Abstract
Indonesian dried-salted fish (DSF) was produced from skipjack tuna by soaking the flesh in 15% NaCl (DSF I) or 25% NaCl (DSF II). The DSFs were then hydrolyzed by trypsin, chymotrypsin, Pronase E, and pepsin. Angiotensin I-converting enzyme (ACE) inhibitory activity was measured. The pepsin digest showed the highest inhibitory activity (IC5o ; 0. 63mg protein/ml). DSF II hydrolysate had higher inhibitory activity than that in DSF I. A three-month storage period of DSF gave higher ACE-inhibitory activity than that of 6 months. An oral administration of pepsin hydrolysate significantly decreased the blood pressure of rats. From the purification steps, at least 4 inhibitor peptides were found. The amino acid sequences of the peptides were Val-Ala-Trp-Lys-Leu, Trp-Ser-Lys-Val-Val-Leu, Ser-Lys-Val-Pro-Pro, and Cys-Trp-Leu-Pro-Val-Tyr, with an lC5o value of 31. 97, 156. 28, 74. 22, and 22. 20μM, respectively.
