This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: Peanut allergy is one of the most serious food allergies and can lead to sudden, life-threatening reactions. Researchers from Wroclaw University of Environmental and Life Sciences, in collaboration with Wroclaw Medical University, investigated whether a natural enzyme obtained from figleaf gourd (Cucurbita ficifolia) could reduce recognition of peanut proteins by antibodies involved in allergic reactions.
The study is published in the journal Food Chemistry, and the results show that enzymatic hydrolysis can significantly reduce the immunoreactivity of peanut proteins. The study has not produced a product that is safe for people with peanut allergy, but it points to a potential way to develop foods with reduced allergenic potential. "Peanut allergy is particularly challenging because even a small amount of the allergen can trigger a serious reaction in sensitized individuals, including anaphylaxis.
We are therefore looking for methods that can modify allergenic proteins and reduce their recognition by the immune system," said Ewa Willak-Janc, MD, Ph.D., of the 1st Department and Clinic of Pediatrics, Allergology and Cardiology at Wroclaw Medical University and a co-author of the publication. Enzymes used to hydrolyze plant and animal proteins are mainly commercial preparations of digestive enzymes. Using them individually, in combination or with additional processes such as heat treatment can significantly reduce the allergenicity of many proteins.
However, researchers are still searching for new enzymes from readily available sources that can efficiently hydrolyze proteins found in food and reduce their allergenicity more effectively. One promising group is noncommercial extracellular serine proteases obtained from figleaf gourd (Cucurbita ficifolia). A protein's structure is one factor that determines whether the immune system can recognize it.
In people with allergies, antibodies react with specific protein fragments called epitopes. "If enzymatic hydrolysis appropriately modifies protein structure, its ability to bind antibodies may be reduced. In the case of allergens, this approach is particularly interesting because it allows us not only to break down the protein, but above all to control changes in its properties," said Joanna Bajzert, Ph.D., Eng., from the Department of Immunology, Pathophysiology and Veterinary Prevention at Wroclaw University of Environmental and Life Sciences and an author of the publication.
The idea of using a pumpkin-derived protease was not accidental. Previous long-term studies by the team from Wroclaw University of Environmental and Life Sciences showed that this enzyme can effectively break down milk proteins and modify their properties. This time, the researchers investigated whether a similar approach could be applied to peanut proteins, one of the most important sources of food allergens.
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