Results 141 to 150 of about 1,716 (182)

Depolymerization of the Glutenin Macropolymer During Mixing: II. Differences in Retention of Specific Glutenin Subunits

Cereal Chemistry, 1999
ABSTRACTThe depolymerization of individual high and low molecular weight (HMW and LMW, respectively) glutenin subunits (GS) from the glutenin macropolymer (GMP) in doughs during mixing was investigated by reversed‐phase (RP) HPLC and SDS‐PAGE. Cultivars with different dough strengths, as well as lines null for specific HMW‐GS and biotypes differing at ...
John H. Skerritt, Luch Hac, Megan P. Lindsay, Ferenc Bekes   +3 more
openaire   +1 more source

Phosphorus affects high-molecular-weight glutenin subunits and glutenin macropolymer size distribution in wheat grains

The Journal of Agricultural Science, 2013
SUMMARYTwo winter wheat (Triticum aestivumL.) cultivars, Jimai20 and Shannong12, differing in phosphorus (P) utilization efficiency, were selected to study the effect of P application rate on changes in glutenin macropolymer (GMP) size distribution and the content of high-molecular-weight glutenin subunits (HMW-GS) in wheat grain. Four P levels (0, 40,
Y. NI, D. YANG, Z. WANG, Y. YIN, T. CAI, Z. DAI, S. YAN, W. LI   +7 more
openaire   +1 more source

Rheology of Mixtures of Glutenin Subfractions

Journal of Cereal Science, 1997
Abstract The dynamic rheological behaviours of mixtures of glutenin fractions extracted from wheat cultivar Hereward were investigated as a function of the relative concentration of high to low molecular weight glutenin concatenations. Time-temperature superposition could be applied to both the mixtures and to the total gluten, as long as heat ...
A.A. Tsiami, A. Bot, W.G.M. Agterof
openaire   +1 more source

Degradation of HMW Glutenins During Wheat Sourdough Fermentations

Cereal Chemistry, 2004
ABSTRACTBakeries use sourdoughs to improve bread properties such as flavor and shelf life. The degradation of gluten proteins during fermentation may, however, crucially alter the gluten network formation. We observed changes that occurred in the HMW glutenins during wheat sourdough fermentations.
Jussi Loponen, Kati Katina, Tuula Sontag-Strohm   +2 more
exaly   +4 more sources

Fingerprinting of glutenin and gliadin

Journal of the Science of Food and Agriculture, 1966
AbstractProbability considerations applied to fingerprints of enzymic digests of Conley glutenin and gliadin have shown a significant relationship between them. Acetic acid‐soluble proteins of wheat and rye also gave closely similar fingerprints. It is tentatively concluded that there may be a basic similarity in the aminoacid sequences of considerable
openaire   +1 more source

Proteolytic Action of Pepsin on Glutenin

Journal of Food Science, 1965
SUMMARY Pepsin rapidly decreases the viscosity of a glutenin dispersion having an acid reaction and rapidly increases‐the amount of water‐soluble fragments. The molecular weight of the solubilized fragments, estimated by the gel‐filtration method, indicates that most of the fragments are large and have: molecular weights greater than ...
S. OKA, F. J. BABEL, H. N. DRAUDT
openaire   +1 more source

Wheat transformation with glutenin gene.

Mededelingen (Rijksuniversiteit te Gent. Fakulteit van de Landbouwkundige en Toegepaste Biologische Wetenschappen), 2005
The rheological properties of wheat grains are associated with the composition of the starchy endosperm in high molecular weight (HMW) glutenin proteins. The HMW glutenin 1xDy12 subunit gene was co introduced with the screenable bar and the reporter gus marker genes in the commercial spring wheat Minaret cultivar (cv).
F, Delporte, B, Jérouville, A, Mélard, L, Kutten, R, Baleux, M, Iuliano, D, Schellingen, J M, Jacquemin   +7 more
openaire   +1 more source

PREPARATION OF GLUTENIN IN UREA SOLUTIONS

Canadian Journal of Research, 1931
A new method has been developed for preparing glutenin, using concentrated urea solution as a dispersion medium. The starch is removed from the dispersion by passing it through a Sharpies supercentrifuge. The glutenin is then removed from the gliadin by precipitation: (a) by adding magnesium sulphate to about 0.17 of saturation; or (b) by adding water ...
W. H. Cook, C. L. Alsberg
openaire   +1 more source

Hydrogen ion equilibria of wheat glutenin and gliadin

Archives of Biochemistry and Biophysics, 1963
Abstract Hydrogen ion titration curves of twice-precipitated wheat glutenin and gliadin have been obtained in 3 M urea plus 0.15 M KCl at 25 °C. The data have been analyzed by equations treating the electrostatic effect as an empirical factor. The ionizing groups per 10 5 g. glutenin, and their intrinsic p K 's at 25 °C. are: 38 carboxyl (4.76),
Y V, WU, R J, DIMLER
openaire   +2 more sources

Reduction and reoxidation of wheat glutenin★

Biochimica et Biophysica Acta (BBA) - General Subjects, 1966
Abstract The nature of disulfide bonds in wheat glutenin and the factors that influence their formation were investigated by reducing and reoxidizing them under various conditions. The presence in glutenin of intramolecular disulfide bonds, as well as intermolecular, is indicated by a small viscosity increase that follows the large viscosity drop ...
A.C. Beckwith, J.S. Wall
openaire   +1 more source