Pumpkin power: The influence of serine protease isolated from Cucurbita ficifolia on peanut proteins.

Peanut allergies are among the most severe food allergies. One of the treatment is avoidance of peanuts. Enzymatic hydrolysis is widely used in the food industry to disrupt IgE-binding epitopes. This study evaluated optimal conditions for hydrolysis of peanut proteins fraction isolate using plant protease from Cucurbita ficifolia. Different enzyme activities (150/300/600 U/mg of protein), temperatures (37/42 °C) and reaction times (0/1/5/24 h) were tested. The effects on immunoreactivity were investigated. Findings using competitive ELISA and immunoblotting with chicken anti-peanut protein antibodies indicated that the immunoreactivity of the obtained hydrolysates was influenced by time and temperature but remained independent of enzyme activity. The lowest antibodies binding properties showed hydrolysates obtained at 42 °C after 24 h. Results concerning IgE binding capacity revealed that small peptides after hydrolysis still reacted with antibodies, making the complete removal of allergenicity impossible. Future experiments should focus on cells activation tests to determine whether these peptides trigger their degranulation.