Abstract
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.
Highlights
Coeliac disease (CD) is a chronic, immune-mediated intestinal disorder characterized by an inflammatory response to dietary gluten that can develop in genetically susceptible individuals [1].Gluten is a general name for a class of seed storage proteins from wheat, barley, rye, and oats that can be sub-divided into the alcohol-soluble prolamins and insoluble glutelins.Gluten contains a higher proportion of proline and glutamine, the term prolamin, than the average seed storage protein, and they contain fewer tryptic sites, rendering them recalcitrant to digestion in the gastrointestinal tract
As questions remain over the accuracy of enzyme-linked immunosorbent assay (ELISA) measurement in highly processed food [12], this study has focused on the utility of liquid chromatography-mass spectrometry (LC-Mass spectrometry (MS)) to detect grain-specific peptide markers in a range of Australian breakfast foods
Been determined to be specific to their source grain and show ideal analytical properties were investigated to ensure that they persist in heavily processed foods and were free from interference in complex matrices
Summary
Gluten is a general name for a class of seed storage proteins from wheat (gliadins and glutenins), barley (hordeins), rye (secalins), and oats (avenins) that can be sub-divided into the alcohol-soluble prolamins and insoluble glutelins. Gluten contains a higher proportion of proline and glutamine, the term prolamin, than the average seed storage protein, and they contain fewer tryptic sites, rendering them recalcitrant to digestion in the gastrointestinal tract. Gluten evades complete digestion by host proteases and gut microbiota, resulting in the generation of gluten immunogenic peptides [2,3]. CD has a recorded prevalence of 1–3% in Western populations, with 0.7% of the US population diagnosed with CD [4]. The prevalence of CD in Australia was noted to be 1.2% for men and 1.9% for Molecules 2019, 24, 3665; doi:10.3390/molecules24203665 www.mdpi.com/journal/molecules
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