Peptides inhibiting the activity of angiotensin converting enzyme (ACE) were obtained by trypsin-catalyzed hydrolysis of bovine milk casein, performed at 37 °C, during 1, 2, 5, 8 and 24 h. Results of in vitro inhibitory activity ranged between 13.4 % and 78.5 %. The highest ACE inhibitory activity was evidenced for hydrolysates obtained after 2 h of reaction. Aqueous two-phase systems (ATPS) formed by polyethylene glycol of 1500 g mol-1 (PEG1500) + sodium phosphate or potassium phosphates were produced and evaluated, in terms of partition coefficients (K) and extraction yields (y), to recovery the casein hydrolysates at room temperature. In ATPS containing sodium phosphate, the peptides showed a slightly greater affinity towards the bottom salt-rich phase (0.1 < K < 0.9; 5.7 % < y < 47 %). In the case of ATPS containing potassium phosphates, these molecules showed substantially greater affinity towards the top polymer-rich phase (137 < K < 266; y > 99 %). These results point out extraction using PEG1500/potassium phosphate ATPS is an efficient technique to recover casein hydrolysates containing ACE inhibitors peptides. Outlined data will be helpful in integrating such unit operation to larger scale processes.