Abstract

BackgroundStaple cereals and their products are important foods. Many cereals contain an important protein group, gluten, which provides structure to bakery products and pasta. Gluten proteins have an unusual amino acid composition, containing high proline and glutamine contents. These amino acids confer resistance to proteolysis by gastrointestinal tract enzymes, producing indigestible proline- and glutamine-rich peptides that can trigger immunogenic reactions responsible for gluten-related health disorders. These disorders represent a serious public health issue, affecting approximately 5% of the global population. The prescription of a gluten-free diet (GFD) is the only accepted therapy for gluten-related health disorders. Scope and approachAdherence to a GFD remains a difficult goal for many reasons. Alternative approaches have been proposed to supplement or substitute a GFD. Among them, the use of gluten-specific enzymes to degrade immunogenic peptides has shown promising results. Most of the enzymes used in this approach are of microbial origin. Identification of natural alternatives is a timely requirement. Key findingsSeveral enzymes of microbial origin have been identified that are claimed to digest gluten in the human gastrointestinal tract. However, only a few claim to be able to digest immunogenic gluten peptides. Most of these enzyme therapies are still being developed and are not yet viable practical solutions. Fruit-borne proteases are a possible alternative solution. Notably, green kiwifruit (Actinidia deliciosa), containing the cysteine protease actinidin, degraded gluten in animal trials and could be a natural way to manage gluten-related health disorders – an example of positive food synergy.

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