Angiotensin-I converting enzyme (ACE) inhibitory peptides from chicken skin gelatin hydrolysate and its antihypertensive effect in spontaneously hypertensive rats

Chicken skin gelatin hydrolysates and peptides with angiotensin converting enzyme inhibitory (ACEI) activity were produced enzymatically using alcalase, pronase E, and collagenase before fractionation into <2, <5, and <10 kDa fractions. The fraction with the highest ACEI activity was further purified sequentially using gel filtration chromatography RP-HPLC. The ACEI activity of <2, <5 and <10 kDa hydrolysate fractions were 69.64, 76.80 and 87.69%, respectively. Gel filtration chromatography of <2 kDa fraction produced peptides with ACEI activity (92%), and showed a similarity to the synthetic drug captopril (93%). The relative molecular mass range of the