The most important position among products which very often may elicit allergy takes legumins. The aim of this study was to determine the influence of thermal and enzymatic modification on allergenic properties of pea proteins. Allergenicity of pea proteins was decreased about 25-50% after thermal process like cooking. However, enzymatic hydrolysis decreased allergenicity about 47-70%. In majority cases trypsin hydrolysis caused more reduction of allergenicity of pea proteins than Alcalase hydrolysis. Immunoreactivity of major pea proteins (albumins, legumins, vicilins) in obtained hydrolysates were determined using specific polyclonal rabbit antibodies produced against isolated and purified pea protein fractions. Pea globulins have more resistance to Alcalase hydrolysis than trypsin one. Particularly it concerns vicilin fraction. It can be the reason of lower allergenicity of pea protein hydrolysates obtained by trypsin. Especially, the highest level of antibodies in sera patients was against pea vicilins (non modified). It may provide the highest allergenicity of vicilins among pea proteins.