Diversity of Novel Glutenin Subunits in Bread Wheat (Triticum aestivum L.)

Kamal, Abu Hena Mostafa; Kim, Ki‐Hyun; Shin, Kyong‐Oh; Seo, Hyung-Seok; Tsujimoto, Hisashi; Heo, Hwa‐Young; Choi, Jong‐Soon; Park, Chul‐Soo; Woo, Sun Hee

doi:10.1007/s12374-009-9069-z

Cited by 14 publications

(21 citation statements)

References 33 publications

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“…After protein quantification, a total of 300 μg of solubilized proteins was used for 2-DE, as previously described (Kamal et al 2009b). The first dimension was performed with a prepared isoelectric focusing (IEF) tube gel solution consisting of a 30% acrylamide solution that contained 7 M urea, 10% NP-40, 0.5% carrier ampholytes (pH 3 to 10), 10% APS, and TEMED.…”

Section: -D Gel Electrophoresismentioning

confidence: 99%

“…Using a protocol modified from that reported by Kamal et al (2009b), we excised selected protein spots from preparative gels, stained with Coomassie Brilliant Blue (R-250). These had been washed with 100 μL of distilled water and incubated three times (10 min each) at 37°C for 10 min.…”

Section: In-gel Digestion and Mass Spectrometrymentioning

confidence: 99%

“…For analysis via MALDI-TOF mass spectrometry (AXIMA CFR + Plus, Shimadzu, Japan), proteins that had been separated by 2-DE were digested by trypsin according to the method of Kamal et al (2009b). The machine was run in a reflector/time-lag-focusing mode controlled by Launchpad software ver.…”

Section: In-gel Digestion and Mass Spectrometrymentioning

confidence: 99%

“…Glutenin contains two kinds of isoforms-high molecular weight and low molecular weight subunits (Kamal et al 2009b). Puroindoline is another storage protein that may act as a membranotoxin, probably through its antibacterial and antifungal activities.…”

Section: Functional Categorization Based On Biological Processmentioning

confidence: 99%

“…Storage proteins in the seed are responsible for dough substance and, hence, have been evaluated extensively in an attempt to elucidate their biochemical properties, yielding better dough and higher viscoelasticity. Hybridization can be used to transfer both HMW-GS and LMW-GS from wild relatives into cultivated species (Kamal et al 2009b). Yan et al (2003) have identified 42 HMW-GS alleles from A. tauschii, among which are several alleles not presently detected in bread wheat.…”

Section: Introductionmentioning

confidence: 99%

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Wild Relatives of the Wheat Grain Proteome

et al. 2010

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We applied proteomics analysis to generate a map of the wild relatives of wheat grain proteins. These differentially expressed proteins are potentially involved in metabolism, stress responses, and other biological activities. Using two-dimensional electrophoresis, we detected 119, 134, and 193 reproducible spots on gels loaded with protein samples extracted from the A, B, and D genomes, respectively, of the mature grain. In all, 89, 53, and 54 distinct proteins, respectively, were found among these genomes through MALDI-TOF mass spectrometry. Of these, 26% (n=52) proteins were considered distinct. They included 18.89% (n=17) in the A, 28.30% (n=15) in the B, and 37.04% (n=20) in the D genome, all functioning in disease and defense roles. For example, the ABA-inducible protein PHVA1 can be induced by drought, cold, heat, and salinity, while the basic endochitinase confers protection against chitin-containing fungal pathogens. The diverse functional categories found here suggest different biological processes, such as disease/defense, energy metabolism, protein synthesis and storage, cellular organization, signal transduction, transcription, and the facilitation of transport. Our findings demonstrate that these functional proteins have important roles in stress tolerance and the maintenance of quality in mature grains. The interacting effects of genetics and environment on differential protein production may be partially mediated by a regulatory mechanism in those grains.

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Section: -D Gel Electrophoresismentioning

confidence: 99%

Section: In-gel Digestion and Mass Spectrometrymentioning

confidence: 99%

Section: In-gel Digestion and Mass Spectrometrymentioning

confidence: 99%

Section: Functional Categorization Based On Biological Processmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Wild Relatives of the Wheat Grain Proteome

et al. 2010

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Effects of ozone treatment on physicochemical properties of Korean wheat flour

Lee

Kim

Kwak

et al. 2017

Food Sci Biotechnol

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The objective of this study was to investigate the effects of ozone treatment on the physicochemical properties of Korean wheat flour. Wheat flour samples were treated with ozone gas at 120 ppm for 15, 30, 45, and 60 min. Color b value, pH, and mold of flour decreased as exposure time to ozone increased. The water absorption index, peak viscosity, and final viscosity of flour increased by ozone treatment. Photomicrographs of flour suspensions under polarized light showed granules tended to lose birefringence owing to ozone during swelling. The result of SDS-PAGE showed that the intensity of protein bands at low molecular weights slightly increased in ozone-treated flours compared to the intensity in the control flour. The results of this study showed ozone gas affected the starch and protein of wheat flour, suggesting a need for further investigation on structural changes in starch and protein by ozone.

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Wheat storage proteins: changes on the glutenins after wheat infection with different isolates of Fusarium graminearum

et al. 2018

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Wheat gluten proteins are decisive for the industrial properties of flour, so alterations resulting from grain infection with Fusarium graminearum produce changes in the glutenin content that affect the baking properties. This work analyzes the high-molecular-weight glutenin changes from wheat flour with different degrees of F. graminearum infection at field, since these proteins are determinant for the quality properties of flour. Wheat cultivars-on field trials-infected with F. graminearum isolates of diverse aggressiveness showed severity values between 9.1 and 42.58% and thousand kernel weight values between 28.12 and 32.33 g. Negative correlations between severity and protein content and positive correlations between yield and protein content were observed, employing reversed-phase high-performance liquid chromatography and polyacrylamide gel electrophoresis. Furthermore, the protein signal changes were in agreement for both methodological approaches. Also, the degree of disease observed and the protein changes on infected wheat cultivars varied in relation with the aggressiveness of the isolate responsible for the infection. The principal component analysis showed a close arrangement among protein values obtained by HPLC. For each cultivar, two principal components were obtained, which explained 80.85%, 88.48%, and 93.33% of the total variance (cultivars Sy200, AGP Fast, and Klein Tigre respectively). To our knowledge, the approaches employed for the analysis of protein changes according to the degree of disease, as well as the thorough statistical analysis, are novel for the study of Fusarium Head Blight.

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Diversity of Novel Glutenin Subunits in Bread Wheat (Triticum aestivum L.)

Cited by 14 publications

References 33 publications

Wild Relatives of the Wheat Grain Proteome

Wild Relatives of the Wheat Grain Proteome

Effects of ozone treatment on physicochemical properties of Korean wheat flour

Wheat storage proteins: changes on the glutenins after wheat infection with different isolates of Fusarium graminearum

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