This　study　investigated　the　effects　of　ultrasound,　enzyme　concentration　and　enzyme　treatment　time　on　soluble　protein　and　major　allergenic　proteins　(Ara　h　1　and　Ara　h　2)　of　roasted　peanut　kernels.　A　3-factor,　five-level　orthogonal　experimental　design　was　implemented　with　various　ultrasonication　times,　concentrations　of　trypsin　or　α-chymotrypsin　and　treatment　times.　The　total　soluble　proteins　were　determined　by　the　Bicinchoninic　acid　(BCA)　method,　Ara　h　1　and　Ara　h　2　were　evaluated　by　SDS-PAGE　and　sandwich　ELISA.　The　IgE-binding　of　peanut　extracts　was　analysed　by　a　competitive　inhibition　ELISA.　Results　indicate　that　ultrasound　treatment,　followed　by　protease　digestion　of　peanuts,　significantly　increased　the　solubility　of　peanut　protein　and　decreased　the　concentrations　of　Ara　h　1　and　Ara　h　2.　The　sequential　treatment　of　peanuts　by　ultrasonication-trypsin-alpha　chymotrypsin,　resulted　in　maximum　reductions　of　Ara　h　1/Ara　h　2,　and　lowest　IgE-binding.　This　study　provides　an　approach　to　significantly　reduce　allergenic　proteins　in　peanut　product.　©　2013　Elsevier　Ltd.　All　rights　reserved.