Results 321 to 330 of about 64,624 (342)
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Hydrogen-ion equilibria of wheat gluten

Archives of Biochemistry and Biophysics, 1963
Abstract Hydrogen-ion titration curves of wheat gluten have been studied in 3 M urea plus 0.15 M KCl at 25 °C. Ionizing groups per 105 g. gluten and their intrinsic pK's at 25 δC. are: 29 carboxyl (4.77), 15 imidazole (6.43), 2 α-amino (8.4), 1 sulfhydryl (10.1), 20 tyrosyl (10.26), and 9 lysyl (10.78).
R.J. Dimler, Ying Victor Wu
openaire   +3 more sources

THE SELECTIVE DEGRADATION OF WHEAT GLUTEN

Canadian Journal of Chemistry, 1955
A method believed to hydrolyze peptide bonds of proteins selectively at the amino groups of serine was used to obtain polypeptides from wheat gluten. The procedure involved the use of strong acid and introduced appreciable amounts of sulphur into the products possibly as sulphonic acid groups.
L. Wilson, L. Wiseblatt, W. B. McConnell
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Rheological properties of wheat gluten

Journal of Cereal Science, 1990
Glutens were prepared from four wheat varieties (Kadet, Timmo, Extrem, San Pastore), which perform very differently in cereal products. The dynamic rheological and tensile properties of the glutens were measured by: (i) small angle oscillatory deformation of hydrated glutens in the temperature range 25–100 °C using a Rheometrics mechanical spectrometer
D.J. Barnes   +3 more
openaire   +2 more sources

Chemical modification of wheat gluten with hydrazine

Canadian Journal of Biochemistry, 1969
The side-chain amide groups of wheat gluten were converted to hydrazide groups by reaction with hydrazine in aqueous and anhydrous systems. When the reaction was carried out in aqueous hydrazine, extensive hydrolysis of side-chain, as well as peptide-amide groups occurred. Anhydrous hydrazine, when used as solvent and reactant, increased the extent of
J. S. Wall, L. H. Krull
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Specificity of a wheat gluten aspartic proteinase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1998
The substrate and peptide bond specificities of a purified wheat gluten aspartic proteinase (GlAP) are studied. GlAP shows maximum gluten hydrolysing activity at pH 3.0. At this pH, especially the wheat high molecular weight glutenin subunits (HMW-GS) and to a lesser extent the low molecular weight glutenin subunits and gliadins are hydrolysed.
Fred Van Leuven   +4 more
openaire   +3 more sources

Wheat gluten applications in food products

Journal of the American Oil Chemists' Society, 1979
AbstractVital wheat gluten has traditionally been noted for its functional benefits in various bakery applications. In recent years extensive research and development work has taken place to more clearly identify wheat gluten's unique characteristics and functional properties. As a result, many new and novel applications have been developed.
openaire   +3 more sources

Chemical Modification of Wheat Gluten [PDF]

open access: possible, 2001
Wheat gluten was cross-linked using water soluble 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide HC1 (EDC) together with N-hydroxysuccinimide (NHS) in order to improve its functional properties in non-food applications. By varying reaction parameters, it was demonstrated that cross-linking of the proteins occurred through different mechanisms.
Françoise Silvestre   +3 more
openaire   +1 more source

The Ultrastructure of Commercial Wheat Gluten

Canadian Institute of Food Science and Technology Journal, 1975
Abstract Structural relationships of the component parts of wheat gluten and flour doughs were studied by electron microscopy. Consideration was given to characteristics relative to use of wheat gluten in texturized vegetable protein products. Transmission and scanning electron microscope techniques revealed that starch granules played an important ...
D.B. Cumming, Marvin A. Tung
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To Wheat or not to Wheat: Timing of Gluten Introduction

Evidence-Based Practice, 2021
Ashley U. Hall   +3 more
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Wheat, Gluten and ATI: An Overview

2019
In this chapter, the history of wheat cultivation and breeding is described. Wheat originated in the Middle East, spread to Europe and captured the whole world. Modern wheat varieties developed from old ones, namely by breeding and crossbreeding from low-yielding diploid wild wheat to modern hexaploid high-performance wheat.
Detlef Schuppan   +1 more
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