The study is aimed to establish the optimum conditions under which conglycinin can be hydrolyzed to produce the peptides,and then to purify the peptide and determine its antibacterial activity.The peptides were prepared by hydrolyzing conglycinin with flavourzyme.The 2h hydrolysates had exhibited good inhibitory activities to Escherichia coli and Staphylococcus aureus.The minimal inhibitory concentrations(MICs) against E.coli and S.aureus were 2.6 mg/mL and 3.2 mg/mL,respectively.Components of the 2 h hydrolysates were further separated using Sephadex-G15 gel filtration chromatography.The results of bacterial growth assays showed that CP2 had the maximum growth inhibitory activity to E.coli(P0.05).It suggested that the hydrolysates from conglycinin exhibited significant inhibitory activities to E.coli and S.aureus.