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Yang, Tao, Pei Wang, Qin Zhou, et al. "Effects of Different Gluten Proteins on Starch’s Structural and Physicochemical Properties during Heating and Their Molecular Interactions." International Journal of Molecular Sciences 23, no. 15 (2022): 8523. http://dx.doi.org/10.3390/ijms23158523.
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Starch–gluten interactions are affected by biopolymer type and processing. However, the differentiation mechanisms for gluten–starch interactions during heating have not been illuminated. The effects of glutens from two different wheat flours (a weak-gluten (Yangmai 22, Y22) and a medium-strong gluten (Yangmai 16, Y16)) on starch’s (S) structural and physicochemical properties during heating and their molecular interactions were investigated in this study. The results showed that gluten hindered the gelatinization and swelling of starch during heating when temperature was below 75 °C, due to competitive hydration and physical barriers of glutens, especially in Y22. Thus, over-heating caused the long-range molecular order and amylopectin branches of starch to be better preserved in the Y22-starch mixture (Y22-S) than in the Y16-starch mixture (Y16-S). Meanwhile, the starch’s degradation pattern during heating in turn influenced the polymerization of both glutens. During heating, residual amylopectin branching points restricted the aggregation and cross-linking of gluten proteins due to steric hindrance. More intense interaction between Y16 and starch during heating mitigated the steric hindrance in starch–gluten networks, which was due to more residual short-range ordered starch and hydrogen bonds involved in the formation of starch–gluten networks in Y16-S during heating.
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Wieser, Herbert. "Chemistry of gluten proteins." Food Microbiology 24, no. 2 (2007): 115–19. http://dx.doi.org/10.1016/j.fm.2006.07.004.
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Ortolan, Fernanda, Karoline Urbano, and Caroline Joy Steel. "Simple tests as tools for vital wheat gluten evaluation." British Food Journal 120, no. 7 (2018): 1590–99. http://dx.doi.org/10.1108/bfj-06-2017-0356.
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Purpose The purpose of this paper is to evaluate the viscoelastic quality of commercial vital wheat glutens from different origins (A and B) through simple tests, and correlate these results with dough rheological parameters measured using more complex equipment (farinograph and extensograph) and with bread quality characteristics (specific volume and crumb firmness) obtained from wheat flour fortified with 7 g/100 g of vital gluten. Design/methodology/approach For the evaluation of vital gluten quality, two commercial vital wheat gluten named A and B were used. The simple tests performed with these samples were wet and dry gluten contents and index gluten, extensbility test and expansion test. The Pearson correlation was performed among data from dough rheological tests (farinograph and extensograph) and bread quality parameters (specific volume (SV) and crumb firmness) obtained from the fortification of wheat flour with 7 g/100 g of VGA or VGB (previous work, data not shown). Findings The simple tests showed differences in the viscoelastic properties of vital gluten A and B; vital gluten A presented higher elasticity and lower extensibility than vital gluten B, and the gluten ball of sample A presented higher SV. By correlation analysis, it was verified that the simple tests studied may be useful to assess the baking performance of commercial vital gluten when this product is added to wheat flour for its fortification. Furthermore, the results indicate the need for more information on vital wheat gluten proteins for its commercialisation and use. Originality/value This work is very important, not just for the scientific community, but also for the bakery industry, that requires more information about vital wheat gluten before its use in bread making. As there are great differences in the protein quality of commercial vital wheat glutens and their functionality, the study was developed to solve this problem.
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Skendi, Adriana, Maria Papageorgiou, and Theodoros Varzakas. "High Protein Substitutes for Gluten in Gluten-Free Bread." Foods 10, no. 9 (2021): 1997. http://dx.doi.org/10.3390/foods10091997.
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Gluten-free products have come into the market in order to alleviate health problems such as celiac disease. In this review, recent advances in gluten-free bread are described along with plant-based gluten-free proteins. A comparison with animal-based gluten-free proteins is made reporting on different high protein sources of animal origin. Sea microorganisms- and insect-based proteins are also mentioned, and the optimization of the structure of gluten-free bread with added high protein sources is highlighted along with protein digestibility issues. The latter is an issue for consideration that can be manipulated by a careful design of the mixture in terms of phenolic compounds, soluble carbohydrates and fibres, but also the baking process itself. Additionally, the presence of enzymes and different hydrocolloids are key factors controlling quality features of the final product.
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Kharrazian, Datis. "Gluten Ataxia Associated with Dietary Protein Cross-Reactivity with GAD-65." Reports — Medical Cases, Images, and Videos 3, no. 3 (2020): 24. http://dx.doi.org/10.3390/reports3030024.
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Cross-reactivity occurs when antibodies formed against an antigen have amino acid sequence homology with another target protein. This allows antibodies formed against the antigen to also bind to similar proteins that share structural similarity. Autoimmune reactions to gluten can lead to sporadic ataxia in susceptible genotypes due to cross-reactivity. With gluten ataxia, dietary consumption of gluten proteins induce immunological cross-reactivity with glutamic-acid decarboxylase-65 (GAD-65) target proteins found in the cerebellum. Implementation of a strict gluten-free diet has been shown to improve the expression of this form of ataxia with most patients in this subgroup. However, there are some subjects that have limited clinical responses to only a strict gluten-free diet. Dietary protein cross-reactivity to other food proteins, besides gluten, that also share structural similarity to GAD-65 may also play a role in this reaction. In this case report, we report of a patient suffering from gluten-ataxia in which a gluten-free diet alone did not generate significant clinical outcomes until other foods that cross-react with GAD-65 were also removed from their diet.
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Mariann Móré, Zoltán Győri, and Péter Sipos. "The relationship between gluten proteins and baking quality." Acta Agraria Debreceniensis, no. 48 (July 31, 2012): 117–22. http://dx.doi.org/10.34101/actaagrar/48/2465.
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Wheat, one of the most important cereals, is grown on the largest area in Hungary. During hydration of storage proteins of wheat – gliadin and glutenin – the gluten complex is evolved. The gliadin is responsible for the extensibility of gluten complex as well as the glutenin for the strength of gluten. The structure, composition and rheological properties of gluten proteins influence significantly the baking quality. The gliadin/glutenin ratio and the quality and structure of glutenin fraction play the most important role in evolving gluten complex. Changes in the steps of breadmaking technology also have effect on the quality of product. Several tests proved that the higher glutenin content increases the strength of dough while the higher gliadin content increases the extensibility of dough and decreases maximum resistance to extension. The monomer gliadins play a great part in plasticity of glutenin polymer. The quality of glutenin fraction significantly influences the evolving gluten complex, because of the spiral structure of glutenin which deforms under stress conditions, then the β-spiral structure resumes their original conformation by releasing from stress.The final quality of product evolves as a result of complex characteristics of wheat proteins, so detailed knowledge on the roles of different protein compounds is the base of the quality oriented product development.
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Van Buiten, Charlene B., and Ryan J. Elias. "Gliadin Sequestration as a Novel Therapy for Celiac Disease: A Prospective Application for Polyphenols." International Journal of Molecular Sciences 22, no. 2 (2021): 595. http://dx.doi.org/10.3390/ijms22020595.
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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.
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Van Buiten, Charlene B., and Ryan J. Elias. "Gliadin Sequestration as a Novel Therapy for Celiac Disease: A Prospective Application for Polyphenols." International Journal of Molecular Sciences 22, no. 2 (2021): 595. http://dx.doi.org/10.3390/ijms22020595.
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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.
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Marcela, Sluková, Levková Julie, Michalcová Alena, Horáčková Šárka, and Skřivan Pavel. "Effect of the dough mixing process on the quality of wheat and buckwheat proteins." Czech Journal of Food Sciences 35, No. 6 (2017): 522–31. http://dx.doi.org/10.17221/220/2017-cjfs.
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The changes in the structure of cereal proteins during the mixing of flour into dough was described and evaluated. Wheat gliadins and glutenins (gluten proteins) have unique physical properties and play an important role in breadmaking. The effect of mixing time on the formation and the structure of the gluten network was determined using scanning electron microscopy (SEM). Buckwheat flour (gluten-free) was used to compare the development of structure during the mixing process.
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Gibson, Peter R., Jane G. Muir, and Evan D. Newnham. "Other Dietary Confounders: FODMAPS et al." Digestive Diseases 33, no. 2 (2015): 269–76. http://dx.doi.org/10.1159/000371401.
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Background: While it is well documented and widely appreciated that ingestion of wheat (and less so rye and barley) is associated with gastrointestinal symptoms such as bloating or abdominal pain, the component of wheat to which such an effect is attributed is less well established. Key Messages: Wheat is a complex of proteins (80% gluten, 20% metabolic proteins), carbohydrates (starch, non-starch polysaccharides, fructans), lipids and other components. The majority of attention has focused on gluten as the culprit in triggering symptoms, but re-challenge studies have nearly all used wheat flour-related products (such as bread) as the stimulus. When carbohydrate-deplete gluten was used as the challenge agent, gluten-specific feelings of depression and not gut symptoms were observed in those who fulfilled strict criteria of ‘non-coeliac gluten sensitivity', thereby underlining the complexity of cereals and of undertaking research in this area. Candidate components other than gluten include poorly absorbed oligosaccharides (mainly fructans), non-gluten wheat proteins such as amylase-trypsin inhibitors or wheat germ agglutinin, and exorphins released during the digestion of gluten. Specific biological and/or clinical effects associated with gluten-free diets or wheat ingestion need to be carefully dissected before attribution to gluten can be claimed. Conclusions: Currently, coeliac disease is the only common condition that has been unequivocally linked to gluten. Inaccurate attribution will be associated with suboptimal therapeutic advice and at least partly underlies the current gluten-free epidemic gripping the Western world.
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Ziobro, Rafał, Lesław Juszczak, Mariusz Witczak, and Jarosław Korus. "Non-gluten proteins as structure forming agents in gluten free bread." Journal of Food Science and Technology 53, no. 1 (2015): 571–80. http://dx.doi.org/10.1007/s13197-015-2043-5.
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Krupa-Kozak, U., M. Wronkowska, and M. Soral-Śmietana. "Effect of buckwheat flour on microelements and proteins contents in gluten-free bread." Czech Journal of Food Sciences 29, No. 2 (2011): 103–8. http://dx.doi.org/10.17221/136/2010-cjfs.
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Coeliac disease is an autoimmune gluten-sensitive entheropathy. The only available treatment for it is the life-long adherence to a gluten-free diet although these products are often poor in proteins, minerals, and vitamins. The current study was designed to investigate the effect of buckwheat flour incorporation to a gluten-free experimental formulation on the size-related parameters, and microelements and proteins contents. Buckwheat flour affected positively the technological quality of bread, like bread specific volume index and loaf size. Increasing concentration of buckwheat flour (10–40%) in bread affected the proportional enrichment in proteins and microelements, especially in copper and manganese.
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Vader, L. Willemijn, Arnoud de Ru, Yvonne van der Wal, et al. "Specificity of Tissue Transglutaminase Explains Cereal Toxicity in Celiac Disease." Journal of Experimental Medicine 195, no. 5 (2002): 643–49. http://dx.doi.org/10.1084/jem.20012028.
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Celiac disease is caused by a selective lack of T cell tolerance for gluten. It is known that the enzyme tissue transglutaminase (tTG) is involved in the generation of T cell stimulatory gluten peptides through deamidation of glutamine, the most abundant amino acid in gluten. Only particular glutamine residues, however, are modified by tTG. Here we provide evidence that the spacing between glutamine and proline, the second most abundant amino acid in gluten, plays an essential role in the specificity of deamidation. On the basis of this, algorithms were designed and used to successfully predict novel T cell stimulatory peptides in gluten. Strikingly, these algorithms identified many similar peptides in the gluten-like hordeins from barley and secalins from rye but not in the avenins from oats. The avenins contain significantly lower percentages of proline residues, which offers a likely explanation for the lack of toxicity of oats. Thus, the unique amino acid composition of gluten and related proteins in barley and rye favors the generation of toxic T cell stimulatory gluten peptides by tTG. This provides a rationale for the observation that celiac disease patients are intolerant to these cereal proteins but not to other common food proteins.
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L. Shan and C. Khosla. "Chemistry and Biology of Gluten Proteins." Immunology, Endocrine & Metabolic Agents in Medicinal Chemistry 7, no. 3 (2007): 187–93. http://dx.doi.org/10.2174/187152207780832397.
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Shewry, P. R., and A. S. Tatham. "Disulphide Bonds in Wheat Gluten Proteins." Journal of Cereal Science 25, no. 3 (1997): 207–27. http://dx.doi.org/10.1006/jcrs.1996.0100.
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Kõiv, Viia, and Tanel Tenson. "Gluten-degrading bacteria: availability and applications." Applied Microbiology and Biotechnology 105, no. 8 (2021): 3045–59. http://dx.doi.org/10.1007/s00253-021-11263-5.
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Abstract Gluten is a mixture of storage proteins in wheat and occurs in smaller amounts in other cereal grains. It provides favorable structure to bakery products but unfortunately causes disease conditions with increasing prevalence. In the human gastrointestinal tract, gluten is cleaved into proline and gluten rich peptides that are not degraded further. These peptides trigger immune responses that might lead to celiac disease, wheat allergy, and non-celiac gluten sensitivity. The main treatment option is a gluten-free diet. Alternatively, using enzymes or microorganisms with gluten-degrading properties might alleviate the disease. These components can be used during food production or could be introduced into the digestive tract as food supplements. In addition, natural food from the environment is known to enrich the microbial communities in gut and natural environmental microbial communities have high potential to degrade gluten. It remains to be investigated if food and environment-induced changes in the gut microbiome could contribute to the triggering of gluten-related diseases. Key points • Wheat proteins, gluten, are incompletely digested in human digestive tract leading to gluten intolerance. • The only efficient treatment of gluten intolerance is life-long gluten-free diet. • Environmental bacteria acquired together with food could be source of gluten-degrading bacteria detoxifying undigested gluten peptides.
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Gabler, Angelika Miriam, and Katharina Anne Scherf. "Comparative Characterization of Gluten and Hydrolyzed Wheat Proteins." Biomolecules 10, no. 9 (2020): 1227. http://dx.doi.org/10.3390/biom10091227.
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Hydrolyzed wheat proteins (HWPs) are widely used as functional ingredients in foods and cosmetics, because of their emulsifying and foaming properties. However, in individuals suffering from celiac disease or wheat allergy, HWPs may have a modified immunoreactivity compared to native gluten due to changes in molecular structures. Although a variety of HWPs are commercially available, there are no in-depth comparative studies that characterize the relative molecular mass (Mr) distribution, solubility, and hydrophilicity/hydrophobicity of HWPs compared to native gluten. Therefore, we aimed to fill this gap by studying the above characteristics of different commercial HWP and gluten samples. Up to 100% of the peptides/proteins in the HWP were soluble in aqueous solution, compared to about 3% in native gluten. Analysis of the Mr distribution indicated that HWPs contained high percentages of low-molecular-weight peptides/proteins and also deamidated glutamine residues. We also found considerable differences between the seven HWPs studied, so that each HWP needs to be studied in detail to help explain its potential immunoreactivity.
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Lei, Duo, and Xiaojun Ma. "Effect of enzymatic glycosylation on the structure and properties of wheat gluten protein fibers." Journal of Engineered Fibers and Fabrics 16 (January 2021): 155892502110003. http://dx.doi.org/10.1177/15589250211000337.
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Wheat gluten proteins are good raw materials for preparing fibers due to their excellent viscoelasticity. However, protein fibers made directly from wheat gluten have poor mechanical properties. In this paper, transglutaminase was used to induce the glycosylation reaction between wheat gluten proteins and carboxymethyl chitosan. The glycated proteins were then made into fibers by wet spinning. After glycosylation modification, the breaking strength and breaking elongation of the wheat gluten protein fibers (WGPF) improved by 43% and 127%, respectively. Fourier transform infrared spectroscopy and sodium dodecyl sulfate-polyacrylamide gel electrophoresis analyses revealed that the glycosylation-modified WGPF molecules contained saccharide portions, which confirms the covalent attachment of carboxymethyl chitosan to the wheat gluten protein. Scanning electron microscopy showed that the number of pores in the cross-section of the modified WGPF was lower than that in the unmodified WGPF. The thermal stability and dyeability of the modified WGPF were also improved.
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& Nasser, Jasim. "FUNCTIONAL PROPERTIES OF ENZYMETICALLY MODIFIED WHEAT GLUTEN." IRAQI JOURNAL OF AGRICULTURAL SCIENCES 51, no. 3 (2020): 777–88. http://dx.doi.org/10.36103/ijas.v51i3.1033.
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This study was aimed to investigate the potentiality of gluten inclusion into functional foods. The effect of controlled enzymatic hydrolysis on the antioxidant properties of Pepsin, Trypsin, and Papain-assisted wheat gluten hydrolysates have been studied. Lyophilized and dried gluten from durum wheat, commercial durum gluten, and whey proteins were enzymatically hydrolyzed. Based on the antioxidant activity of the obtained hydrolysates, papain hydrolyzed gluten was selected for this study. Functional properties (water holding capacity, emulsifying capacity and stability, foam formation and stability, protein solubility, and oil binding capacity) were investigated for the selected samples. Results revealed that the enzymatic modification improved the functional properties of all selected proteins significantly (P<0.05), with the superiority of the lyophilized and dried wheat gluten in some functional properties especially in alkaline pH and pH 4.
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Sharma, Girdhari M. "Immunoreactivity and Detection of Wheat Proteins by Commercial ELISA Kits." Journal of AOAC INTERNATIONAL 95, no. 2 (2012): 364–71. http://dx.doi.org/10.5740/jaoacint.sge_sharma.
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Abstract Wheat proteins are responsible for sensitivities, including baker's asthma, immunoglobulin E (IgE)-mediated allergic reaction, wheat-dependent, exercise-induced anaphylaxis, and celiac disease. The detection of gluten/wheat traces in foods is important to safeguard the health of wheat-sensitive individuals and comply with food labeling. Many immunoanalytical-based commercial kits are available for the quantification of gliadin/gluten/wheat proteins. We compared the immunoreactivity of wheat fractions with wheat-allergic human serum IgE and antibody conjugates used in six commercial immunoassay kits. Moreover, the performance of the kits was tested using corn flour spiked with gluten (5, 10, 25, and 50 ppm) and wheat flour (50, 100, 250, and 500 ppm). The albumin, globulin, gliadin, and glutenin fractions reacted with IgE from nine, eight, two, and eight patients' sera, respectively, out of nine wheat allergic patients tested. Among the antibodies from commercial kits, those from R-Biopharm, Morinaga, and Romer Labs reacted strongly with the gliadin fraction, whereas those from BioKits, ALLERTEK, and ELISA Systems reacted strongly with the glutenin fraction. All kits showed minimal or no reactivity with albumin and globulin fractions. All kits detected the gluten and wheat flour in a corn flour matrix at the lowest spiked levels of 5 and 50 ppm, respectively. However, there was wide variation among the kits when comparing the recovery of gluten and wheat flour. The recovery was also dependent on the source material (gluten or wheat flour) used for spiking the corn flour matrix.
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JOHANSSON, E., M. L. PRIETO-LINDE, G. SVENSSON, and J. Ö. JÖNSSON. "Influences of cultivar, cultivation year and fertilizer rate on amount of protein groups and amount and size distribution of mono- and polymeric proteins in wheat." Journal of Agricultural Science 140, no. 3 (2003): 275–84. http://dx.doi.org/10.1017/s0021859603003162.
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Influences of cultivar and environment, i.e. cultivation year and fertilizer rate, on amount of protein groups and amount and size distribution of mono- and polymeric proteins, were investigated in four sets of wheat (Triticum aestivum L.). The cultivars were chosen in order to obtain a high range of variation in protein concentration and gluten strength. Environmental influences on protein concentration and gluten strength were investigated, as well as relations between variation in protein concentration and gluten strength and variation in protein groups and amount and size distribution of mono- and polymeric proteins.The results showed that cultivar and environmental influences giving rise to variation in protein concentration also gave rise to variation in most of the investigated protein components. Protein concentration was significantly positively correlated to the total amounts of glutenins and gliadins and amounts of most mono- and polymeric proteins. However, the correlation with the amount of gliadins and sodium dodecyl sulphate (SDS)-soluble mono- and polymeric proteins were often higher than the correlation to the glutenins and the SDS-insoluble mono- and polymeric proteins. Cultivar influences giving rise to variation in gluten strength were found to influence the relation between SDS-soluble and -insoluble polymeric proteins, leading to a significant positive correlation between the gluten strength and the percentage of total unextractable polymeric protein (TUPP) in the total polymeric protein and large unextractable polymeric protein (LUPP) in the total large polymeric protein. Environmental variation in gluten strength was found to be significantly positively correlated to SDS-insoluble proteins and negatively correlated to SDS-soluble proteins. This also led to a significant positive correlation with the percentage of LUPP and/or TUPP.
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Banc, A., C. Charbonneau, M. Dahesh, et al. "Small angle neutron scattering contrast variation reveals heterogeneities of interactions in protein gels." Soft Matter 12, no. 24 (2016): 5340–52. http://dx.doi.org/10.1039/c6sm00710d.
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The SANS analysis of gluten gels prepared with deuterated solvent evidences the formation of large scale zones enriched in protonated proteins. The formation of these zones is associated to the heterogeneities of interaction between the different gluten proteins and the solvent.
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Caputo, Ivana, Marilena Lepretti, Stefania Martucciello, and Carla Esposito. "Enzymatic Strategies to Detoxify Gluten: Implications for Celiac Disease." Enzyme Research 2010 (October 7, 2010): 1–9. http://dx.doi.org/10.4061/2010/174354.
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Celiac disease is a permanent intolerance to the gliadin fraction of wheat gluten and to similar barley and rye proteins that occurs in genetically susceptible subjects. After ingestion, degraded gluten proteins reach the small intestine and trigger an inappropriate T cell-mediated immune response, which can result in intestinal mucosal inflammation and extraintestinal manifestations. To date, no pharmacological treatment is available to gluten-intolerant patients, and a strict, life-long gluten-free diet is the only safe and efficient treatment available. Inevitably, this may produce considerable psychological, emotional, and economic stress. Therefore, the scientific community is very interested in establishing alternative or adjunctive treatments. Attractive and novel forms of therapy include strategies to eliminate detrimental gluten peptides from the celiac diet so that the immunogenic effect of the gluten epitopes can be neutralized, as well as strategies to block the gluten-induced inflammatory response. In the present paper, we review recent developments in the use of enzymes as additives or as processing aids in the food biotechnology industry to detoxify gluten.
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Cui, Tingting, Rui Liu, Tao Wu, Wenjie Sui, and Min Zhang. "Influence of Konjac Glucomannan and Frozen Storage on Rheological and Tensile Properties of Frozen Dough." Polymers 11, no. 5 (2019): 794. http://dx.doi.org/10.3390/polym11050794.
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The impact of various amounts of konjac glucomannan on the structural and physicochemical properties of gluten proteins/dough at different periods of frozen storage is evaluated in the present study. As frozen storage time was prolonged, the molecular weight and the free sulfhydryl content of gluten proteins and the tensile properties of frozen dough all decreased. The addition of konjac glucomannan reduced the variations in the structural and rheological properties of gluten proteins/dough. Frozen dough with 2.5% added konjac glucomannan showed the highest water binding capacity and retarded the migration of water. Scanning electron microscopy and differential scanning calorimetry results also revealed that adding konjac glucomannan reduced the cracks and holes in the dough and enhanced its thermal stability. The correlations between mechanical characteristics and structure parameters further indicated that konjac glucomannan could not only stabilize the structures of gluten proteins but also bind free water to form more stable complexes, thereby retaining the rheological and tensile properties of the frozen dough.
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Sabença, Carolina, Miguel Ribeiro, Telma de Sousa, Patrícia Poeta, Ana Sofia Bagulho, and Gilberto Igrejas. "Wheat/Gluten-Related Disorders and Gluten-Free Diet Misconceptions: A Review." Foods 10, no. 8 (2021): 1765. http://dx.doi.org/10.3390/foods10081765.
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In the last 10,000 years, wheat has become one of the most important cereals in the human diet and today, it is widely consumed in many processed food products. Mostly considered a source of energy, wheat also contains other essential nutrients, including fiber, proteins, and minor components, such as phytochemicals, vitamins, lipids, and minerals, that together promote a healthy diet. Apart from its nutritional properties, wheat has a set of proteins, the gluten, which confer key technical properties, but also trigger severe immune-mediated diseases, such as celiac disease. We are currently witnessing a rise in the number of people adhering to gluten-free diets unwarranted by any medical need. In this dynamic context, this review aims to critically discuss the nutritional components of wheat, highlighting both the health benefits and wheat/gluten-related disorders, in order to address common misconceptions associated with wheat consumption.
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Jin, Hua Li, Jin Shui Wang, and Ke Bian. "Characteristics of Enzymatic Hydrolysis of the Wheat Gluten Proteins Treated by Ultrasound Wave." Advanced Materials Research 343-344 (September 2011): 1015–22. http://dx.doi.org/10.4028/www.scientific.net/amr.343-344.1015.
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Effects of sonication at 150W and 300W power output on hydrolysis of wheat gluten using two proteinases (Protamex and papain) were evaluated in the present study. Sonication resulted in the increase in amounts of free sulphydryl (SH) of wheat gluten. Significant (P < 0.05) increase in SH contents at 300W power output was found compared with the control and those samples sonicated at 150W power output. Degree of hydrolysis (DH) and protein recovery (PR) of the wheat gluten hydrolysates increased with sonication time and power output. Significant (P < 0.05) increase in DH and PR of the wheat gluten hydrolysate from the sample sonicated by 300W power output was found compared to those sonicated by 150W output. Sonication caused the decrease in the relative percent of the large peptide fractions and increase in the relative percent of the small peptide fractions in the hydrolysates compared to the control. Structure change in insoluble wheat gluten proteins was the principal reason of improvement in their characteristics of enzymatic hydrolysis.
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Haro, Carmen, María H. Guzmán-López, Miriam Marín-Sanz, et al. "Consumption of Tritordeum Bread Reduces Immunogenic Gluten Intake without Altering the Gut Microbiota." Foods 11, no. 10 (2022): 1439. http://dx.doi.org/10.3390/foods11101439.
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Gluten proteins are responsible for the wheat breadmaking quality. However, gluten is also related to human pathologies for which the only treatment is a gluten-free diet (GFD). GFD has gained popularity among individuals who want to reduce their gluten intake. Tritordeum is a cereal species that originated after crossing durum wheat with wild barley and differs from bread wheat in its gluten composition. In this work, we have characterized the immunogenic epitopes of tritordeum bread and results from a four-phase study with healthy adults for preferences of bread and alterations in the gut microbiota after consuming wheat bread, gluten-free bread, and tritordeum bread are reported. Tritordeum presented fewer peptides related to gluten proteins, CD-epitopes, and IgE binding sites than bread wheat. Participants rated tritordeum bread higher than gluten-free bread. Gut microbiota analysis revealed that the adherence to a strict GFD involves some minor changes, especially altering the species producing short-chain fatty acids. However, the short-term consumption of tritordeum bread does not induce significant changes in the diversity or community composition of the intestinal microbiota in healthy individuals. Therefore, tritordeum bread could be an alternative for healthy individuals without wheat-related pathologies who want to reduce their gluten consumption without harming their gut health.
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Lundin, K. E., H. Scott, T. Hansen, et al. "Gliadin-specific, HLA-DQ(alpha 1*0501,beta 1*0201) restricted T cells isolated from the small intestinal mucosa of celiac disease patients." Journal of Experimental Medicine 178, no. 1 (1993): 187–96. http://dx.doi.org/10.1084/jem.178.1.187.
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Celiac disease (CD) is most probably an immunological disease, precipitated in susceptible individuals by ingestion of wheat gliadin and related proteins from other cereals. The disease shows a strong human HLA association predominantly to the cis or trans encoded HLA-DQ(alpha 1*0501,beta 1*0201) (DQ2) heterodimer. T cell recognition of gliadin presented by this DQ heterodimer may thus be of immunopathogenic importance in CD. We therefore challenged small intestinal biopsies from adult CD patients on a gluten-free diet in vitro with gluten (containing both gliadin and other wheat proteins), and isolated activated CD25+ T cells. Polyclonal T cell lines and a panel of T cell clones recognizing gluten were established. They recognized the gliadin moiety of gluten, but not proteins from other cereals. Inhibition studies with anti-HLA antibodies demonstrated predominant antigen presentation by HLA-DQ molecules. The main antigen-presenting molecule was established to be the CD-associated DQ(alpha 1*0501, beta 1*0201) heterodimer. The gluten-reactive T cell clones were CD4+, CD8-, and carried diverse combinations of T cell receptor (TCR) V alpha and V beta chains. The findings suggest preferential mucosal presentation of gluten-derived peptides by HLA-DQ(alpha 1*0501, beta 1*0201) in CD, which may explain the HLA association.
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Gojkovic Cvjetkovic, Vesna S., Dragana M. Skuletic, Zeljka R. Marjanovic-Balaban, Dragan P. Vujadinovic, Danijela Z. Rajic, and Vladimir M. Tomovic. "Gliadin Proteins in Muffins with Quinoa Flour." Food Processing: Techniques and Technology 54, no. 1 (2024): 82–92. http://dx.doi.org/10.21603/2074-9414-2024-1-2490.
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Partial replacement of wheat flour in foodstuffs is of great importance in the food industry. Muffins are a type of semi-sweet cake that is traditionally made from wheat flour. They are especially favored by children and senior citizens. Muffins have a long shelf life, which also contributes to their popularity. However, gluten, the main protein in wheat flour, is commonly associated with celiac disease. Gluten consists of two fractions: gliadins and glutenins.
 In this experiment, the original muffins contained 100% wheat flour. Then, we replaced a portion of wheat flour with 25, 50, and 75% quinoa flour. The samples were stored for 0, 2, and 4 weeks. After that, gliadin proteins were extracted with 70% (v/v) ethanol. We separated gliadin using a high-performance liquid chromatograph (Agilent Technologies 1260 Infinity, USA) and measured the total amount of gliadin protein and the amount of gliadin proteins per fraction. The absorbance tests were conducted at 210 nm. 
 The gliadin protein content was significantly reduced to the wheat vs. quinoa ratio of 50:50 because quinoa is gluten-free, even though it is rich in protein. During the storage time of 0, 2, and 4 weeks, the protein content fell down in the samples with the wheat vs. quinoa ratios of 100:0, 75:25, and 50:50. However, the muffins with 25% wheat flour and 75% quinoa demonstrated an increase in gliadin content. 
 The results obtained could be a good starting point for the development of high-fiber, gluten-free, and more nutritionally valuable muffins.
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Shewry, P. R., N. G. Halford, P. S. Belton, and A. S. Tatham. "The structure and properties of gluten: an elastic protein from wheat grain." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 357, no. 1418 (2002): 133–42. http://dx.doi.org/10.1098/rstb.2001.1024.
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The wheat gluten proteins correspond to the major storage proteins that are deposited in the starchy endosperm cells of the developing grain. These form a continuous proteinaceous matrix in the cells of the mature dry grain and are brought together to form a continuous viscoelastic network when flour is mixed with water to form dough. These viscoelastic properties underpin the utilization of wheat to give bread and other processed foods. One group of gluten proteins, the HMM subunits of glutenin, is particularly important in conferring high levels of elasticity (i.e. dough strength). These proteins are present in HMM polymers that are stabilized by disulphide bonds and are considered to form the ‘elastic backbone’ of gluten. However, the glutamine–rich repetitive sequences that comprise the central parts of the HMM subunits also form extensive arrays of interchain hydrogen bonds that may contribute to the elastic properties via a ‘loop and train’ mechanism. Genetic engineering can be used to manipulate the amount and composition of the HMM subunits, leading to either increased dough strength or to more drastic changes in gluten structure and properties.
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Li, Bose, Stockwell, Howitt, and Colgrave. "Assessing the Utility of Multiplexed Liquid Chromatography-Mass Spectrometry for Gluten Detection in Australian Breakfast Food Products." Molecules 24, no. 20 (2019): 3665. http://dx.doi.org/10.3390/molecules24203665.
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Coeliac disease (CD) is an autoimmune disorder triggered by the ingestion of gluten that is associated with gastrointestinal issues, including diarrhea, abdominal pain, and malabsorption. Gluten is a general name for a class of cereal storage proteins of wheat, barley, and rye that are notably resistant to gastrointestinal digestion. After ingestion, immunogenic peptides are subsequently recognized by T cells in the gastrointestinal tract. The only treatment for CD is a life-long gluten-free diet. As such, it is critical to detect gluten in diverse food types, including those where one would not expect to find gluten. The utility of liquid chromatography-mass spectrometry (LC-MS) using cereal-specific peptide markers to detect gluten in heavily processed food types was assessed. A range of breakfast products, including breakfast cereals, breakfast bars, milk-based breakfast drinks, powdered drinks, and a savory spread, were tested. No gluten was detected by LC-MS in the food products labeled gluten-free, yet enzyme-linked immunosorbent assay (ELISA) measurement revealed inconsistencies in barley-containing products. In products containing wheat, rye, barley, and oats as labeled ingredients, gluten proteins were readily detected using discovery proteomics. Panels comprising ten cereal-specific peptide markers were analyzed by targeted proteomics, providing evidence that LC-MS could detect and differentiate gluten in complex matrices, including baked goods and milk-based products.
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Marjanović-Balaban, Željka, Vesna Gojković Cvjetković, and Radoslav Grujić. "Gliadin proteins from wheat flour: the optimal determination conditions by ELISA." Foods and Raw Materials 9, no. 2 (2021): 364–70. http://dx.doi.org/10.21603/2308-4057-2021-2-364-370.
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Introduction. The number of people with celiac disease is rapidly increasing. Gluten, is one of the most common food allergens, consists of two fractions: gliadins and glutenins. The research objective was to determine the optimal conditions for estimating gliadins by using enzyme-linked immunosorbent assay (ELISA). 
 Study objects and methods. The experiment involved wheat flour samples (0.10; 0.20, 0.25, 0.50, and 1.0 g) suspended in different solvents (ethanol, methanol, 1-propanol, and isopropanol) of different concentrations (40, 50, 60, 70, 80, and 90% v/v). The samples were diluted with Tris buffer in ratios of 1:50, 1:100, 1:150, and 1:200. The gliadin test was performed using a Gliadin/Gluten Biotech commercial ELISA kit (Immunolab).
 Results and discussion. The optimal conditions for determining gliadin proteins that provided the highest gliadin concentration were: solvent – 70% v/v ethanol, extract:Tris buffer ratio – 1:50, and sample weight – 1.0 g. 
 Conclusion. The obtained results can be of great importance to determine gliadin/gluten concentrations in food products by rapid analysis methods.
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Riefolo, C., D. Ficco, L. Cattivelli, and P. Vita. "Genetic diversity of gluten proteins inT. turgidumL." Cereal Research Communications 39, no. 3 (2011): 405–14. http://dx.doi.org/10.1556/crc.39.2011.3.10.
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Ribotta, P. D., S. F. Ausar, D. M. Beltramo, and A. E. León. "Interactions of hydrocolloids and sonicated-gluten proteins." Food Hydrocolloids 19, no. 1 (2005): 93–99. http://dx.doi.org/10.1016/j.foodhyd.2004.04.018.
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Lee, Ga-Yang, Min-Jeong Jung, Byoung-Mok Kim, and Joon-Young Jun. "Identification and Growth Characteristics of a Gluten-Degrading Bacterium from Wheat Grains for Gluten-Degrading Enzyme Production." Microorganisms 11, no. 12 (2023): 2884. http://dx.doi.org/10.3390/microorganisms11122884.
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Immunogenic peptides from wheat gluten can be produced during digestion, which are difficult to digest by gastrointestinal proteases and negatively affect immune responses in humans. Gluten intolerance is a problem in countries where wheat is a staple food, and a gluten-free diet is commonly recommended for its treatment and prevention. Enzyme approaches for degradation of the peptides can be considered as a strategy for its prevention. Here, we isolated a gluten-degrading bacterium, Bacillus amyloliquefaciens subsp. plantarum, from wheat grains. The culture conditions for enzyme production or microbial use were considered based on gluten decomposition patterns. Additionally, the pH range for the activity of the crude enzyme was investigated. The bacterium production of gluten-degrading enzymes was temperature-dependent within 25 °C to 45 °C, and the production time decreased with increasing culture temperature. However, it was markedly decreased with increasing biofilm formation. The bacterium decomposed high-molecular-weight glutenin proteins first, followed by gliadin proteins, regardless of the culture temperature. Western blotting with an anti-gliadin antibody revealed that the bacterium decomposed immunogenic proteins related to α/β-gliadins. The crude enzyme was active in the pH ranges of 5 to 8, and enzyme production was increased by adding gliadin into the culture medium. In this study, the potential of the B. amyloliquefaciens subsp. plantarum for gluten-degrading enzyme production was demonstrated. If further studies for purification of the enzyme specific to the immunogenic peptides and its characteristics are conducted, it may contribute as a strategy for prevention of gluten intolerance.
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Caminero, Alberto, Esther Nistal, Alexandra R. Herrán, et al. "Differences in gluten metabolism among healthy volunteers, coeliac disease patients and first-degree relatives." British Journal of Nutrition 114, no. 8 (2015): 1157–67. http://dx.doi.org/10.1017/s0007114515002767.
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AbstractCoeliac disease (CD) is an immune-mediated enteropathy resulting from exposure to gluten in genetically predisposed individuals. Gluten proteins are partially digested by human proteases generating immunogenic peptides that cause inflammation in patients carrying HLA-DQ2 and DQ8 genes. Although intestinal dysbiosis has been associated with patients with CD, bacterial metabolism of gluten has not been studied in depth thus far. The aim of this study was to analyse the metabolic activity of intestinal bacteria associated with gluten intake in healthy individuals, CD patients and first-degree relatives of CD patients. Faecal samples belonging to twenty-two untreated CD patients, twenty treated CD patients, sixteen healthy volunteers on normal diet, eleven healthy volunteers on gluten-free diet (GFD), seventy-one relatives of CD patients on normal diet and sixty-nine relatives on GFD were tested for several proteolytic activities, cultivable bacteria involved in gluten metabolism, SCFA and the amount of gluten in faeces. We detected faecal peptidasic activity against the gluten-derived peptide 33-mer. CD patients showed differences in faecal glutenasic activity (FGA), faecal tryptic activity (FTA), SCFA and faecal gluten content with respect to healthy volunteers. Alterations in specific bacterial groups metabolising gluten such as Clostridium or Lactobacillus were reported in CD patients. Relatives showed similar parameters to CD patients (SCFA) and healthy volunteers (FTA and FGA). Our data support the fact that commensal microbial activity is an important factor in the metabolism of gluten proteins and that this activity is altered in CD patients.
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Kłosok, Konrad, Renata Welc, Emilia Fornal, and Agnieszka Nawrocka. "Effects of Physical and Chemical Factors on the Structure of Gluten, Gliadins and Glutenins as Studied with Spectroscopic Methods." Molecules 26, no. 2 (2021): 508. http://dx.doi.org/10.3390/molecules26020508.
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This review presents applications of spectroscopic methods, infrared and Raman spectroscopies in the studies of the structure of gluten network and gluten proteins (gliadins and glutenins). Both methods provide complimentary information on the secondary and tertiary structure of the proteins including analysis of amide I and III bands, conformation of disulphide bridges, behaviour of tyrosine and tryptophan residues, and water populations. Changes in the gluten structure can be studied as an effect of dough mixing in different conditions (e.g., hydration level, temperature), dough freezing and frozen storage as well as addition of different compounds to the dough (e.g., dough improvers, dietary fibre preparations, polysaccharides and polyphenols). Additionally, effect of above mentioned factors can be determined in a common wheat dough, model dough (prepared from reconstituted flour containing only wheat starch and wheat gluten), gluten dough (lack of starch), and in gliadins and glutenins. The samples were studied in the hydrated state, in the form of powder, film or in solution. Analysis of the studies presented in this review indicates that an adequate amount of water is a critical factor affecting gluten structure.
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Tian, Na, Daniel A. Leffler, Ciaran P. Kelly, et al. "Despite sequence homologies to gluten, salivary proline-rich proteins do not elicit immune responses central to the pathogenesis of celiac disease." American Journal of Physiology-Gastrointestinal and Liver Physiology 309, no. 11 (2015): G910—G917. http://dx.doi.org/10.1152/ajpgi.00157.2015.
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Celiac disease (CD) is an inflammatory disorder triggered by ingested gluten, causing immune-mediated damage to the small-intestinal mucosa. Gluten proteins are strikingly similar in amino acid composition and sequence to proline-rich proteins (PRPs) in human saliva. On the basis of this feature and their shared destination in the gastrointestinal tract, we hypothesized that salivary PRPs may modulate gluten-mediated immune responses in CD. Parotid salivary secretions were collected from CD patients, refractory CD patients, non-CD patients with functional gastrointestinal complaints, and healthy controls. Structural similarities of PRPs with gluten were probed with anti-gliadin antibodies. Immune responses to PRPs were investigated toward CD patient-derived peripheral blood mononuclear cells and in a humanized transgenic HLA-DQ2/DQ8 mouse model for CD. Anti-gliadin antibodies weakly cross-reacted with the abundant salivary amylase but not with PRPs. Likewise, the R5 antibody, recognizing potential antigenic gluten epitopes, showed negligible reactivity to salivary proteins from all groups. Inflammatory responses in peripheral blood mononuclear cells were provoked by gliadins whereas responses to PRPs were similar to control levels, and PRPs did not compete with gliadins in immune stimulation. In vivo, PRP peptides were well tolerated and nonimmunogenic in the transgenic HLA-DQ2/DQ8 mouse model. Collectively, although structurally similar to dietary gluten, salivary PRPs were nonimmunogenic in CD patients and in a transgenic HLA-DQ2/DQ8 mouse model for CD. It is possible that salivary PRPs play a role in tolerance induction to gluten early in life. Deciphering the structural basis for the lack of immunogenicity of salivary PRPs may further our understanding of the toxicity of gluten.
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Yamada, Yukinori, Tomoharu Yokooji, Kyohei Kunimoto та ін. "Hypoallergenic Wheat Line (1BS-18H) Lacking ω5-Gliadin Induces Oral Tolerance to Wheat Gluten Proteins in a Rat Model of Wheat Allergy". Foods 11, № 15 (2022): 2181. http://dx.doi.org/10.3390/foods11152181.
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The early ingestion of food can prevent the onset of food allergy related to inducing oral tolerance (OT). We developed the Hokushin wheat line as a hypoallergenic wheat (1BS-18H) lacking ω5-gliadin, a major allergen of wheat-dependent exercise-induced anaphylaxis (WDEIA). The 1BS-18H wheat had lower ability of sensitization for ω5-gliadin compared with Hokushin wheat. Here, we evaluated the induction of OT to gluten and ω5-gliadin by the early consecutive ingestion of 1BS-18H gluten using a rat model of wheat allergy. Rats were subcutaneously immunized with commercial gluten or native ω5-gliadin following the daily oral administration of gluten. The daily oral administration of 1BS-18H gluten for 5 days before immunization suppressed the increase in gluten- or ω5-gliadin-specific IgE and IgG1 antibodies induced by immunization to a level similar to Hokushin gluten. Intravenous challenge with gluten or ω5-gliadin did not decrease the rectal temperature in rats with OT induced by 1BS-18H or Hokushin gluten, although it was decreased in non-OT rats. In conclusion, the early consecutive ingestion of 1BS-18H wheat before sensitization induced OT to gluten and ω5-gliadin. These findings support the benefit of 1BS-18H wheat to prevent wheat allergy including WDEIA by consecutive ingestion in humans.
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Espinoza-Herrera, Javier, Luz María Martínez, Sergio O. Serna-Saldívar, and Cristina Chuck-Hernández. "Methods for the Modification and Evaluation of Cereal Proteins for the Substitution of Wheat Gluten in Dough Systems." Foods 10, no. 1 (2021): 118. http://dx.doi.org/10.3390/foods10010118.
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The substitution of wheat gluten in the food industry is a relevant research area because the only known treatment for celiac disease is abstinence from this protein complex. The use of gluten-free cereals in dough systems has demonstrated that the viscoelastic properties of gluten cannot be achieved without the modification of the protein fraction. The quality of the final product is determined by the ability of the modification to form a matrix similar to that of gluten and to reach this, different methods have been proposed and tested. These procedures can be classified into four main types: chemical, enzymatic, physical, and genetic. This article provides a comprehensive review of the most recent research done in protein modification of cereal and pseudocereals for gluten substitution. The reported effects and methodologies for studying the changes made with each type of modification are described; also, some opportunity areas for future works regarding the study of the effect of protein modifications on gluten-free products are presented.
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Espinoza-Herrera, Javier, Luz María Martínez, Sergio O. Serna-Saldívar, and Cristina Chuck-Hernández. "Methods for the Modification and Evaluation of Cereal Proteins for the Substitution of Wheat Gluten in Dough Systems." Foods 10, no. 1 (2021): 118. http://dx.doi.org/10.3390/foods10010118.
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The substitution of wheat gluten in the food industry is a relevant research area because the only known treatment for celiac disease is abstinence from this protein complex. The use of gluten-free cereals in dough systems has demonstrated that the viscoelastic properties of gluten cannot be achieved without the modification of the protein fraction. The quality of the final product is determined by the ability of the modification to form a matrix similar to that of gluten and to reach this, different methods have been proposed and tested. These procedures can be classified into four main types: chemical, enzymatic, physical, and genetic. This article provides a comprehensive review of the most recent research done in protein modification of cereal and pseudocereals for gluten substitution. The reported effects and methodologies for studying the changes made with each type of modification are described; also, some opportunity areas for future works regarding the study of the effect of protein modifications on gluten-free products are presented.
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Gasparre, Nicola, Marco van den Berg, Filip Oosterlinck, and Arjen Sein. "High-Moisture Shear Processes: Molecular Changes of Wheat Gluten and Potential Plant-Based Proteins for Its Replacement." Molecules 27, no. 18 (2022): 5855. http://dx.doi.org/10.3390/molecules27185855.
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Nowadays, a growing offering of plant-based meat alternatives is available in the food market. Technologically, these products are produced through high-moisture shear technology. Process settings and material composition have a significant impact on the physicochemical characteristics of the final products. Throughout the process, the unfolded protein chains may be reduced, or associate in larger structures, creating rearrangement and cross-linking during the cooling stage. Generally, soy and pea proteins are the most used ingredients in plant-based meat analogues. Nevertheless, these proteins have shown poorer results with respect to the typical fibrousness and juiciness found in real meat. To address this limitation, wheat gluten is often incorporated into the formulations. This literature review highlights the key role of wheat gluten in creating products with higher anisotropy. The generation of new disulfide bonds after the addition of wheat gluten is critical to achieve the sought-after fibrous texture, whereas its incompatibility with the other protein phase present in the system is critical for the structuring process. However, allergenicity problems related to wheat gluten require alternatives, hence an evaluation of underutilized plant-based proteins has been carried out to identify those that potentially can imitate wheat gluten behavior during high-moisture shear processing.
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Ribeiro, Miguel, Telma de Sousa, Patrícia Poeta, Ana Sofia Bagulho, and Gilberto Igrejas. "Review of Structural Features and Binding Capacity of Polyphenols to Gluten Proteins and Peptides In Vitro: Relevance to Celiac Disease." Antioxidants 9, no. 6 (2020): 463. http://dx.doi.org/10.3390/antiox9060463.
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Polyphenols have been extensively studied due to their beneficial effects on human health, particularly for the prevention and treatment of diseases related to oxidative stress. Nevertheless, they are also known to have an anti-nutritional effect in relation to protein metabolism. This effect is a consequence of its binding to digestive enzymes and/or protein substrates. Dietary gluten is the main trigger of celiac disease, a common immune-based disease of the small intestine and for which the only treatment available is the adherence to a gluten-free diet. Recent studies have addressed the use of dietary polyphenols to interact with gluten proteins and avoid its downstream deleterious effects, taking the advantage of the anti-nutritive nature of polyphenols by protein sequestering. Flavonoids, coumarins and tannins have shown the ability to form insoluble complexes with gluten proteins. One of the most promising molecules has been epigallocatechin-3-gallate, which through its binding to gliadins, was able to reduce gliadins digestibility and its ability to stimulate monolayer permeability and transepithelial transport of immunodominant peptides in cell models. This review focuses on the structural features and binding capacity of polyphenols to gluten proteins and peptides, and the prospects of developing an adjuvant therapy in celiac disease.
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Sánchez-León, Susana, María José Giménez, Isabel Comino, et al. "Stimulatory Response of Celiac Disease Peripheral Blood Mononuclear Cells Induced by RNAi Wheat Lines Differing in Grain Protein Composition." Nutrients 11, no. 12 (2019): 2933. http://dx.doi.org/10.3390/nu11122933.
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Wheat gluten proteins are responsible for the bread-making properties of the dough but also for triggering important gastrointestinal disorders. Celiac disease (CD) affects approximately 1% of the population in Western countries. The only treatment available is the strict avoidance of gluten in the diet. Interference RNA (RNAi) is an excellent approach for the down-regulation of genes coding for immunogenic proteins related to celiac disease, providing an alternative for the development of cereals suitable for CD patients. In the present work, we report a comparative study of the stimulatory capacity of seven low-gluten RNAi lines differing in grain gluten and non-gluten protein composition, relevant for CD and other gluten pathologies. Peripheral blood mononuclear cells (PBMCs) of 35 patients with active CD were included in this study to assess the stimulatory response induced by protein extracts from the RNAi lines. Analysis of the proliferative response and interferon-gamma (INF-γ) release of PBMCs demonstrated impaired stimulation in response to all RNAi lines. The lower response was provided by lines with a very low content of α- and γ-gliadins, and low or almost devoid of DQ2.5 and p31–43 α-gliadin epitopes. The non-gluten protein seems not to play a key role in PBMC stimulation.
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Fernández-Pérez, Silvia, Jenifer Pérez-Andrés, Sergio Gutiérrez, et al. "The Human Digestive Tract Is Capable of Degrading Gluten from Birth." International Journal of Molecular Sciences 21, no. 20 (2020): 7696. http://dx.doi.org/10.3390/ijms21207696.
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The human gastrointestinal system has the capacity to metabolize dietary gluten. The capacity to degrade gliadin-derived peptide is present in humans from birth and increases during the first stages of life (up to 6–12 months of age). Fecal samples from 151 new-born and adult non-celiac disease (NCD) volunteers were collected, and glutenase and glianidase activities were evaluated. The capacity of total fecal proteins to metabolize 33-mer, 19-mer, and 13-mer gliadin peptides was also evaluated by high-performance liquid chromatography (HPLC). Feces from new-borns (meconium) showed glutenase and gliadinase activities, and peptidase activity against all three gliadin peptides. Maximal gluten degradative activity was observed in fecal samples from the youngest volunteers (0–12 months old). After the age of nine months, the gluten digestive capacity of gastrointestinal tract decreases and, from ±8 years old, individuals lose the ability to completely degrade toxic peptides. The gastrointestinal proteases involved in gluten digestion: elastase 2A, elastase 3B, and carboxipeptidase A1 are present from earlier stages of life. The human digestive tract contains the proteins capable of metabolizing gluten from birth, even before starting gluten intake. Humans are born with the ability to digest gluten and to completely degrade the potentially toxic gliadin-derived peptides (33-, 19-, and 13-mer).
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Muslimov, N. Zh, A. B. Abuova, and A. I. Kabylda. "Characteristics of the amino acid composition of flour types for gluten-free pasta production." Journal of Almaty Technological University, no. 3 (September 25, 2022): 64–73. http://dx.doi.org/10.48184/2304-568x-2022-3-64-73.
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Research on the study of the formulation of gluten-free pasta and the selection of raw materials for their production, depending on the amino acid composition, is necessary for the prevention and treatment of diseases such as phenylketonuria and celiac disease, non-celiac non-allergic sensitivity. In the world it occurs with a frequency of 1: 100. More than 472 people are registered in Kazakhstan. Wheat gliadin is characterized by a deficient content of essential amino acids: methionine, cysteine, threonine, tryptophan, arginine, histidine, especially limiting lysine. However, wheat contains non-essential amino acids (glutamic acid, proline in an amount of 16-44 %), which have the ability to be synthesized in the human body, have a toxic effect on people with signs of gluten intolerance. For the treatment and prevention of these diseases, the gluten content should not exceed 20 ppm/kg of the consumed product. The only way out for all patients, except for the treatment of comorbidities, is the observance of a strict gluten-free diet. Gluten-free types of flour from corn and rice do not contain the necessary amounts of essential amino acids, in particular lysine. Legume proteins, including chickpeas, are well balanced in terms of amino acid composition compared to cereal proteins. It has been determined that food sorghum contains all the basic substances necessary for normal human life: proteins from 11-16 %, including lysine 0.17 % - 0.33 %, starch from 60 - 66 %, fat up to 5,5 %. Purpose: selection of cereals and legumes by amino acid composition for the production of gluten-free pasta. The resarch of the amino acid composition of the studied types of flour showed that the combined use of gluten-free buckwheat, corn, rice flour in various compositions and ratios with sorghum or chickpea flour increases the nutritional value of gluten-free pasta products.
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Torbica, Aleksandra M., Jasna S. Mastilović, Milica M. Pojić, and Žarko S. Kevrešan. "Effects of Wheat Bug (Eurygasterspp. andAeliaspp.) Infestation in Preharvest Period on Wheat Technological Quality and Gluten Composition." Scientific World Journal 2014 (2014): 1–6. http://dx.doi.org/10.1155/2014/148025.
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The effects of wheat bug infestation (Eurygasterspp. andAeliaspp.) on the composition of wheat gluten proteins and its influence on flour technological quality were investigated in the present study. Wheat samples of six wheat varieties, collected from two localities in northern Serbia, were characterized by significantly different level of wheat bug infestation. Composition of wheat gluten proteins was determined using sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS PAGE), while the selected parameters of technological quality were determined according to standard and modified empirical rheological methods (Farinograph, Extensograph, Alveograph, and Gluten Index). The surface morphology of the selected samples was viewed using scanning electron microscopy (SEM). Wheat from wheat bug-infested locality regardless of the variety had deteriorated technological quality expressed with higher Farinograph softening degree, lower or immeasurable Extensograph energy, and Alveograph deformation energy. The most important changes in the gluten proteins composition of bug-infested wheat were related to gliadin subunits with molecular weights below 75 kDa, which consequently caused deterioration of uniaxial and biaxial extensibility and dough softening during mixing.
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Leisle, D., M. I. Kovacs, and N. Howes. "Inheritance and linkage relationships of gliadin proteins and glume color in durum wheat." Canadian Journal of Genetics and Cytology 27, no. 6 (1985): 716–21. http://dx.doi.org/10.1139/g85-107.
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Reciprocal backcross lines of two crosses were used to study the inheritance and linkage relationships of gliadin bands 42 and 45, as determined by polyacrylimide gel electrophoresis, and glume color in durum wheat (Triticum turgidum L.). Glume color was monogenically inherited, with partial dominance of buff color. Gliadin bands 42 and 45 were each controlled by one gene, located 7.87 ± 2.39 and 10.32 ± 2.44 crossover units, respectively, from the gene for glume color. Gliadin band 42 was always associated with bands 31 and 35. Gluten strength, as determined by sodium dodecyl sulphate sedimentation test, related closely to the genetics of gliadin bands 42 and 45, with the heterozygous band 42/45 types falling midway between the weak gluten homozygous band 42 and strong gluten homozygous band 45 types. Gluten strength data indicated that at least one additional gene, independent of those controlling these gliadins, is also involved.Key words: Triticum, gliadin, glume colour, linkage.
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Pătraşcu, Livia, Iuliana Banu, Ina Vasilean, and Iuliana Aprodu. "Effect of gluten, egg and soy proteins on the rheological and thermo-mechanical properties of wholegrain rice flour." Food Science and Technology International 23, no. 2 (2016): 142–55. http://dx.doi.org/10.1177/1082013216665722.
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The effect of protein addition on the rheological, thermo-mechanical and baking properties of wholegrain rice flour was investigated. Gluten, powdered eggs and soy protein concentrate were first analyzed in terms of rheological properties, alone and in admixture with rice flour. The temperature ramp tests showed clear differences in the rheological behavior of the batters supplemented with different proteins. The highest thermal stability was observed in case of soy protein samples. Frequency sweep tests indicated significant improvements of the rheological properties of rice flour supplemented with 15% gluten or soy proteins. The thermo-mechanical tests showed that, due to the high fat contents and low level of free water, the dough samples containing powdered eggs exhibited the highest stability. Addition of gluten resulted in a significant decrease of the dough development time, whereas samples with powdered eggs and soy proteins were more difficult to hydrate. The incorporation of proteins into the rice flour-based dough formulations significantly affected starch behavior by decreasing the peak consistency values. Concerning the quality of the rice flour-based breads, soy protein addition resulted in lighter crumb color and increased texture attributes, samples with gluten had better resilience and adhesiveness, whereas breads with egg protein were less brittle.
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Uri, Csilla, Árpád Tóth, Péter Sipos, Mária Borbélyné Varga, and Zoltán Győri. "The composition of gluten proteins and their effect on the rheological properties of gluten." Acta Agraria Debreceniensis, no. 23 (May 23, 2006): 124–29. http://dx.doi.org/10.34101/actaagrar/23/3215.
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Wheat is the major cereal component of bread in the world and is grown worldwide. Of the cereals only the bread wheats – and less the triticale – includes storage proteins that play an important role in the performance of gluten. Proteins of gluten complex may be present in two classes:− low molecular weight (gliadin-) components, and− high molecular weight (glutenin-) components.Gliadins shown appreciable heterogenity and can be separated into 40-50 components with gel electrophoresis. The composition of gliadins is employable for the identification the wheat varieties and to investigate the varieties. In the decreasing electrophoretic mobility sequence may be distinguish α-, β-, γ- and ω-gliadins. A glutenin subunits may be include in two classes:− high molecular weight glutenin subunits (HMW-GS),− low molecular weight glutenin subunits (LMW-GS).Wheat varieties can be identified by glutenin and their quality selection is also possible. The gliadin’s polypeptides encoding genes are located on the short arm of chromosomes 1A, 1B and 1D, 6A, 6B and 6D. Genetic coding for HMW subunits is located on the long arms of chromosomes 1A, 1B and 1D, the LMW-GS are also located on chromosomes 1A, 1B and 1D (Glu-3 loci) near the gliadin-coding loci.Storage proteins affect the rheological properties of gluten by two factors:1. The quality and quantity of the protein components of the gluten complex,2. The interactions between the protein fractions.