Angiotensin converting enzyme (ACE) inhibitory peptides derived from the simulated in vitro gastrointestinal digestion of cooked chicken breast

The release of encrypted angiotensin converting enzyme (ACE) inhibitory peptides upon simulated in vitro gastrointestinal (GI) digestion of Korat crossbred (KC) and commercial broiler (BR) breast meat varied with cooking methods. Digestas of KC breast meat heated at 70 °C for 0.5 h (H-0.5) showed the highest ACE inhibitory activity, while digestas of KC chicken heated at 121 °C for 1 h showed the lowest inhibitory activity. ACE inhibitory activity varied with the protein digestibility. After a series of chromatographic techniques, we identified KPLLCS, ELFTT, and KPLL, novel potent ACE inhibitor peptides whose sequences were homologous to that of myosin and whose IC50 values were 0.37, 6.35 and 11.98 μM, respectively. ELFTT and KPLL were resistant to plasmin hydrolysis for up to 60 min. Therefore, KC chicken meat heated at H-0.5 could serve as a source of ACE inhibitory peptides upon GI digestion.