Gluten Proteins

2004 ◽  
Keyword(s):  
Gluten Proteins

NanoUPLC-MSE reveals differential abundance of gluten proteins in wheat flours of different technological qualities

2021 ◽  
Vol 239 ◽  
pp. 104181
Author(s):  
V.C. M. Victorio ◽  
T. O. Alves ◽  
G.H. M. F. Souza ◽  
L.C. Gutkoski ◽  
L.C. Cameron ◽  
...  
Keyword(s):  
Differential Abundance ◽  
Gluten Proteins ◽  
Wheat Flours

scholarly journals Gliadin Sequestration as a Novel Therapy for Celiac Disease: A Prospective Application for Polyphenols

2021 ◽  
Vol 22 (2) ◽  
pp. 595
Author(s):  
Charlene B. Van Buiten ◽  
Ryan J. Elias
Keyword(s):  
Immune Response ◽  
Celiac Disease ◽  
Gastrointestinal Symptoms ◽  
Autoimmune Disorder ◽  
Treatment Method ◽  
Mucosal Damage ◽  
Protective Effects ◽  
Novel Therapy ◽  
Gluten Proteins ◽  
Prospective Application

Celiac disease is an autoimmune disorder characterized by a heightened immune response to gluten proteins in the diet, leading to gastrointestinal symptoms and mucosal damage localized to the small intestine. Despite its prevalence, the only treatment currently available for celiac disease is complete avoidance of gluten proteins in the diet. Ongoing clinical trials have focused on targeting the immune response or gluten proteins through methods such as immunosuppression, enhanced protein degradation and protein sequestration. Recent studies suggest that polyphenols may elicit protective effects within the celiac disease milieu by disrupting the enzymatic hydrolysis of gluten proteins, sequestering gluten proteins from recognition by critical receptors in pathogenesis and exerting anti-inflammatory effects on the system as a whole. This review highlights mechanisms by which polyphenols can protect against celiac disease, takes a critical look at recent works and outlines future applications for this potential treatment method.

Effects of gamma-irradiation of wheat on gluten proteins

1998 ◽  
Vol 28 (3) ◽  
pp. 243-250 ◽  
Author(s):  
H. Köksel ◽  
H.D. Sapirstein ◽  
S. Çelik ◽  
W. Bushuk
Keyword(s):  
Gamma Irradiation ◽  
Gluten Proteins

Study of structural changes of gluten proteins during bread dough mixing by Raman spectroscopy

2021 ◽  
Vol 358 ◽  
pp. 129916
Author(s):  
Eloïse Lancelot ◽  
Joran Fontaine ◽  
Joëlle Grua-Priol ◽  
Ali Assaf ◽  
Gérald Thouand ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Structural Changes ◽  
Bread Dough ◽  
Gluten Proteins ◽  
Dough Mixing

PREPARATION AND HEAT DENATURATION OF THE GLUTEN PROTEINS

1931 ◽  
Vol 5 (4) ◽  
pp. 389-406 ◽  
Author(s):  
W. H. Cook
Keyword(s):  
Elevated Temperatures ◽  
Marked Decrease ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Heat Denaturation ◽  
Hydrogen Ion Concentration ◽  
Gluten Proteins ◽  
Buffer Solutions ◽  
Natural Moisture Content ◽  
Low Solubility

Gliadin prepared by several different methods had the same nitrogen content and distribution. The critical peptization temperature (C.P.T.) in 60% alcohol and viscosity in 30% urea-buffer solutions, however, showed considerable variation, preparations of high C.P.T. (low solubility) being more viscous. This variation in the physical properties is explained by fractionation or denaturation incidental to the method of preparation.Gluten precipitated from 30% urea solutions at salt concentrations varying from 0.1 to 0.5 of saturation, yielded fractions that varied continuously in their gliadin and glutenin content, as judged from their percentage of arginine nitrogen.Gluten dispersed in buffered 30% urea solutions showed no change in viscosity during 101 hr. after the gluten was completely dispersed. A variation of hydrogen ion concentration between pH 6.0 and 6.95 had little effect on its viscosity. Heating at 70 °C. caused a marked decrease in the viscosity of this dispersion during the first hour. When gliadin dispersions are heated as above only samples having a high initial viscosity and C.P.T. become less viscous. Heating gliadin of natural moisture content (12 to 14%) at 70 °C. for varying periods of time did not change significantly its subsequent C.P.T. and viscosity in 60% alcohol. More severe heat treatments at higher moisture contents rendered the gliadin insoluble in 60% alcohol. Dilute alcoholic extracts of heated flours contained less protein than those of unheated controls. However, the C.P.T. of the former was lower than that of the latter. It is concluded from these experiments that when the gluten proteins are subjected to elevated temperatures, the glutenin fraction is first affected, next the gliadin fractions of low solubility, and finally, under severe conditions, all of the gliadin is denatured.

The Effect of Non-Gluten Proteins on the Staling of Bread

2001 ◽  
Vol 53 (6) ◽  
pp. 278-280 ◽  
Author(s):  
Juliet A. Gerrard ◽  
Rebecca C. Abbot ◽  
Marcus P. Newberry ◽  
Margy J. Gilpin ◽  
Marcela Ross ◽  
...  
Keyword(s):  
Gluten Proteins

scholarly journals A modified extraction protocol enables detection and quantification of celiac disease-related gluten proteins from wheat

2009 ◽  
Vol 877 (10) ◽  
pp. 975-982 ◽  
Author(s):  
Hetty C. van den Broeck ◽  
Antoine H.P. America ◽  
Marinus J.M. Smulders ◽  
Dirk Bosch ◽  
Rob J. Hamer ◽  
...  
Keyword(s):  
Celiac Disease ◽  
Gluten Proteins ◽  
Extraction Protocol ◽  
Detection And Quantification
Sign in / Sign up

Export Citation Format

Share Document