Abstract
Gluten is the ethanol-soluble protein fraction of cereal endosperms like wheat, rye, and barley. It is widely used in the food industry because of the physical–chemical properties it gives to dough. Nevertheless, there are some gluten-related diseases that are presenting increasing prevalences, e.g., celiac disease, for which a strict gluten-free diet is the best treatment. Due to this situation, gluten labeling legislation has been developed in several countries around the world. This article reviews the gluten immune detection systems that have been applied to comply with such regulations. These systems have followed the development of antibody biotechnology, which comprise three major methodologies: polyclonal antibodies, monoclonal antibodies (mAbs) derived from hybridoma cells (some examples are 401.21, R5, G12, and α-20 antibodies), and the most recent methodology of recombinant antibodies. Initially, the main objective was the consecution of new high-affinity antibodies, resulting in low detection and quantification limits that are mainly achieved with the R5 mAb (the gold standard for gluten detection). Increasing knowledge about the causes of gluten-related diseases has increased the complexity of research in this field, with current efforts not only focusing on the development of more specific and sensitive systems for gluten but also the detection of protein motifs related to pathogenicity. New tools based on recombinant antibodies will provide adequate safety and traceability methodologies to meet the increasing market demand for gluten-free products.
Highlights
Gluten is the general term for the ethanol-soluble proteins present in various cereal endosperms, including wheat, rye, barley, spelt, and kamut [1]
It is know that the two fractions contain proteins that are structurally related, with the differences in solubility resulting from their presence as monomers that interact by non-covalent forces or as high molecular mass polymers stabilized by interchain disulphide bonds
Gliadins are represented as single chain polypeptides, and it is accepted that gliadins are divided, according to their electrophoretic mobility in Polyacrylamide gel Electrophoresis (PAGE)
Summary
Gluten is the general term for the ethanol-soluble proteins present in various cereal endosperms, including wheat, rye, barley, spelt, and kamut [1]. In 1924, Osborne introduced a classification method for plant proteins by extraction with different solvents that is still in use After applying this classification (Table 1), wheat proteins are divided by their solubility behavior into the following fractions: globulins (soluble in a diluted salt solution), albumins (water soluble), gliadins (ethanol soluble), and glutelins (soluble in diluted acetic acid) [3]. When considering the alpha-gliadin structure, their central domain contains the proline- (P) and glutamine-rich (Q) heptapeptide PQPQPFP and pentapeptide PQQPY This domain contains the most characteristic immunogenic fragment, a 33-mer peptide comprising six overlapping epitopes significant for celiac disease pathogenesis [9], this peptide is not present in every wheat cultivar [10]. Several fragments of gliadins and glutelins are associated with different types of gluten-related diseases, e.g., α and γ-gliadins in celiac disease [11]; γ-, α/β-, ω5-, and ω1,2-gliadins, as well as HMW and LMW subunits of glutenin, are involved in wheat allergies [12]
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