wang ◽  
Xi Chen ◽  
Slaven Prodanovic ◽  
Xiaohui Li ◽  
...  
Keyword(s):  
Phylogenetic Analysis ◽  
Quality Improvement ◽  
Related Species ◽  
Storage Proteins ◽  
Aegilops Speltoides ◽  
Amino Acid Residues ◽  
Sequence Characterization ◽  
Specific Pcr ◽  
High Level ◽  
Wheat Storage Proteins

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.

The Industrial Use of EU Wheats

1996 ◽  
Vol 25 (4) ◽  
pp. 243-251
Author(s):  
Jean-Claude Autran
Keyword(s):  
European Union ◽  
Storage Proteins ◽  
Research Programme ◽  
Wheat Breeding ◽  
The European Union ◽  
Processing Industry ◽  
Milling Quality ◽  
Industrial Use ◽  
Sprouting Resistance ◽  
Wheat Storage Proteins

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.

scholarly journals Effects of Cold Jet Atmospheric Pressure Plasma on the Structural Characteristics and Immunoreactivity of Celiac-Toxic Peptides and Wheat Storage Proteins

2020 ◽  
Vol 21 (3) ◽  
pp. 1012
Author(s):  
Fusheng Sun ◽  
Xiaoxue Xie ◽  
Yufan Zhang ◽  
Jiangwei Duan ◽  
Mingyu Ma ◽  
...  
Keyword(s):  
Atmospheric Pressure ◽  
Storage Proteins ◽  
Structural Characteristics ◽  
Atmospheric Pressure Plasma ◽  
High Energy ◽  
Backbone Cleavage ◽  
Excited Atoms ◽  
Wheat Storage Proteins ◽  
Toxic Peptides

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.

scholarly journals Reducing Immunoreactivity of Gliadins and Coeliac-Toxic Peptides Using Peptidases from L. acidophilus 5e2 and A. niger

Catalysts ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 923
Author(s):  
Bartosz Brzozowski ◽  
Katarzyna Stasiewicz ◽  
Mateusz Ostolski ◽  
Marek Adamczak
Keyword(s):  
Lactobacillus Acidophilus ◽  
Storage Proteins ◽  
Prolyl Endopeptidase ◽  
Bread Making ◽  
Initial Value ◽  
Histocompatibility Complex ◽  
Wheat Storage Proteins ◽  
Toxic Peptides ◽  
Hydrolysis Of ◽  
Hla Dq2

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.

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