Influence of different nitrogen application on flour properties, gluten properties by HPLC and end-use quality of Korean wheat

Cho, Seong-Woo; Chen, Kang; Kang, Tak; Cho, Kwang-Min; Park, Chul Soo

doi:10.1016/s2095-3119(18)61920-3

Cited by 15 publications

(12 citation statements)

References 29 publications

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“…In the current study, a significant cultivar effect was found in the case of 1Dy12, 1Dx2, 1Bx7, and 1Ax1. HMW-GS composition was found to be genetically determined (Johansson, Henriksson, Svensson, & Heneen, 1993;Payne, Nightingale, Krattiger, & Holt, 1987), but the concentration of subunits is largely determined by environmental factors such as N in the soil (Cho, Kang, Kang, Cho, & Park, 2018;Graybosch, Peterson, Shelton, & Baenziger, 1996). A significant treatment effect was evident for 1Ax1, 1Dy12, and 1By8 in the current study.…”

Section: Resultsmentioning

confidence: 43%

“…Liu et al (2016) concluded that dough strength and baking performance of wheat cultivars are related to allelic variation in HMW-GS. HMW-GS composition was found to be genetically determined (Johansson, Henriksson, Svensson, & Heneen, 1993;Payne, Nightingale, Krattiger, & Holt, 1987), but the concentration of subunits is largely determined by environmental T A B L E 3 Peak percentage areas of high molecular weight glutenin subunits 1Ax1, 1Bx7, 1By8, 1Dx2, and 1Dy12 in SST806 at different nitrogen and phosphorus treatments factors such as N in the soil (Cho, Kang, Kang, Cho, & Park, 2018;Graybosch, Peterson, Shelton, & Baenziger, 1996). Sabine, Oberfoster, Werteker, Grausgruber, and Lelly (1997) reported that the Glu-B1 alleles 7 + 9 and the Glu-D1 alleles 5 + 10 occurred more frequently in cultivars with better bread-making quality, and no cultivar with good quality contained subunits 6 + 8 and 2 + 12.…”

Section: Resultsmentioning

confidence: 99%

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Effects of different fertilization levels on the concentration of high molecular weight glutenin subunits of two spring, hard red bread wheat cultivars

et al. 2019

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Backgrounds and objectives:High molecular weight gluten subunits (HMW-GS) are generally considered to play a key role in gluten formation and structure and are closely related to wheat quality. In this study, two spring wheat cultivars (PAN3497 and SST806) with the same HMW-GS composition (1Ax1, 1Bx7, 1By8, 1Dx2, and 1Dy12) were tested in the greenhouse, over 2 years, in order to determine how different genetic backgrounds, and low-nitrogen and low-phosphorus treatments, influenced the expression and quantity of the HMW-GS, as measured by reverse-phase high-performance liquid chromatography (RP-HPLC). Findings: Cultivar effect was highly significant for all HMW-GS, except for 1By8.A large treatment effect was found on subunits 1Ax1, 1Dy12, and 1By8. Cultivar-bytreatment interaction was highly significant and contributed to variation of subunit 1Dx2. Subunits 1Dy12 and 1By8 were highly influenced by low-N conditions. Ratio of HMW-GS x type/y type was higher for PAN3497 than for SST806. Furthermore, a strong treatment effect was observed for the ratio of x type/y type, which was 45% higher in PAN3497 under optimal and low-N conditions, compared to SST806. Conclusions: This study showed that fertilization level had a considerable effect on HMW-GS composition and on FPC, with low-N conditions having the largest influence, followed by a combination of low N and low P. Significance and novelty: The results highlighted the importance of the y-type subunits in the bread wheat quality breeding programs, especially under low-N and low-P growing conditions. K E Y W O R D Sabiotic stress, glutenin subunits, nutrient deficiency, wheat quality

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Section: Resultsmentioning

confidence: 43%

Section: Resultsmentioning

confidence: 99%

Effects of different fertilization levels on the concentration of high molecular weight glutenin subunits of two spring, hard red bread wheat cultivars

et al. 2019

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“…Gliadins of wasko.gl+ and wasko.glwere separated based on hydrophobicity differences between ω (lowest hydrophobicity), α/β (medium hydrophobicity), and γ (highest hydrophobicity) fractions [ 41 , 43 , 44 , 45 ]. Figure 2 presents a reverse-phase chromatogram of the gliadin fraction from kernels of both lines.…”

Section: Resultsmentioning

confidence: 99%

FT-Raman Spectroscopy as a Tool to Study the Secondary Structures of Wheat Gliadin Proteins

et al. 2021

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Raman spectroscopy is a useful method in biological, biomedical, food, and agricultural studies, allowing the simultaneous examination of various chemical compounds and evaluation of molecular changes occurring in tested objects. The purpose of our research was to explain how the elimination of ω-fractions from the wheat gliadin complex influences the secondary structures of the remaining αβγ-gliadins. To this aim, we analyzed the endosperm of wheat kernels as well as gliadin proteins extracted from two winter wheat genotypes: wasko.gl+ (control genotype containing the full set of gliadins) and wasko.gl− (modified genotype lacking all ω-gliadins). Based on the decomposition of the amide I band, we observed a moderate increase in β-forms (sheets and turns) at the expense of α-helical and random coil structures for gliadins isolated from the flour of the wasko.gl− line. Since ω-gliadins contain no cysteine residues, they do not participate in the formation of the disulfide bridges that stabilize the protein structure. However, they can interact with other proteins via weak, low-energetic hydrogen bonds. We conclude that the elimination of ω-fractions from the gliadin complex causes minor modifications in secondary structures of the remaining gliadin proteins. In our opinion, these small, structural changes of proteins may lead to alterations in gliadin allergenicity.

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“…GLIs and GLUs are the two main groups of gluten proteins, the endosperm storage proteins, accounting for 60~80% of the total grain proteins. Gluten proteins influence dough rheological properties that determine the processing quality of bread, noodles and cookies [7][8][9]. GLIs belong to the monomeric prolamin fraction, and are classified into three structural groups of polypeptides according to their electrophoretic mobility, α/β-, γ-and ω-GLI.…”

Section: Introductionmentioning

confidence: 99%

“…Grain nitrogen content plays an important role affecting the ratio of storage to nonstorage proteins, the percentage of the storage protein fractions and, thus, the GLI/GLU ratio and the ratio of HMW-GS/LMW-GS [8,11,13]. To obtain the maximum wheat potential in the field, N is the most limiting nutrient required by plants.…”

Section: Introductionmentioning

confidence: 99%

Gluten Protein Compositional Changes in Response to Nitrogen Application Rate

et al. 2021

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Field trials were conducted to evaluate the effect of nitrogen level on wheat protein content and composition in 16 cultivars over two years at three locations. The nitrogen treatment comprised two nitrogen levels, 0 kg ha−1 as low and 100 kg ha−1 as high nitrogen, applied as top dressings of 50 kg nitrogen per ha at tillering and stem extension growth stages. Increased nitrogen level generally enhanced grain protein by 11.3% (11.5% vs. 12.8%). Considering protein composition determined by reversed phase–high-pressure liquid chromatography, higher nitrogen supply generally enhanced the proportion of total gliadins, α-gliadins, γ-gliadins and high-molecular-weight glutenin subunits by 1.1%, 2.0%, 3.7%, 0.6% and 0.9%, respectively, and reduced albumins and globulins, ω-gliadins, total glutenins and low-molecular-weight glutenin subunits by 1.1%, 1.7%, 1.9% and 3.2%. Under a high nitrogen level, the historical cultivars Libellula, San Pastore and U-1 had a higher protein content (13.1–15.2%) with significantly higher total gliadins, which resulted in a significantly higher gliadin/glutenin ratio (1.68–1.92). In the modern cultivars, protein content varied between 11.4% and 14.6% with a well-balanced gliadin/glutenin ratio (1.08–1.50), except for cultivar MV Nemere which had a high gliadin/glutenin ratio at both nitrogen levels (1.81 vs. 1.87). In summary, increasing nitrogen level enhanced grain protein content while the composition of gliadin and glutenin fractions was changed to a lesser extent and was largely cultivar specific and therefore should be considered for wheat baking quality assessment and breeding purposes.

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Influence of different nitrogen application on flour properties, gluten properties by HPLC and end-use quality of Korean wheat

Cited by 15 publications

References 29 publications

Effects of different fertilization levels on the concentration of high molecular weight glutenin subunits of two spring, hard red bread wheat cultivars

Effects of different fertilization levels on the concentration of high molecular weight glutenin subunits of two spring, hard red bread wheat cultivars

FT-Raman Spectroscopy as a Tool to Study the Secondary Structures of Wheat Gliadin Proteins

Gluten Protein Compositional Changes in Response to Nitrogen Application Rate

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