scholarly journals Effects of Nitrogen Application in the Wheat Booting Stage on Glutenin Polymerization and Structural–Thermal Properties of Gluten with Variations in HMW-GS at the Glu-D1 Locus

Foods ◽  
2020 ◽  
Vol 9 (3) ◽  
pp. 353
Author(s):  
Lijun Song ◽  
Liqun Li ◽  
Liye Zhao ◽  
Zhenzhen Liu ◽  
Xuejun Li
Keyword(s):  
Thermal Properties ◽  
Wheat Gluten ◽  
Protein Composition ◽  
Grain Filling ◽  
Nitrogen Application ◽  
Glutenin Subunits ◽  
Dough Strength ◽  
Booting Stage ◽  
Α Helix ◽  
Stability Time

Wheat gluten properties can be improved by the application of nitrogen. This study investigates the effects of nitrogen application in the booting stage on glutenin polymerization during grain-filling and structural–thermal properties of gluten based on the high-molecular-weight glutenin subunits (HMW-GSs) using near-isogenic lines (Glu-1Da and Glu-1Dd). The nitrogen rate experiment included rates of 0, 60, 90, and 120 kg N ha−1 applied with three replicates. Nitrogen significantly improved the grain quality traits (wet gluten contents, Zeleny sedimentation values, and maximum resistance) and dough strength (dough development time, dough stability time, and protein weakening), especially in wheat with the Glu-1Da allele. Nitrogen increased the protein composition contents, proportions of glutenins and HMW-GSs, and disulfide bond concentration in the flours of Glu-1Da and Glu-1Dd, and accelerated the polymerization of glutenins (appearing as glutenin macropolymer) during grain-filling, where nitrogen enhanced the accumulation and polymerization of glutenins more for line containing Glu-1Da than Glu-1Dd. The β-sheets, α-helix/β-sheet ratio, microstructures, and thermal stability were also improved to a greater degree by nitrogen for gluten with Glu-1Da compared to Glu-1Dd. Nitrogen treatment was highly effective at improving the gluten structural‒thermal properties of wheat in the booting stage, especially with inferior glutenin subunits.

Functionality-Composition relationships of wheat flour as a result of variation in sulfur availability

1993 ◽  
Vol 44 (8) ◽  
pp. 1767 ◽  
Author(s):  
F MacRitchie ◽  
RB Gupta
Keyword(s):  
Molecular Weight ◽  
Sulfur Content ◽  
Allelic Variation ◽  
Wheat Variety ◽  
Protein Composition ◽  
Sulfur Deficiency ◽  
Glutenin Subunits ◽  
Dough Strength ◽  
Buffer Solution ◽  
Dough Properties

Some recently developed methods for analysing wheat protein composition have been applied to studying the composition/functionality relationships for flours from grain samples of the wheat variety Olympic, grown under differing nitrogen/sulfur fertilizer treatments. In this way, the effects of changing protein composition on functional properties could be followed without the complication of allelic variation. Previous work had established that sulfur deficiency caused an imbalance in dough properties characterized by an increase in dough strength (extensograph maximum resistance, Rmax) and a decrease in extensibility (Ext). In the present study, decreasing flour sulfur content was accompanied by an increase in the ratio of high (HMW) to low (LMW) molecular weight glutenin subunits. As a result, the portion of polymeric proteins (those proteins such as glutenins whose molecules contain multiple polypeptide chains) that is unextractable in SDS-buffer solution (%UPP, a measure of molecular size distribution) also increased with a decrease in sulfur content. A highly significant correlation was found between Rmax and %UPP. In contrast, Rmax showed a high negative correlation with the percentage of polymeric protein in the total protein. Results are generally in agreement with previous studies of wheat samples which varied considerably in genotype but not in environment, thus establishing fundamental relationships between protein composition and dough properties. Extensibility related positively to the percentage of polymeric protein in the flour, but evidence suggested that Ext can be limited by a shift in the molecular weight distribution to too high molecular weight. Reduction in the percentage of polymeric protein in flour (and Ext) as a result of sulfur deficiency was due to a decrease in LMW glutenin subunits which are normally present in greater amounts than the HMW subunits. Dependence of dough mixing and baking performance parameters on protein composition is also reported.

Changes in protein composition during grain development in wheat

2001 ◽  
Vol 52 (4) ◽  
pp. 485 ◽  
Author(s):  
J. F. Panozzo ◽  
H. A. Eagles ◽  
M. Wootton
Keyword(s):  
Molecular Weight ◽  
Maximum Rate ◽  
Average Molecular Weight ◽  
Protein Composition ◽  
Grain Filling ◽  
Triticum Aestivum L ◽  
Logistic Function ◽  
Low Molecular Weight ◽  
Grain Development ◽  
Glutenin Subunits

Changes in glutenin, gliadin, glutenin subunit composition, and polymer size distribution were monitored for 4 cultivars of wheat (Triticum aestivum L.) throughout grain filling in an irrigated and non-irrigated environment over 2 seasons. The synthesis of glutenin and gliadin was modelled using a logistic function to determine the rate and duration of synthesis in response to environmental conditions. The maximum rate of synthesis of glutenin occurred approximately 6–8 days after the maximum rate of gliadins, with the duration extended by a similar period. High molecular weight glutenin subunits (HMWGS) were detected earlier than low molecular weight glutenin subunits (LMWGS). After the initial synthesis of HMWGS, there was a period at approximately mid grain filling when the rate of synthesis was reduced, followed by a period of more rapid synthesis in the latter stages of grain filling. In contrast, once detected, LMWGS increased at a faster rate than, and were in excess with respect to, HMWGS. Cultivar and environmental differences were observed, but in all cases the average molecular weight of polymeric glutenin increased throughout grain filling. Large polymers (>400 kD) increased continuously during grain filling, whereas polymers in the range 150–400 kD remained relatively constant and smaller polymers <150 kD decreased. As grain filling approached physiological maturity, there was a rapid increase in the synthesis of large polymers. The gliadin to glutenin ratio was almost the same in grain from adjacent irrigated and non-irrigated environments subjected to high temperatures at mid grain f illing, but the proportion of highly polymeric glutenin was greater from the non-irrigated environment.

Biochemical and genetic characterisation of a D glutenin subunit encoded at the Glu-B3 locus

Genome ◽  
1998 ◽  
Vol 41 (2) ◽  
pp. 215-220 ◽  
Author(s):  
M T Nieto-Taladriz ◽  
M Rodríguez-Quijano ◽  
J M Carrillo
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Wheat Gluten ◽  
Gene Clusters ◽  
Glutenin Subunits ◽  
Key Words Wheat ◽  
Sds Page ◽  
A Subunit ◽  
Omega Gliadins ◽  
Prolamin Loci

The SDS-PAGE pattern of reduced and alkylated glutenins from the bread wheat cultivar Prinqual presents a subunit (named d4) in the mobility zone of the omega -gliadins that only appears under reduced conditions. This subunit was isolated and characterised at the biochemical and genetic levels. Subunit d4 was shown to form disulphide aggregates with glutenins and had an acidic pI. These characteristics correspond to those of the D glutenin subunits. The N-terminal amino acid sequence of subunit d4 was coincident with the SRL sequence type characteristic of omega -gliadins encoded by genes on the 1B chromosome, and confirms the similarity between D glutenin subunits and omega -gliadins. The genetic study of subunit d4 was performed in the F2 progeny from the 'Prinqual' x 'Ablaca' cross, based on four prolamin loci: Glu-B1, Glu-B3, Gli-B1, and Gli-B5. The recombinants found between Glu-B3 and Gli-B1 demonstrated that subunit d4 was encoded at the Glu-B3 locus, and reinforces the hypothesis of the duplication of prolamin gene clusters in wheat. A preliminary study of the effect of subunit d4 on gluten strength showed that lines with the Glu-B3 allele from 'Prinqual', which includes subunit d4, had a significantly higher sedimentation volume than those with the allele from 'Ablaca'.Key words: wheat gluten proteins, D glutenin subunits, amino acid sequence, linkage mapping, complex loci duplication.

Soil nitrogen dynamics as affected by landscape position and nitrogen fertilizer

2005 ◽  
Vol 85 (5) ◽  
pp. 579-587 ◽  
Author(s):  
Y. K. Soon ◽  
S. S. Malhi
Keyword(s):  
N Mineralization ◽  
N Uptake ◽  
Grain Filling ◽  
Landscape Position ◽  
Slope Position ◽  
Organic N ◽  
Net N Mineralization ◽  
Nitrogen Application ◽  
N Application ◽  
Upper Slope

The influence o f landscape position on the dynamics of N in the soil-plant system has not been adequately studied. Our aim with this study on a predominantly Black Chernozem soil was to evaluate the effect of slope position (upper vs. lower) and N fertilizer application (none vs. 60 kg N ha-1) on soil and wheat (Triticum aestivum L.) N through the growing season. Landscape position had a dominant effect on soil NO3− and soluble organic N (SON) concentrations, especially in the surface 15 cm. These pools of soil N and net N mineralization were greater at the lower than at the upper slope position. The landscape effect is attributed to higher organic matter content (as measured by organic C) and water availability in lower compared with upper slope positions. Nitrogen application had no measurable effect on soil NO3− and SON concentrations. Exchangeable and non-exchangeable NH4+ were little affected by slope position or N fertilization. Nitrogen application increased wheat N uptake; however, its influence was less than that of slope position, especially on N accumulation in wheat heads during grain-filling. Although N application increased wheat yields, landscape position exerted the greater influence: grain yield was less on upper than lower slope positions due to earlier onset of crop maturity. During grain filling, net N mineralization was suppressed at the upper slope position and by N application. The increase in crop yield and N uptake due to N application was not significantly different between slope positions. This study demonstrated that landscape position had a greater influence on N dynamics and availability than the application of typical amounts of fertilizer N and that the two effects were mostly independent of each other. Key words: Available N, landscape position, N uptake, net N mineralization, soluble organic N

Protein expression characteristics and their response to nitrogen application during grain-filling stage of rice (Oryza Sativa.L)

2012 ◽  
Vol 32 (10) ◽  
pp. 3209-3224
Author(s):  
张志兴 ZHANG Zhixing ◽  
陈军 CHENG Jun ◽  
李忠 LI Zhong ◽  
李兆伟 LI Zhaowei ◽  
黄锦文 HUANG Jinwen ◽  
...  
Keyword(s):  
Protein Expression ◽  
Grain Filling ◽  
Nitrogen Application ◽  
Filling Stage ◽  
Expression Characteristics ◽  
Grain Filling Stage

scholarly journals Remobilization of dry matter in wheat: effects of nitrogen application and post-anthesis water deficit during grain filling

2011 ◽  
Vol 39 (4) ◽  
pp. 279-293 ◽  
Author(s):  
A Bahrani ◽  
H Heidari Sharif Abad ◽  
Z Tahmasebi Sarvestani ◽  
GH Moafpourian ◽  
A Ayneh Band
Keyword(s):  
Water Deficit ◽  
Dry Matter ◽  
Grain Filling ◽  
Nitrogen Application

Some Optical Properties of S-β-(4-Pyridylethyl)-L-Cysteine and its Wheat Gluten and Serum Albumin Derivatives

1971 ◽  
Vol 49 (9) ◽  
pp. 1042-1049 ◽  
Author(s):  
Y. Victor Wu ◽  
James E. Cluskey ◽  
L. H. Krull ◽  
Mendel Friedman
Keyword(s):  
Optical Properties ◽  
Ionic Strength ◽  
Serum Albumin ◽  
Disulfide Bonds ◽  
Wheat Gluten ◽  
Spectrophotometric Titration ◽  
Optical Rotatory ◽  
Pyridyl Group ◽  
Helical Content ◽  
Α Helix

The optical properties of S-β-(4-pyridylethyl)-L-cysteine (PEC) and its bovine serum albumin (BSA) and wheat gluten derivatives were studied in 0.01–0.1 N HCl. Optical rotatory dispersions (O.R.D.), circular dichroism (C.D.), ultraviolet (U.V.), and infrared (I.R.) spectra were obtained of PEC, BSA, BSA reduced with mercaptoethanol and alkylated with 4-vinylpyridine (PE-BSA), BSA reduced with mercaptoethanol and alkylated with acrylonitrile (CN-BSA), gluten, gluten reduced with mercaptoethanol and alkylated with 4-vinylpyridine (PE-gluten), and gluten reduced with mercaptoethanol and alkylated with acrylonitrile (CN-gluten). I.R. spectra of the proteins showed the presence of α-helical and unordered conformations. The U.V. absorption at 254 mμ of PEC and PE-BSA depends on pH; a pK value near 6 for the pyridyl group was obtained by spectrophotometric titration. The possible use of PEC as a conformation probe was explored. The O.R.D. of PEC depends on concentration, solvent, and pH but not on ionic strength. The O.R.D. data of proteins were analyzed by the Moffitt–Yang method to get α-helical contents. These helical contents indicate that there is not enough interaction left to support α-helix in gluten with disulfide bonds broken at pH 2.2. However, approximately one-third of the helical content of BSA persists without the aid of disulfide bonds.

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