A growing body of evidence suggests that protein structure can be uniquely altered by lipids. However, the role of lecithin on the digestibility and immunoreactivity of allergenic protein remains poorly understood. Therefore, we investigated the impact of different protein/lecithin (P:L) ratios (5:1, 10:1, 20:1, 30:1 and 40:1) on the digestion properties, peptide profiles and immunoreactivity of β-conglycinin in vitro simulated gastrointestinal digestion. Results revealed that lecithin addition increased the degree of hydrolysis and digestion rate of β-conglycinin during digestion in a dose-dependent manner, which may be attributed to the enhancement of pepsin activity. Additionally, the addition of lecithin contributed to the dispersion and homogeneity of β-conglycinin digestion products. When the ratio of lecithin to β-conglycinin was 1:10, the obtained β-conglycinin digestion products exhibited the highest DH value (23.80 %) and the lowest antigenicity (52.69%) in the intestinal digestion. Peptidomics and immunoinformatic analysis further confirmed that PL-10 disrupted 18/30, 15/44, and 37/75 epitopes in the α, α', and β subunits of β-conglycinin, respectively. These results suggested that lecithin changed the cleavage preferences of β-conglycinin, and promoted the disruption of allergic epitopes, specifically for the β subunit. The study can contribute to our understanding of the role of lecithin in the digestion properties and immunoreactivity of allergenic protein.