The purpose of this study was the purification and characterization of an angiotensin I
converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates of rainbow …

Lizard fish (Saurida elongata) muscle protein was hydrolyzed by neutral protease to obtain
the hydrolysate with angiotensin-I converting enzyme (ACE) inhibitory activity. A novel ACE …

Angiotensin-I-converting enzyme (ACE-I) inhibitory peptides were purified from the seaweed
pipefish muscle protein using papain, alcalase, neutrase, pronase, pepsin and trypsin …

In this study, the angiotensin I‐converting enzyme (ACE) inhibitory peptides were isolated
from snakehead fish sarcoplasmic protein hydrolysates. Enzymatic hydrolysis of …

Angiotensin I converting enzyme (ACE) inhibitory peptide was isolated from tuna dark
muscle hydrolysate prepared by alcalase, neutrase, pepsin, papain, α-chymotrypsin, and …

Angiotensin I converting enzyme (ACE) inhibitory peptide was separated from chum salmon
(Oncorhynchus keta) skin hydrolysate prepared by various hydrolysis enzymes. The trypsin …

The angiotensin I-converting enzyme (ACE) inhibitory activities of protein hydrolysates
prepared from cuttlefish (Sepia officinalis) proteins by treatment with various bacterial …

Proteins, especially the proteins of marine origin, are potential resources of natural drugs
and food additives. Our previous results showed that shark meat hydrolysate obtained with …

The aim of this study was to purify peptides with anti-hypertensive properties from a
hydrolysate of flounder fish muscle. Among four proteolytic hydrolysates, pepsin showed the …

Summary We isolated Phe–Leu as an angiotensin I‐converting enzyme (ACE) inhibitor from
hydrolysate of chum salmon muscle. The IC50 value of this peptide was 13.6 μm, and it …