Pigmented wheat varieties (Triticum aestivum spp.) are getting increasingly popular in modern nutrition and thoroughly researched for their functional and nutraceutical value. The colour of these wheat grains is caused by the expression of natural pigments, including carotenoids and anthocyanins, that can be restricted to either the endosperm, pericarp and/or aleurone layers. While contrasts in phytochemical synthesis give rise to variations among purple, blue, dark and yellow grain's antioxidant and radical scavenging capacities, little is known about their influence on gluten proteins expression, digestibility and immunogenic potential in a Celiac Disease (CD) framework. Herein, it has been found that the expression profile and immunogenic properties of gliadin proteins in pigmented wheat grains might be affected by anthocyanins and carotenoids upregulation, and that the spectra of peptide released upon simulated gastrointestinal digestion is also significantly different. Interestingly, anthocyanin accumulation, as opposed to carotenoids, correlated with a lower immunogenicity and toxicity of gliadins at both protein and peptide levels. Altogether, this study provides first-level evidence on the impact modern breeding practices, seeking higher expression levels of health promoting phytochemicals at the grain level, may have on wheat crops functionality and CD tolerability.
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http://dx.doi.org/10.1016/j.foodres.2024.114008 | DOI Listing |
J Sci Food Agric
December 2024
Department of Food Science and Engineering, Institute of Food Safety and Nutrition, Jinan University, Guangzhou, China.
Background: Wheat gluten (WG) is a crucial cereal protein commonly utilized in the food, biological and pharmaceutical industries. However, WG is poorly soluble in water, resulting in poor functional properties, which restrict its application in the food industry. As a result, there is an urgent need for improving the properties of WG.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Department of Nutrition, China Medical University, No. 100, Sec. 1, Jingmao Rd., Beitun Dist., Taichung City 40604, Taiwan.
Alzheimer's disease (AD), a leading neurodegenerative disorder, is closely associated with the accumulation of amyloid-beta (Aβ) peptides in the brain. The enzyme β-secretase (BACE1), pivotal in Aβ production, represents a promising therapeutic target for AD. While bioactive peptides derived from food protein hydrolysates have neuroprotective properties, their inhibitory effects on BACE1 remain largely unexplored.
View Article and Find Full Text PDFFoods
December 2024
Institute of Collaborative Innovation in Great Health, College of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, China.
Hardness constitutes one of the primary performance indices of bread. However, there is scarce literature regarding the study of the mechanisms of increased hardness in different breads. In this paper, the hardness and retrogradation rates of five popular brands of bread (DaliGarden, Mankattan, MianLunSi, TOLY, and ZhengMao) in China during storage at room temperature were determined, and the mechanism of increased hardness was revealed by the results in terms of Fourier transform infrared spectroscopy (FTIR), disulfide bonds, C solid-state nuclear magnetic resonance (NMR), X-ray diffraction, and differential scanning calorimetry (DSC).
View Article and Find Full Text PDFClin Chim Acta
December 2024
Department of Medical Biotechnology, School of Advanced Medical Sciences and Technologies, Shiraz University of Medical Sciences, Shiraz, Iran; Infertility Research Center, Shiraz University of Medical Sciences, Shiraz, Iran. Electronic address:
Celiac disease (CeD) is an autoimmune disorder triggered by sensitivity to gluten, a protein complex found in wheat, barley, and rye. Gliadins, a component of gluten, are proteins that trigger an immune response in individuals with CeD, primarily affecting the small intestine's inner lining. Despite a 1-1.
View Article and Find Full Text PDFChemMedChem
December 2024
Molecular Cell Biology, Faculty of Medicine, Ruhr University Bochum, Universitätsstr. 150, 44801, Bochum, Germany.
The 33-mer gliadin peptide and its deamidated derivative, known as 33-mer DGP, are proteolytically resistant peptides central to the pathomechanism of celiac disease (CeD), the autoimmune presentation of gluten-related disorders (GRD). Both peptides can form spontaneous oligomers in the nanomolar concentration, leading to the formation of nanostructures. In other protein-related diseases, oligomers and aggregates are central in their pathomechanism; therefore, it was hypothesized that the oligomerization of proteolytical-resistant 33-mer gliadin peptides could be an underrecognized disease trigger.
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