Three novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) using digestive proteases

ACE inhibitory and antioxidant activities of red scorpionfish (Scorpaena notata) protein hydrolysates

“…Those products act as effective substrate competitors to the undigested or partially digested fish proteins. The shape of the hydrolysis curves obtained in this study was similar to those previously reported for sardinelle (Ben Khaled et al 2011), Pacific whiting solid wastes (Benjakul and Morrissey 1997), yellow stripe trevally (Klompong et al 2007), Atlantic salmon (Kristinsson and Rasco 2000) and cuttlefish (Balti et al 2010).…”

Purification and characterization of a novel angiotensin I-converting enzyme inhibitory peptide derived from abalone (Haliotis discus hannai Ino) gonads

“…Hydrolysis of skipjack roe by alcalase produced aCE inhibitory active peptides with IC 50 of 2,497.31 μg/ml [30]. The active hydrolysate from cuttlefish muscle showed 64.47 % aCE inhibitory activity at the concentration of 2 mg of dry weight/ml [31]. The aCE inhibitory activity of hydrolysate in the present study was comparable to that from loach (Misgurnus anguillicaudatus), which showed an IC 50 value of 613.2 μg/ml [32].…”

“…It has been reported that hydrophobic amino acid residues including ala and Met frequently appear in aCE inhibitory peptides, such as peptides from cuttlefish (Met-ala-Trp) [31], hen egg white lysozyme (ala-Met-lys) [33] and tenebrio molitor larva protein hydrolysate (Tyr-ala-asn) [34]. Thus, our present work not only provided a novel tripeptide with high aCE inhibitory activity, but also revealed potential key amino acid residues responsible for aCE inhibition.…”

Antioxidative and antihypertensive activities of pig meat before and after cooking and in vitro gastrointestinal digestion: Comparison between Italian autochthonous pig Suino Nero Lucano and a modern crossbred pig

“…In particular, ACE appears to prefer substrates or competitive inhibitors containing hydrophobic (aromatic or branched side-chains) amino acid residues at each of the three C-terminal positions (Li, Le, Shi, & Shrestha, 2004). Also, Kawakami and Kayahara (1993) suggested that most of ACE inhibitory peptides that are released by proteolityc digestion contain Pro, Lys or aromatic amino acid residues, and these peptides are particularly stable because are not further degraded by intestinal peptidases (Balti, Nejar-Arroume, Bougatef, Guillochon, & Nasri, 2010).…”