scholarly journals Composition, protein contents, and microstructural characterisation of grains and flours of emmer wheats (Triticum turgidum ssp. dicoccum) of the central Italy type

2014 ◽  
Vol 32 (No. 2) ◽  
pp. 115-121 ◽  
Author(s):  
V. Giacintucci ◽  
L. Guardeño ◽  
A. Puig ◽  
I. Hernando ◽  
G. Sacchetti ◽  
...  
Keyword(s):  
Common Wheat ◽  
Triticum Turgidum ◽  
Central Italy ◽  
Wheat Gluten ◽  
Emmer Wheat ◽  
Microstructural Characteristics ◽  
Sds Page ◽  
Weight Protein ◽  
Gliadin Patterns ◽  
Growth Habits

The microstructural characteristics were evaluated of two types of Italian Farro (Triticum turgidum ssp. dicoccum) with spring and autumn growth habits, the former with a vitreous tendency and the latter with a floury tendency. Common wheat flours and grains (Triticum aestivum) were used as controls. Protein fractions such as glutenin and gliadin were extracted from Triticum turgidum ssp. dicoccum flours and studied by SDS-PAGE in order to make a comparison between the electrophoretic analyses and microstructural studies which were conducted on the same samples using Scanning Electron Microscopy (SEM and Cryo-SEM). The results obtained by SDS-PAGE showed that the gliadin patterns of both emmer samples were similar, while the common wheat gliadins showed a band at 90 kDa that was not present in the gliadin fraction of emmer. When the glutenin patterns were analysed, the autumn emmer did not show the low molecular weight protein bands (16–23 kDa) whilst spring emmer wheat appeared more similar to common wheat. Regarding the microstructural characteristics of the kernels, spring (vitreous tendency) emmer showed starch granules covered by protein to a higher extent than autumn emmer. These differences were also observed in flours. The gluten of spring emmer wheat was observed as a homogeneous structure showing similarities with common wheat gluten, while autumnal emmer gluten appeared more heterogeneous and lacking in structure.  

The transfer of leaf and stem rust resistance from wild emmer wheats to durum and common wheat

2005 ◽  
Vol 85 (1) ◽  
pp. 49-57 ◽  
Author(s):  
D. R. Knott ◽  
Dapeng Bai ◽  
Janice Zale
Keyword(s):  
Leaf Rust ◽  
Common Wheat ◽  
Stem Rust ◽  
Hexaploid Wheat ◽  
Rust Resistance ◽  
Triticum Turgidum ◽  
Wheat Breeding ◽  
Stem Rust Resistance ◽  
Emmer Wheat ◽  
Wild Emmer

Wild emmer wheats (Triticum turgidum var. dicoccoides L.) are potentially valuable sources of leaf rust (Puccinia triticina Eriks.) and stem rust (Puccinia graminis f. sp. tritici Eriks. & Henn.) resistance in breeding both durum (T. turgidum var. durum L.) and common wheat (T. aestivum L.). In an extension of previous work, 11 rust resistant accessions of wild emmer wheat were crossed and backcrossed from two to five times to susceptible durum or common wheats. Genes for leaf or stem rust resistance were transferred singly into several susceptible genotypes. Backcross lines homozygous for resistance to leaf rust were tested with a set of either 9 or 10 leaf rust races and those homozygous for resistance to stem rust were tested with a set of either 10 or 13 stem rust races. The emmer wheats proved to carry a number of genes for resistance to each rust. In most cases, when a cross was made to a hexaploid wheat, resistance to both rusts was suppressed in the F1 seedlings, even when resistance was dominant in the tetraploids. Nevertheless, resistance was successfully transferred from several accessions to the hexaploids, indicating that suppressors on the A or B genome chromosomes were involved and segregation occurred for them. Rust resistance tended to decrease when it was transferred to another species, particularly hexaploid wheat. A number of lines carrying genes for either leaf rust or stem rust resistance were resistant to all races with which they were tested and have potential in wheat breeding. Key words: Emmer wheat, Triticum turgidum var. dicoccoides, stem rust, leaf rust, suppressors

scholarly journals Identification of an active 1Ay gene from Triticum turgidum ssp. dicoccoides

2014 ◽  
Vol 50 (No. 3) ◽  
pp. 208-215 ◽  
Author(s):  
Z.-G. Bi ◽  
B.-H. Wu ◽  
X.-G. Hu ◽  
X.-H. Guo ◽  
D.-C. Liu ◽  
...  
Keyword(s):  
Electrophoretic Mobility ◽  
Common Wheat ◽  
Triticum Turgidum ◽  
Structural Characteristics ◽  
Single Point ◽  
Point Mutations ◽  
Diploid Species ◽  
Emmer Wheat ◽  
Beta Turns ◽  
Different Content

The high molecular weight glutenin subunit (HMW-GS), encoded by the 1Ay gene, unexpressed in common wheat, exists in diploid and tetraploid wheats. An active 1Ay gene was first cloned from wild emmer wheat (T. turgidum ssp. dicoccoides, 2n = 4x = 28, AABB), the oldest species in emmer wheat. Here, a novel subunit encoded by the 1Ay gene (JF519636) present in T. turgidum ssp. dicoccoides line D141 was characterized. The protein had 608 amino acids with six cysteine residues and showed faster electrophoretic mobility than 1Dy12 from common wheat. Compared with previously reported 1Ay subunits, it contained 16 single point mutations (SPMs). Comparative and phylogenetic sequence analyses suggested that this gene was more similar to the 1Ay gene from the diploid species (2n = 2x = 14, AA) T. urartu than from T. monococcum ssp. aegilopoides. Its predicted secondary protein structure possessed a different content of motifs relative to the 1Ay gene (AY245578) from T. urartu, which had similar electrophoretic mobility. In the central repetitive domain, JF519636 had more β-turns and β-bends than the 1Ay subunit AY245578. These structural characteristics in JF519636 could possibly be associated with specific gluten properties.

scholarly journals Impact of Extraction Method on the Detection of Quality Biomarkers in Normal vs. DFD Meat

Foods ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1097
Author(s):  
Laura González-Blanco ◽  
Yolanda Diñeiro ◽  
Andrea Díaz-Luis ◽  
Ana Coto-Montes ◽  
Mamen Oliván ◽  
...  
Keyword(s):  
Extraction Method ◽  
Protein Pattern ◽  
Stress Protein ◽  
Electrophoretic Pattern ◽  
Extraction Methods ◽  
Sds Page ◽  
Weight Protein ◽  
Triton X ◽  
Protein Extractability ◽  
Selection Of

The objective of this work was to demonstrate how the extraction method affects the reliability of biomarker detection and how this detection depends on the biomarker location within the cell compartment. Different extraction methods were used to study the sarcoplasmic and myofibrillar fractions of the Longissimus thoracis et lumborum muscle of young bulls of the Asturiana de los Valles breed in two quality grades, standard (Control) or dark, firm, and dry (DFD) meat. Protein extractability and the expression of some of the main meat quality biomarkers—oxidative status (lipoperoxidation (LPO) and catalase activity (CAT)), proteome (SDS-PAGE electrophoretic pattern), and cell stress protein (Hsp70)—were analyzed. In the sarcoplasmic fraction, buffers containing Triton X-100 showed significantly higher protein extractability, LPO, and higher intensity of high-molecular-weight protein bands, whereas the TES buffer was more sensitive to distinguishing differences in the protein pattern between the Control and DFD meat. In the myofibrillar fraction, samples extracted with the lysis buffer showed significantly higher protein extractability, whereas samples extracted with the non-denaturing buffer showed higher results for LPO, CAT, and Hsp70, and higher-intensity bands in the electrophoretic pattern. These findings highlight the need for the careful selection of the extraction method used to analyze the different biomarkers considering their cellular location to adapt the extractive process.

scholarly journals Effects of Wheat Bug (Eurygasterspp. andAeliaspp.) Infestation in Preharvest Period on Wheat Technological Quality and Gluten Composition

2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Aleksandra M. Torbica ◽  
Jasna S. Mastilović ◽  
Milica M. Pojić ◽  
Žarko S. Kevrešan
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Wheat Gluten ◽  
Sodium Dodecyl ◽  
Deformation Energy ◽  
Wheat Varieties ◽  
Gluten Proteins ◽  
Molecular Weights ◽  
Sds Page ◽  
Technological Quality ◽  
Gluten Index

The effects of wheat bug infestation (Eurygasterspp. andAeliaspp.) on the composition of wheat gluten proteins and its influence on flour technological quality were investigated in the present study. Wheat samples of six wheat varieties, collected from two localities in northern Serbia, were characterized by significantly different level of wheat bug infestation. Composition of wheat gluten proteins was determined using sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS PAGE), while the selected parameters of technological quality were determined according to standard and modified empirical rheological methods (Farinograph, Extensograph, Alveograph, and Gluten Index). The surface morphology of the selected samples was viewed using scanning electron microscopy (SEM). Wheat from wheat bug-infested locality regardless of the variety had deteriorated technological quality expressed with higher Farinograph softening degree, lower or immeasurable Extensograph energy, and Alveograph deformation energy. The most important changes in the gluten proteins composition of bug-infested wheat were related to gliadin subunits with molecular weights below 75 kDa, which consequently caused deterioration of uniaxial and biaxial extensibility and dough softening during mixing.

Identification and mapping of a photoperiod response gene (QPpd.zafu-4A) on wild emmer wheat (Triticum turgidum L.) chromosome 4AL

Euphytica ◽  
2019 ◽  
Vol 215 (9) ◽  
Author(s):  
Jinsheng Yu ◽  
Yunzheng Miao ◽  
Siqing Yang ◽  
Zhaobin Shi ◽  
Nana Miao ◽  
...  
Keyword(s):  
Triticum Turgidum ◽  
Wild Emmer Wheat ◽  
Emmer Wheat ◽  
Wild Emmer ◽  
Photoperiod Response ◽  
Response Gene

scholarly journals Genotypic variability for salt stress tolerance among wild and cultivated wheat germplasms at an early development stage

2019 ◽  
Vol 4 (1) ◽  
pp. 375-380
Author(s):  
Imen Klay ◽  
Leila Riahi ◽  
Hajer Slim Amara ◽  
Abderrazak Daaloul
Keyword(s):  
Salt Stress ◽  
Stress Tolerance ◽  
Common Wheat ◽  
Triticum Turgidum ◽  
Wheat Variety ◽  
Development Stage ◽  
Salt Stress Tolerance ◽  
Wheat Varieties ◽  
The Common ◽  
Photosynthetic Traits

AbstractThis study was conducted to evaluate the variability of salt tolerance potentials among nine wheat genotypes representing wild and cultivated species namely Triticum turgidum subsp. durum, Triticum aestivum and Aegilops geniculata. Ionomic and photosynthetic traits were used for the screening of the studied samples when faced with four salinity levels of NaCl (0, 50, 100 and 150 mM) under green house conditions at the seedling stage. The investigated genotypes exhibited different levels of salt stress tolerance. Ionomic and photosynthetic traits underline the distinctiveness of the common wheat varieties which highlighted particular performances under salt stress conditions and showed higher tolerance potentials among the studied genotypes. Interestingly, the Vaga variety showed more ability to maintain higher K+/Na+ ratios and Pq coefficients compared with the control conditions and stable Fv/F0 and Fv/Fm ratios. Stable behaviour was exhibited by wild Aegilops accessions while durum wheat varieties have been shown to be more sensitive to salt stress. Further investigations were required for the common wheat variety Vaga, which could be useful for successful breeding and biotechnological improvement strategies concerning wheat species.

Gliadin polymorphism in Turkish cultivated emmer wheat [Triticum turgidum L. ssp. dicoccon (Schrank) Thell.] landraces

2011 ◽  
Vol 296 (1-2) ◽  
pp. 121-135 ◽  
Author(s):  
Özlem Özbek ◽  
Belgin Göçmen Taşkın ◽  
Sibel Keskin Şan ◽  
Vehbi Eser ◽  
Orhan Arslan
Keyword(s):  
Triticum Turgidum ◽  
Emmer Wheat

scholarly journals Variation in HMW glutenin subunits of different species of wheat

2011 ◽  
Vol 48 (No. 1) ◽  
pp. 15-19
Author(s):  
Z. Gálová ◽  
MichalíkI ◽  
H. Knoblochová ◽  
E. Gregová
Keyword(s):  
Triticum Turgidum ◽  
Wheat Cultivars ◽  
Glutenin Subunits ◽  
Bread Making ◽  
Wheat Varieties ◽  
Hmw Glutenin Subunits ◽  
Sds Page ◽  
Hmw Glutenin ◽  
Triticum Durum Desf

Method ISTA SDS-PAGE was used for separation, detection and evaluation of high molecular weight glutenin subunits (HMW) in the different wheat species. The relation has been studied between the HMW glutenin subunit alleles and the bread-making quality of 25 world wheat cultivars and 21 regional varieties common wheat varieties (Triticum aestivum L.), 17 winter spelt wheat (Triticum spelta L.), 3 durum wheat cultivars (Triticum durum DESF.), 9 cultivars of Triticum turgidum L. and 5 cultivars of Triticum polonicum L. The highest frequency of occurrence of HMW glutenin subunits 2*, 13 + 16 and 5 + 10 were found in world wheat cultivars. In Slovak wheat varieties were analysed subunits 0, 7 + 9 and 5 + 10, 2 + 12. The HMW subunits 0, 7 + 8 with Glu-score 4 were determined in Triticum durum DESF. Three electrophoretical profile groups of different HMW glutenin subunits were found in Triticum turgidum L. and Triticum polonicum L. and six electrophoretical profile groups were determined in Triticum spelta L. The verified correlations between bread-making quality and specific HMW subunits of glutenin can be utilised by wheat breeders using SDS-PAGE of proteins as a screening test for the prediction of bread-making quality of wheat.

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.

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