Recovery of casein-derived peptides with in vitro inhibitory activity of angiotensin converting enzyme (ACE) using aqueous two-phase systems

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