Transient changes in wheat endosperm polymeric proteins during the later stages of grain development

1995 ◽  
Vol 75 (1) ◽  
pp. 195-198 ◽  
Author(s):  
A. Hussain ◽  
O. M. Lukow
Keyword(s):  
Molecular Weight ◽  
Storage Proteins ◽  
Developmental Changes ◽  
Wheat Cultivars ◽  
Grain Development ◽  
Gluten Proteins ◽  
Distal Half ◽  
End Use ◽  
Qualitative Changes

End-use quality of wheat depends mainly on the composition of the storage proteins. These proteins undergo changes during grain development. This study was carried out to examine modifications in the polymeric protein fraction at different days post anthesis (DPA) and to determine whether these changes are cultivar dependent. Endosperm proteins of three hexaploid wheat cultivars harvested at different stages of maturity and extracted sequentially from distal half kernels showed quantitative and qualitative changes when separated in a 7.5–9.0% gradient polyacrylamide gel system. Sudden qualitative changes were observed at a later stage of seed development (35 DPA) in all tested cultivars. Most qualitative changes occurred in proteins of molecular weight 60–90 kDa and least in proteins above 90 kDa. An intense 60-kDa band appeared in the 35-DPA sample of Columbus; this band faded as the grain approached full maturity (40 DPA). Key words: Developmental changes, electrophoresis, gluten proteins, seed ripening

Molecular detection of high- and low-molecular-weight glutenin subunit genes in common wheat cultivars from 20 countries using allele-specific markers

2011 ◽  
Vol 62 (9) ◽  
pp. 746 ◽  
Author(s):  
H. Jin ◽  
J. Yan ◽  
R. J. Peña ◽  
X. C. Xia ◽  
A. Morgounov ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecylsulfate ◽  
Functional Markers ◽  
Low Molecular Weight ◽  
Wheat Cultivars ◽  
High Frequencies ◽  
Allele Specific ◽  
End Use

The composition and quantity of high- and low-molecular-weight glutenin subunits (HMW-GS and LMW-GS) plays an important role in determining the end-use quality of wheat products. In the present study, 718 wheat cultivars and advanced lines from 20 countries were characterised for the HMW-GS and LMW-GS with allele-specific molecular markers. For the Glu-A1 locus, 311 cultivars (43.3%) had the subunit Ax2*, which predominated in cultivars from Canada (83.3%), Romania (91.7%), Russia (72.2%) and USA (72.2%). At Glu-B1 locus, 197 cultivars (27.4%) contained the By8 subunit and its frequency was higher in Japanese (60.0%) and Romanian (62.5%) genotypes than in those from other countries; 264 cultivars (36.8%) carried the By9 subunit, mostly existing in the cultivars from Austria (100.0%), Russia (72.2%), and Serbia (72.7%); the By16 subunit was present in 44 cultivars (6.1%), with a relatively high percentage in Chile (19.5%), whereas almost no cultivars from other countries had this subunit; the frequency of Bx7OE was 3.1%, and was found only in cultivars from Argentina (12.1%), Australia (4.1%), Canada (25.0%), Iran (20.0%), and Japan (30.0%). There were 446 genotypes (62.1%) with the subunit Dx5 at the Glu-D1 locus; high frequencies of Dx5 occurred in cultivars from Hungary (90.0%), Romania (95.8%), and Ukraine (92.3%). At the Glu-A3 locus, the frequencies of Glu-A3a, b, c, d, e, f and g were 2.9, 6.8, 53.2, 12.8, 7.7, 13.8, and 2.4%, respectively. Glu-A3a was detected only in the cultivars from Bulgaria (13.3%), China (12.2%), Germany (2.7%), Iran (6.7%), Mexico (14.3%), Turkey (4.7%), and USA (5.1%); the high frequencies of superior alleles Glu-A3b and d were found in cultivars from Australia (39.7%) and France (24.5%); Glu-A3c was widely distributed in cultivars from all the countries; the high frequencies of Glu-A3e, f and g were detected in cultivars from Argentina (33.3%), Canada (29.2%), and Hungary (20.0%). At the Glu-B3 locus, Glu-B3a, b, c, d, e, f, g, h and i were present in frequencies of 0.4, 22.3, 0.3, 2.8, 1.9, 3.9, 27.2, 18.8, and 7.1%, respectively. Glu-B3a was detected only in cultivars from Argentina (3.0%) and Ukraine (15.4%) cultivars; high frequencies of Glu-B3b and d were found in the cultivars from Romania (62.5%) and Mexico (14.3%); Glu-B3c was detected only in Romanian (8.3%) genotypes; frequencies of e, f, h and i were high in cultivars from Austria (40.0%), China (14.3%), USA (43.0%), and Argentina (33.3%); Glu-B3g was mostly detected in the cultivars from Germany (69.3%), Norway (77.3%), and Serbia (63.6%). The frequency of the 1B·1R translocation was 13.4%; it occurred in cultivars from all the countries except Australia, Austria, Norway, and Serbia. The functional markers applied in this study, in agreement with the results of sodium-dodecylsulfate–polyacrylamide gel electrophoresis, were accurate and stable, and can be used effectively in wheat quality breeding.

Involvement of a Novel Peptide in the Heat Shock Response of Australian Wheats

1990 ◽  
Vol 17 (4) ◽  
pp. 441 ◽  
Author(s):  
CS Blumenthal ◽  
IL Batey ◽  
CW Wrigley ◽  
EWR Barlow
Keyword(s):  
Heat Shock ◽  
High Performance ◽  
Storage Proteins ◽  
Seed Proteins ◽  
Reversed Phase ◽  
Terminal Sequence ◽  
Chinese Spring Wheat ◽  
End Use ◽  
Peptide Gene

A low molecular weight peptide, induced by exposure of coleoptiles to heat stress at 41°C, has been detected by reversed-phase high performance liquid chromatography of extracts from coleoptiles of five wheat (Triticum aestivum) cultivars. This component is detected within 1 h of a 41°C heat shock, is not detected 48 h after cessation of the heat shock, and remains present during a continuous 24 h heat treatment. The appearance of this component is also induced by exposure of the coleoptile to 0.1 M sodium arsenite or 10% ethanol. When other species such as barley (Hordeum vulgare), soybean (Glycine max), sorghum (Sorghum bicolor), maize (Zea mays), mungbean (Vigna radiata), or rice (Oryza sativa) were examined for the presence of a component eluting in the same position, it was only detected in maize. The amino acid sequence for the heat-induced peptide from wheat was determined to be: V-L-V-P-V-P-Q-L-Q-P-Q-N-Q-P/Q. The sequence of 12 of these amino acids is the same as the N-terminal sequence of α- and β gliadins (wheat endosperm storage proteins). The production of this heat-induced peptide in aneuploids of Chinese spring wheat indicated that the peptide gene was located on the same chromosome arm as one of the gliadin genes. The presence of this gliadin-like peptide in heat-stressed coleoptiles may be due to the presence of five heat shock elements in the gene sequence of gliadins. The potential heat inducibility of the gliadin gene has important implications for end-use quality of wheat. The results also imply that seed proteins may have a function other than storage of nitrogen.

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.

Physicochemical Analysis, Electrophoretic Characterization and Verifica-tion of the Protein Fractions Responsible for Celiac Disease of Wheat Varieties Imported and Grown in Western Algeria

2018 ◽  
Vol 7 (3) ◽  
pp. 113-121
Author(s):  
Remil Asma ◽  
Taghouti Mona ◽  
Benali Mohammed ◽  
Belbraouet Slimane
Keyword(s):  
Celiac Disease ◽  
Bread Wheat ◽  
Protein Quality ◽  
Storage Proteins ◽  
Physicochemical Analysis ◽  
Wheat Varieties ◽  
Gluten Proteins ◽  
Sds Page ◽  
Western Algeria

Celiac disease is an inflammatory enteropathy induced by ingestion of wheat proteins. This study aims to verify the protein quality of wheat varieties that are either grown in or imported into Western Algeria, by carrying out physi-cochemical and electrophoretic characterisations of the gluten proteins. We carry out physicochemical analysis of thirty-four samples of durum and bread wheat, with regard to gluten proteins. The quality of gluten was ap-preciated by Zeleny volume of bread wheat and the SDS sedimentation test for durum wheat. Meanwhile, we also characterized glutenins and gliadins into thirteen cereal varieties by monodimensional electrophoresis on SDS-PAGE and Acid-PAGE respectively. The results showed that gluten levels ranges varied from 26.82±3.99% to 56.1±1.43%. The values of the total pro-tein content had the range of 11.35±0.42% to 20.57±0.98%. The varieties studied had Zeleny values between 7.79±1.45 mL to 40.07±2.96 mL for bread wheat, and the SDS sedimentation volume ranged from 24.5±0.70 mL to 51.25±2.47 mL for durum varieties. The analysis of the glutenin and gliadin composition of the wheat varieties by electrophoresis showed the existence of α- and ω-gliadins subunits, responsible for celiac disease. Furthermore, the results revealed the presence of gliadin subunits "γ-45" and glutenins "GS-LMW Type2" related to the good quality of gluten in some varieties of wheat. As a result, we can conclude that the wheat consumed in Western Algeria has a good quality of storage proteins. Therefore, it is far from being responsible for the decrease of celiac disease in this region.

scholarly journals The relationship between gluten proteins and baking quality

2012 ◽  
pp. 117-122
Author(s):  
Mariann Móré ◽  
Zoltán Győri ◽  
Péter Sipos
Keyword(s):  
Spiral Structure ◽  
Storage Proteins ◽  
Great Part ◽  
Detailed Knowledge ◽  
Gluten Proteins ◽  
Baking Quality ◽  
Wheat Gliadin ◽  
Glutenin Polymer ◽  
The Relationship

Wheat, one of the most important cereals, is grown on the largest area in Hungary. During hydration of storage proteins of wheat – gliadin and glutenin – the gluten complex is evolved. The gliadin is responsible for the extensibility of gluten complex as well as the glutenin for the strength of gluten. The structure, composition and rheological properties of gluten proteins influence significantly the baking quality. The gliadin/glutenin ratio and the quality and structure of glutenin fraction play the most important role in evolving gluten complex. Changes in the steps of breadmaking technology also have effect on the quality of product. Several tests proved that the higher glutenin content increases the strength of dough while the higher gliadin content increases the extensibility of dough and decreases maximum resistance to extension. The monomer gliadins play a great part in plasticity of glutenin polymer. The quality of glutenin fraction significantly influences the evolving gluten complex, because of the spiral structure of glutenin which deforms under stress conditions, then the β-spiral structure resumes their original conformation by releasing from stress.The final quality of product evolves as a result of complex characteristics of wheat proteins, so detailed knowledge on the roles of different protein compounds is the base of the quality oriented product development.

Flour Characteristics and End-Use Quality of Korean Wheats with 1Dx2.2+1Dy12 Subunits in High Molecular Weight Glutenin

2006 ◽  
Vol 11 (3) ◽  
pp. 243-252 ◽  
Author(s):  
Chul-Soo Park ◽  
Byung-Kee Baik ◽  
Moon-Seok Kang ◽  
Jong-Chul Park ◽  
Jae-Gun Park ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
End Use

The high-molecular-weight glutenin subunit composition of Australian wheat cultivars

1986 ◽  
Vol 37 (2) ◽  
pp. 125 ◽  
Author(s):  
GJ Lawrence
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunit ◽  
Subunit Composition ◽  
Wheat Cultivars ◽  
Australian Wheat ◽  
Hmw Glutenin

The seed storage proteins of 106 Australian wheat cultivars were fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis to determine the allelic composition of the cultivars at each of the three loci controlling high-molecular-weight (HMW) glutenin subunits. Amongst the cultivars, three alleles were identified at the Glu-A1 locus, eight at the Glu-B1locus and four at the Glu-D1 locus. The results are presented in the form of a key to aid identification of unknown samples. Sixteen of the cultivars were found to consist of two or more biotypes with respect to HMW glutenin subunit composition.

End-Use Quality of Six Hard Red Spring Wheat Cultivars at Different Irrigation Levels

Crop Science ◽  
2000 ◽  
Vol 40 (3) ◽  
pp. 631-635 ◽  
Author(s):  
Mary J. Guttieri ◽  
Rashid Ahmad ◽  
Jeffrey C. Stark ◽  
Edward Souza
Keyword(s):  
Spring Wheat ◽  
Wheat Cultivars ◽  
Hard Red Spring Wheat ◽  
End Use ◽  
Irrigation Levels
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