A study published in the journal Food Chemistry has found that a protease enzyme from the figleaf gourd (Cucurbita ficifolia) can reduce the ability of peanut proteins to trigger allergic reactions in laboratory tests. Researchers from Wroclaw University of Environmental and Life Sciences and Wroclaw Medical University explored whether this natural enzyme could alter peanut proteins in a way that makes them less likely to be recognized by antibodies involved in allergies. The study showed that the enzyme can change the structure of peanut proteins, which may lower their ability to bind to IgE antibodies. These antibodies are key players in allergic reactions. However, the process did not eliminate the allergenic properties entirely. Some protein fragments, such as Ara h 2, Ara h 6, and Ara h 3, still had the potential to be recognized by IgE antibodies. The researchers pointed out that traditional food processing techniques may not effectively reduce the allergenic nature of peanut proteins, which are known to resist digestion and heat. In contrast, the figleaf gourd protease demonstrated a controlled ability to break down these proteins. The effectiveness of the process depended largely on the duration and temperature of the hydrolysis. The study’s authors stressed that while the findings suggest a possible way to create foods with lower allergenic potential, the resulting product is not yet safe for people with peanut allergies. More research is needed to determine whether the remaining protein fragments can trigger allergic responses by activating cells like basophils. Further functional studies will be essential to assess the practical use of this method. The research also points to broader opportunities in the development of functional foods. Enzymatic hydrolysis can generate peptides with varied biological and technological properties, offering new possibilities for creating food ingredients with specific characteristics and health benefits. Using naturally derived enzymes allows for precise protein modification, which could be important in developing new food products with reduced allergenic potential and beneficial biological activity.