Using high-temperature soybean meal as raw materials and Alcalase 2.4L as a catalyst, the optimal conditions of ACE inhibitory activity was obtained using the L9(34) orthogonal experiment as followed: substrate concentration 4%, enzyme activity 1500U/g, pH value 8.5 and the temperature 50℃. Under these conditions, the high ACE inhibitory activity reached 78.85%. Based on these results, Actinomucor elegans peptidases were employed to treat the hydrolysates for 3h and 6h, and 1%, 2% β-cyclodextrin (β-CD) were also used to embed hydrolysates to remove bitterness. The results showed that 1% of β-CD treatment can effectively remove bitterness and obtain the highest preservation of the ACE inhibitory activity.