نتایج جستجو برای: weight glutenin subunits overall
تعداد نتایج: 827295 فیلتر نتایج به سال:
In order to evaluate the relationship between SDS-sedimentation value and breadmaking quality of wheat (Triticum aestivum L.), glutenin subunits of different genotypes (foreign and Iranian cultivars) were analyzed by reverse-phase high performance liquid chromatography (RP-HPLC). SDS-sedimentation value was used as an indirect criterion for breadmaking quality. Correlation coefficients revealed...
In order to evaluate the relationship between SDS-sedimentation value and breadmaking quality of wheat (Triticum aestivum L.), glutenin subunits of different genotypes (foreign and Iranian cultivars) were analyzed by reverse-phase high performance liquid chromatography (RP-HPLC). SDS-sedimentation value was used as an indirect criterion for breadmaking quality. Correlation coefficients revealed...
To study grain quality traits and their relationships with high molecular weight (HMW) and low moleculor weight (LMW) glutenin subunits, 104 durum wheat genotypes were used. Six grain quality characteristics comprising wet and dry gluten content, test weight, grain hardiness, protein content and SDS sedimentation volume were studied. HMW and LMW glutenin subunits were evaluated using SDS-polyac...
To study grain quality traits and their relationships with high molecular weight (HMW) and low moleculor weight (LMW) glutenin subunits, 104 durum wheat genotypes were used. Six grain quality characteristics comprising wet and dry gluten content, test weight, grain hardiness, protein content and SDS sedimentation volume were studied. HMW and LMW glutenin subunits were evaluated using SDS-polyac...
high molecular weight (hmw) subunits of wheat glutenin are generally considered as playing a key role in gluten formation and structure, as well as to be closely related to wheat quality. the endosperm storage proteins of 80 synthetic lines and wheat cultivars (triticum aestivum) were fractionated through sodium dodecyl sulfate polyacrylamide gel electrophoresis to determine their high-molecula...
Abstract Background Wheat flour maturation affects the aggregation and structural stability of proteins. The number high-molecular-weight glutenin subunits (HMW-GSs) differs in various wheat varieties. effects Dx2 absence on protein characteristics thermal were investigated during 120 days using near-isogenic lines (NILs). Results delayed decreased flours maturation, i.e., maturation-induced in...
in this study, 120 aegilops crassa (mmdd genome) accessions from iran were evaluated for high molecular weight proteins. based on sds-page analysis, 17 bands were selected and mass spectrometry was used for protein identification. among 17 bands selected for maldi-tof-tof-ms analyzing, only 4 bands were identified as high molecular weight glutenin subunit similar to aegilops ventricosa and trit...
The polypeptide subunits of wheat glutenin obtained after reductive cleavage of disulfide bonds have been separated into two fractions by a modified Osborne technique. Approximately 62% of the subunits by weight are soluble, as is gliadin, in neutral 70% ethanol; the ethanol-soluble subunits are mainly of 44,000 molecular weight (MW). The ethanol-insoluble glutenin subunit fraction is markedly ...
Background and Objectives Wheat is essential to secure nutrition for the world's population. Its unique processing properties are largely determined by gluten protein content composition. Findings Gluten proteins subdivided into types, α-, γ-, ω1,2-, ω5-gliadins high-molecular-weight glutenin subunits low-molecular-weight subunits. The overall relative proportions of these types vary considerab...
Glutenin is a major protein fraction contributing to the functional properties of gluten and dough. The glutenin constitutes 30-40% of the protein in wheat flour and about half of that in gluten. It is essential to identify correct glutenin alleles and to improve wheat quality by selecting alleles that exert favorable effects. Moroccan wheat cultivars are unique in West Asia and North Africa re...
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