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Barley Protein (barley + protein)

Distribution by Scientific Domains
Chemistry80%

Selected Abstracts

Effects of Transglutaminase on SDS-PAGE Patterns of Wheat, Soy, and Barley Proteins and their Blends

JOURNAL OF FOOD SCIENCE, Issue 7 2002
A. Basman
ABSTRACT: Transglutaminase (TG) catalyzes the formation of nondisulfide covalent crosslinks between pep-tide-bound glutaminyl residues and ,-amino groups of lysine residues in proteins. TG can be used for polymerizing proteins from 1 or more sources through formation of intermolecular crosslinks. This study investigated, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, polymers created by the action of TG on proteins of wheat, soy, barley, wheat-soy, and wheat-barley blends. Electrophoretic results showed that with increasing incubation time, the crosslinking reaction is substantially increased, with progressive decrease or disappearance of some protein monomers. Densitometric results showed that soy proteins were the best substrates of TG while barley and wheat proteins were similar in reactivity. [source]

Apparent amino acid availability from feedstuffs in extruded diets for rainbow trout Oncorhynchus mykiss

AQUACULTURE NUTRITION, Issue 4 2010
T.G. GAYLORD
Abstract Apparent amino acid availability coefficients of several typical and novel feed ingredients were determined in rainbow trout using extruded diets and the faecal stripping technique. The ingredients were tested included five fish meals, three terrestrial animal by-products, five plant protein concentrates, four plant meals, and seven low-protein plant ingredients. Amino acid availability from the fish meals was relatively high ranging from 90 to 101%. Lower coefficients overall were observed for Menhaden fish meal FAQ when compared to the other fish meals. No differences in apparent amino acid availability were detected among the animal by-products. Within the plant concentrate group, rice protein concentrate and barley protein concentrate exhibited generally lower amino acid availabilities compared to other concentrates tested. Among the plant meals, only the availabilities of histidine, valine, isoleucine and lysine in flaxseed meal were lower than those of soybean meal. Apparent amino acid availabilities among the low-protein plant products were variable and significantly different. [source]

Molecular chemical structure of barley proteins revealed by ultra-spatially resolved synchrotron light sourced FTIR microspectroscopy: Comparison of barley varieties

BIOPOLYMERS, Issue 4 2007
Peiqiang Yu
Abstract Barley protein structure affects the barley quality, fermentation, and degradation behavior in both humans and animals among other factors such as protein matrix. Publications show various biological differences among barley varieties such as Valier and Harrington, which have significantly different degradation behaviors. The objectives of this study were to reveal the molecular structure of barley protein, comparing various varieties (Dolly, Valier, Harrington, LP955, AC Metcalfe, and Sisler), and quantify protein structure profiles using Gaussian and Lorentzian methods of multi-component peak modeling by using the ultra-spatially resolved synchrotron light sourced Fourier transform infrared microspectroscopy (SFTIRM). The items of the protein molecular structure revealed included protein structure ,-helices, ,-sheets, and others such as ,-turns and random coils. The experiment was performed at the National Synchrotron Light Source in Brookhaven National Laboratory (BNL, US Department of Energy, NY). The results showed that with the SFTIRM, the molecular structure of barley protein could be revealed. Barley protein structures exhibited significant differences among the varieties in terms of proportion and ratio of model-fitted ,-helices, ,-sheets, and others. By using multi-component peaks modeling at protein amide I region of 1710,1576 cm,1, the results show that barley protein consisted of approximately 18,34% of ,-helices, 14,25% of ,-sheets, and 44,69% others. AC Metcalfe, Sisler, and LP955 consisted of higher (P < 0.05) proportions of ,-helices (30,34%) than Dolly and Valier (,-helices 18,23%). Harrington was in between which was 25%. For protein ,-sheets, AC Metcalfe, and LP955 consisted of higher proportions (22,25%) than Dolly and Valier (13,17%). Different barley varieties contained different ,-helix to ,-sheet ratios, ranging from 1.4 to 2.0, although the difference were insignificant (P > 0.05). The ratio of ,-helices to others (0.3 to 1.0, P < 0.05) and that of ,-sheets to others (0.2 to 0.8, P < 0.05) were different among the barley varieties. It needs to be pointed out that using a multi-peak modeling for protein structure analysis is only for making relative estimates and not exact determinations and only for the comparison purpose between varieties. The principal component analysis showed that protein amide I Fourier self-deconvolution spectra were different among the barley varieties, indicating that protein internal molecular structure differed. The above results demonstrate the potential of the SFTIRM to localize relatively pure protein areas in barley tissues and reveal protein molecular structure. The results indicated relative differences in protein structures among the barley varieties, which may partly explain the biological differences among the barley varieties. Further study is needed to understand the relationship between barley molecular chemical structure and biological features in terms of nutrient availability and digestive behavior. © 2006 Wiley Periodicals, Inc. Biopolymers 85:308,317, 2007. This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com [source]

MALDI-TOF mass spectrometry of hordeins: rapid approach for identification of malting barley varieties

JOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 9 2009
alplachta
Abstract A procedure for identification of malting barley varieties using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) of ethanol-soluble barley proteins (hordeins) is described. The hordeins were first extracted from milled barley grains by several extraction protocols (using different extraction agents and conditions). Hordein extracts were then analyzed directly via MALDI-TOF MS without any preliminary purification or separation step, and the protein profiles of analyzed hordein extracts were compared in order to find out the most suitable extraction procedure for mass spectrometric analysis. The optimized procedure was successfully applied to identification of 13 malting barley varieties. Our results revealed that the proposed mass spectrometry-based approach provides characteristic mass patterns of extracted hordeins, which can be advantageously used for barley variety identification. Copyright © 2009 John Wiley & Sons, Ltd. [source]

Molecular chemical structure of barley proteins revealed by ultra-spatially resolved synchrotron light sourced FTIR microspectroscopy: Comparison of barley varieties

BIOPOLYMERS, Issue 4 2007
Peiqiang Yu
Abstract Barley protein structure affects the barley quality, fermentation, and degradation behavior in both humans and animals among other factors such as protein matrix. Publications show various biological differences among barley varieties such as Valier and Harrington, which have significantly different degradation behaviors. The objectives of this study were to reveal the molecular structure of barley protein, comparing various varieties (Dolly, Valier, Harrington, LP955, AC Metcalfe, and Sisler), and quantify protein structure profiles using Gaussian and Lorentzian methods of multi-component peak modeling by using the ultra-spatially resolved synchrotron light sourced Fourier transform infrared microspectroscopy (SFTIRM). The items of the protein molecular structure revealed included protein structure ,-helices, ,-sheets, and others such as ,-turns and random coils. The experiment was performed at the National Synchrotron Light Source in Brookhaven National Laboratory (BNL, US Department of Energy, NY). The results showed that with the SFTIRM, the molecular structure of barley protein could be revealed. Barley protein structures exhibited significant differences among the varieties in terms of proportion and ratio of model-fitted ,-helices, ,-sheets, and others. By using multi-component peaks modeling at protein amide I region of 1710,1576 cm,1, the results show that barley protein consisted of approximately 18,34% of ,-helices, 14,25% of ,-sheets, and 44,69% others. AC Metcalfe, Sisler, and LP955 consisted of higher (P < 0.05) proportions of ,-helices (30,34%) than Dolly and Valier (,-helices 18,23%). Harrington was in between which was 25%. For protein ,-sheets, AC Metcalfe, and LP955 consisted of higher proportions (22,25%) than Dolly and Valier (13,17%). Different barley varieties contained different ,-helix to ,-sheet ratios, ranging from 1.4 to 2.0, although the difference were insignificant (P > 0.05). The ratio of ,-helices to others (0.3 to 1.0, P < 0.05) and that of ,-sheets to others (0.2 to 0.8, P < 0.05) were different among the barley varieties. It needs to be pointed out that using a multi-peak modeling for protein structure analysis is only for making relative estimates and not exact determinations and only for the comparison purpose between varieties. The principal component analysis showed that protein amide I Fourier self-deconvolution spectra were different among the barley varieties, indicating that protein internal molecular structure differed. The above results demonstrate the potential of the SFTIRM to localize relatively pure protein areas in barley tissues and reveal protein molecular structure. The results indicated relative differences in protein structures among the barley varieties, which may partly explain the biological differences among the barley varieties. Further study is needed to understand the relationship between barley molecular chemical structure and biological features in terms of nutrient availability and digestive behavior. © 2006 Wiley Periodicals, Inc. Biopolymers 85:308,317, 2007. This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com [source]