Quality determination of wheat: genetic determination, biochemical markers, seed storage proteins - bread and durum wheat germplasm

2014 ◽  
Vol 94 (14) ◽  
pp. 2819-2829 ◽  
Author(s):  
Theo Varzakas ◽  
Natalia Kozub ◽  
Ioannis N Xynias
Keyword(s):  
Durum Wheat ◽  
Biochemical Markers ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Genetic Determination ◽  
Wheat Germplasm

Determination of Seed Storage Proteins and Total Isoflavones in Wild and Cultivated Soybeans

2009 ◽  
Vol 19 (1) ◽  
pp. 115-118
Author(s):  
Savithiry S. Natarajan ◽  
Devanand L. Luthria ◽  
Qijian Song ◽  
Perry Cregan
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins

scholarly journals Genetic diversity in several genotypes of Algerian lentil using biochemical markers

2021 ◽  
Vol 22 (6) ◽  
Author(s):  
Hamida Hammadi ◽  
DOUNIA HAMMOUDA-BOUSBIA ◽  
GHANIA CHAIB ◽  
ANFEL TIR
Keyword(s):  
Genetic Diversity ◽  
Biochemical Markers ◽  
Storage Proteins ◽  
Economic Value ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Grain Protein Content ◽  
Protein Profiling ◽  
Specific Marker ◽  
Pattern Polymorphism

Abstract. Hammadi H, Hammouda-Bousbia D, Chaib G, Tir A. 2021. Genetic diversity in several genotypes of Algerian lentil using biochemical markers. Biodiversitas 22: 3494-2500. Studying seed storage proteins in legumes (Fabaceae) is very important besides its economic value; seed storage proteins play an important role in plant taxonomy because of the stability of their contents. The grain protein content and protein profiles of 12 lentil genotypes (Lens culinaris Medik.) were characterized based on protein profiling through SDS-PAGE. The obtained gel has shown forty bands ranged from 13 to 21 with molecular weight 10 to 120 KDa. Of which six monomorphic bands, thirty-four polymorphic bands and five unique bands in Flip90-31, Idlep3, idlep2, Idlep4 and Radjas genotypes. The protein banding pattern polymorphism (84%) revealed an inter-genotypic variability. The Idlep3 genotype is characterized by specific bands (or a specific marker), followed by the Flip90-31 genotype. So these two genotypes can be considered as valuable gene resources for further breeding programs.

scholarly journals Development of reduced gluten wheat enabled by determination of the genetic basis of thelys3alow hordein barley mutant

2018 ◽  
Author(s):  
Charles P. Moehs ◽  
William J. Austill ◽  
Aaron Holm ◽  
Tao A. G. Large ◽  
Dayna Loeffler ◽  
...  
Keyword(s):  
Celiac Disease ◽  
Storage Proteins ◽  
Single Gene ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Nucleotide Polymorphisms ◽  
Related Condition ◽  
Single Nucleotide ◽  
Wheat Gene

AbstractCeliac disease is the most common food-induced enteropathy in humans with a prevalence of approximately 1% world-wide [1]. It is induced by digestion-resistant, proline- and glutamine-rich seed storage proteins, collectively referred to as “gluten,” found in wheat. Related prolamins are present in barley and rye. Both celiac disease and a related condition called non-celiac gluten sensitivity (NCGS) are increasing in incidence [2] [3]. This has prompted efforts to identify methods of lowering gluten in wheat, one of the most important cereal crops. Here we used BSR-seq (Bulked Segregant RNA-seq) and map-based cloning to identify the genetic lesion underlying a recessive, low prolamin mutation (lys3a) in diploid barley. We confirmed the mutant identity by complementing thelys3amutant with a transgenic copy of the wild type barley gene and then used TILLING (Targeting Induced Local Lesions in Genomes) [4] to identify induced SNPs (Single Nucleotide Polymorphisms) in the three homoeologs of the corresponding wheat gene. Combining inactivating mutations in the three sub-genomes of hexaploid bread wheat in a single wheat line lowered gliadin and low molecular weight glutenin accumulation by 50-60% and increased free and protein-bound lysine by 33%. This is the first report of the combination of mutations in homoeologs of a single gene that reduces gluten in wheat.

Seed Storage Proteins of Triticum turgidum ssp. dicoccoides and Their Effect on the Technological Quality in Durum Wheat

1991 ◽  
Vol 107 (4) ◽  
pp. 309-319 ◽  
Author(s):  
M. Ciaffi ◽  
S. Benedettelli ◽  
B. Giorgi ◽  
E. Porceddu ◽  
D. Lafiandra
Keyword(s):  
Durum Wheat ◽  
Storage Proteins ◽  
Triticum Turgidum ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Technological Quality

scholarly journals Wheat (Triticum aestivum L.) TaHMW1D Transcript Variants Are Highly Expressed in Response to Heat Stress and in Grains Located in Distal Part of the Spike

Plants ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 687
Author(s):  
Chan Seop Ko ◽  
Jin-Baek Kim ◽  
Min Jeong Hong ◽  
Yong Weon Seo
Keyword(s):  
Heat Stress ◽  
High Temperature ◽  
Temperature Stress ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Grain Filling ◽  
High Temperature Stress ◽  
Two Dimensional Gel Electrophoresis ◽  
Transcript Variants

High-temperature stress during the grain filling stage has a deleterious effect on grain yield and end-use quality. Plants undergo various transcriptional events of protein complexity as defensive responses to various stressors. The “Keumgang” wheat cultivar was subjected to high-temperature stress for 6 and 10 days beginning 9 days after anthesis, then two-dimensional gel electrophoresis (2DE) and peptide analyses were performed. Spots showing decreased contents in stressed plants were shown to have strong similarities with a high-molecular glutenin gene, TraesCS1D02G317301 (TaHMW1D). QRT-PCR results confirmed that TaHMW1D was expressed in its full form and in the form of four different transcript variants. These events always occurred between repetitive regions at specific deletion sites (5′-CAA (Glutamine) GG/TG (Glycine) or (Valine)-3′, 5′-GGG (Glycine) CAA (Glutamine) -3′) in an exonic region. Heat stress led to a significant increase in the expression of the transcript variants. This was most evident in the distal parts of the spike. Considering the importance of high-molecular weight glutenin subunits of seed storage proteins, stressed plants might choose shorter polypeptides while retaining glutenin function, thus maintaining the expression of glutenin motifs and conserved sites.

scholarly journals A Single Seed Protein Extraction Protocol for Characterizing Brassica Seed Storage Proteins

Agronomy ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 107
Author(s):  
Mahmudur Rahman ◽  
Lei Liu ◽  
Bronwyn J. Barkla
Keyword(s):  
Seed Protein ◽  
Storage Proteins ◽  
Protein Extraction ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Yield ◽  
Tissue Type ◽  
Single Seed ◽  
Material Optimization ◽  
Hazardous Chemical

Rapeseed oil-extracted expeller cake mostly contains protein. Various approaches have been used to isolate, detect and measure proteins in rapeseeds, with a particular focus on seed storage proteins (SSPs). To maximize the protein yield and minimize hazardous chemical use, isolation costs and the loss of seed material, optimization of the extraction method is pivotal. For some studies, it is also necessary to minimize or avoid seed-to-seed cross-contamination for phenotyping and single-tissue type analysis to know the exact amount of any bioactive component in a single seed, rather than a mixture of multiple seeds. However, a simple and robust method for single rapeseed seed protein extraction (SRPE) is unavailable. To establish a strategy for optimizing SRPE for downstream gel-based protein analysis, yielding the highest amount of SSPs in the most economical and rapid way, a variety of different approaches were tested, including variations to the seed pulverization steps, changes to the compositions of solvents and reagents and adjustments to the protein recovery steps. Following SRPE, 1D-SDS-PAGE was used to assess the quality and amount of proteins extracted. A standardized SRPE procedure was developed and then tested for yield and reproducibility. The highest protein yield and quality were obtained using a ball grinder with stainless steel beads in Safe-Lock microcentrifuge tubes with methanol as the solvent, providing a highly efficient, economic and effective method. The usefulness of this SRPE was validated by applying the procedure to extract protein from different Brassica oilseeds and for screening an ethyl methane sulfonate (EMS) mutant population of Brassica rapa R-0-18. The outcomes provide useful methodology for identifying and characterizing the SSPs in the SRPE.

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