Results 191 to 200 of about 18,117 (243)
Surface Films of Gliadin [PDF]
Nature, 1938 MITCHELL1 has reported that under suitable conditions proteins can be spread from a solution to give films the force-area curves of which show a sharp transition point in the region of 1–2 dynes/cm., the extrapolated areas of the two distinct portions of the curve being approximately 0.3 and 0.7 × 10−7gm. /sq. cm. respectively.
T. W. J. Taylor, G. I. Jenkins
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Colloid and Polymer Science, 2016
Bio-derived, fully biodegradable closed-cell micro- and nanocellular foams were generated from gliadin. Gliadin, an abundantly available wheat storage protein, was extracted with aqueous ethanol from wheat gluten. For the newly developed foaming process, dry gliadin powder was plasticized by equal volumes of water and ethanol resulting in a ...
Silke Quester +2 more
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Bio-derived, fully biodegradable closed-cell micro- and nanocellular foams were generated from gliadin. Gliadin, an abundantly available wheat storage protein, was extracted with aqueous ethanol from wheat gluten. For the newly developed foaming process, dry gliadin powder was plasticized by equal volumes of water and ethanol resulting in a ...
Silke Quester +2 more
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Journal of Food Science, 1991
ABSTRACTCrude wheat gliadin from acetic acid solution showed lower water sorption by pulse and frontal Inverse Gas Chromatography methods as compared to a static method but the pulse data for a highly purified Ponca wheat gliadin from ethanol agreed with static data for crude gliadin.
Henryk Daun +2 more
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ABSTRACTCrude wheat gliadin from acetic acid solution showed lower water sorption by pulse and frontal Inverse Gas Chromatography methods as compared to a static method but the pulse data for a highly purified Ponca wheat gliadin from ethanol agreed with static data for crude gliadin.
Henryk Daun +2 more
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Biochemical and molecular characterization of gliadins
Molecular Biology, 2006Gliadins account for about 40-50% of the total proteins in wheat seeds and play an important role on the nutritional and processing quality of flour. Usually, gliadins could be divided into alpha- (alpha/beta-), gamma- and omega-groups, whereas the low-molecular-weigh (LMW) gliadins were novel seed storage proteins.
Yuan-Wen Yue +4 more
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Correlation between gliadin bands
Theoretical and Applied Genetics, 1983Starch gel electrophoresis of gliadins was carried out for 37 bread wheat cultivars chosen for their distant relationships. Simple correlations were calculated between each of the 41 bands (variates) observed with these wheats. It was found that a band is usually negatively correlated with the two neighbouring mobility bands.
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Polymorphism of gliadin and unusual gliadin alleles in Triticum boeoticum
Genome, 1992More than 50 gliadin electrophoretic patterns (Al-lactate, pH 3.1) have been found in a collection of 60 T. monococcum L. ssp. boeoticum accessions. Analyses of F2 seeds of the two intraspecies crosses revealed two unlinked gliadin-coding loci (Gli-A1bt and Gli-A2bt) in each genotype studied.
E. V. Metakovsky, S. K. Baboev
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Foaming Properties of Wheat Gliadin
Journal of Agricultural and Food Chemistry, 2011We studied gliadin solubility, surface tension and foam behavior, and the presence of different gliadin types in gliadin aqueous solutions and foams as a function of pH. Gliadin has excellent foaming properties only at neutral and alkaline pH. Its solubility is minimal near neutral pH, while almost complete at acidic and alkaline pH.
Bert G. Thewissen +3 more
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1978
Becarri, in 1745, and Einhof, in 1805, were the first to study the proteins present in wheat flour, but the name ‘gliadin’ was not known until 1820 when Taddei used this name to describe the alcohol-soluble protein components of flour. Since then, an ever-increasing amount of literature has appeared on gliadin. Up to 1970, Chemical Abstracts quotes 536
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Becarri, in 1745, and Einhof, in 1805, were the first to study the proteins present in wheat flour, but the name ‘gliadin’ was not known until 1820 when Taddei used this name to describe the alcohol-soluble protein components of flour. Since then, an ever-increasing amount of literature has appeared on gliadin. Up to 1970, Chemical Abstracts quotes 536
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Journal of the Science of Food and Agriculture, 1977
AbstractA β‐gliadin from Cappelle‐Desprez wheat has been purified sufficiently to be analysed. Its amino acid composition is typical of the gliadin class. The molecule appears to be a single polypeptide chain with no carbohydrate or SH groups and a molecular weight of 38 000.
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AbstractA β‐gliadin from Cappelle‐Desprez wheat has been purified sufficiently to be analysed. Its amino acid composition is typical of the gliadin class. The molecule appears to be a single polypeptide chain with no carbohydrate or SH groups and a molecular weight of 38 000.
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Plant Science, 1988
Abstract A low stringency screening of a wheat ( Triticum aestivum L.) genomic library produced three types of γ gliadin clones. The sequence of one clone, λ10–20, encoded a γ gliadin of 34.3 kDa. Comparisons of this protein with the proteins encoded by other γ gliadin DNA sequences revealed a general γ gliadin structure: a 19-residue signal peptide;
Kay Scheets, Charles Hedgcoth
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Abstract A low stringency screening of a wheat ( Triticum aestivum L.) genomic library produced three types of γ gliadin clones. The sequence of one clone, λ10–20, encoded a γ gliadin of 34.3 kDa. Comparisons of this protein with the proteins encoded by other γ gliadin DNA sequences revealed a general γ gliadin structure: a 19-residue signal peptide;
Kay Scheets, Charles Hedgcoth
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