Key result
The pearl matrix protein-derived peptide KKCHFWPFPW competitively inhibited angiotensin-converting enzyme in vitro with a half-maximal inhibitory concentration (IC50) of 4.17 μM.
Why the study?
The study aimed to identify and characterize ACE-inhibitory peptides derived from Indonesian dried-salted fish to evaluate their potential blood pressure-lowering effects.
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 (IC50; 0.63 mg 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 IC50 value of 31.97, 156.28, 74.22, and 22.20 microM, respectively.
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Astawan et al. (1995) studied Hypertension (in vitro). Pearl matrix peptide KKCHFWPFPW vs. Blank control was evaluated on Angiotensin-converting enzyme (ACE) inhibitory activity (IC50 4.17 μM). The pearl matrix protein-derived peptide KKCHFWPFPW competitively inhibited angiotensin-converting enzyme in vitro with a half-maximal inhibitory concentration (IC50) of 4.17 μM.
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