Angiotensin I-converting enzyme inhibitory activity of low-molecular-weight peptides from Atlantic salmon (Salmo salar L.) skin

Abstract

Collagen extracted from Atlantic salmon (Salmo salar L.) skin (which is normally discarded in the process of manufacture) was hydrolyzed with Alcalase and papain, and treated by multistage separation. The salmon skin collagen peptides (SSCP) obtained had high protein content (91.20±1.03%) and low molecular weights, 90.79% of which were less than 1000Da. SSCP was then separated by reversed-phase high performance liquid chromatography. Eleven major fractions were collected and their angiotensin I-converting enzyme (ACE) inhibitory activity was assayed. Fractions 5 and 7 displaying higher ACE inhibitory activity were subjected to mass spectrometer to identify the ACE inhibitory peptides. A total of eleven peptide sequences were identified, and two dipeptides, Ala-Pro and Val-Arg, were selected for further ACE inhibitory activity analysis. The ACE inhibitory activities of Ala-Pro (IC50=0.060±0.001mg/ml) and Val-Arg (IC50=0.332±0.005mg/ml) were found to be approximately 20- and 4-fold higher than that of SSCP (1.165±0.087mg/ml), respectively.