title: Two novel peptides with angiotensin I converting enzyme inhibitory and antioxidative activities from Scorpaena notata muscle protein hydrolysate.
abstract: Fish protein hydrolysate was prepared from muscle of small red scorpionfish (Scorpaena notata) by treatment with a protease from the fungus Penicillium digitatum. Protein hydrolysate was found to strongly inhibit the angiotensin I converting enzyme and exhibited high antioxidative activity through 1,1-diphenyl-2-picrylhydrazyl free radical scavenging assay. After ultrafiltration, peptides were isolated by a two-step procedure: size exclusion chromatography on a Toyopearl HW-40 followed by reversed-phase high-performance liquid chromatography with a high purification yield of 2.5 mg of peptide per gram of initial protein. Two major peptides were then identified by nanoscale liquid chromatography coupled to tandem mass spectrometry (nano-LC-MS/MS), corresponding to the following sequences: Leu-Val-Thr-Gly-Asp-Asp-Lys-Thr-Asn-Leu-Lys (1,204.665 Da) and Asp-Thr-Gly-Ser-Asp-Lys-Lys-Gln-Leu (992.511 Da). These peptides, mainly composed of hydrophilic amino acids, showed high antioxidative and angiotensin I converting enzyme inhibitory activities. These data suggest that the two novel peptides isolated from the muscle hydrolysate of small red scorpionfish can be a beneficial ingredient for functional foods or pharmaceuticals against hypertension and oxidative stress.
authors.affiliation: Laboratory of Protein Engineering and Bioactive Molecules (LIP-MB), National Institute of Applied Sciences and Technology, University of Carthage, Tunis Cedex, Tunisia.
authors.forename: Neyssene
authors.initials: N
authors.lastname: Aissaoui
authors.affiliation: Laboratory of Protein Engineering and Bioactive Molecules (LIP-MB), National Institute of Applied Sciences and Technology, University of Carthage, Tunis Cedex, Tunisia.
authors.forename: Ferid
authors.initials: F
authors.lastname: Abidi
authors.affiliation: CNRS UMR 6270, Laboratory of Polymers, Biopolymers and Surfaces, University of Rouen, Rouen, France.
authors.forename: Julie
authors.initials: J
authors.lastname: Hardouin
authors.affiliation: Laboratory of Venoms and Therapeutic Biomolecules, Institut Pasteur of Tunis, Tunis, Tunisia.
authors.forename: Zaineb
authors.initials: Z
authors.lastname: Abdelkafi
authors.affiliation: Laboratory of Venoms and Therapeutic Biomolecules, Institut Pasteur of Tunis, Tunis, Tunisia.
authors.forename: Naziha
authors.initials: N
authors.lastname: Marrakchi
authors.affiliation: CNRS UMR 6270, Laboratory of Polymers, Biopolymers and Surfaces, University of Rouen, Rouen, France.
authors.forename: Thierry
authors.initials: T
authors.lastname: Jouenne
authors.affiliation: Laboratory of Protein Engineering and Bioactive Molecules (LIP-MB), National Institute of Applied Sciences and Technology, University of Carthage, Tunis Cedex, Tunisia.
authors.forename: M Nejib
authors.initials: MN
authors.lastname: Marzouki
mesh_terms: D000595:Amino Acid Sequence / Q000235:genetics; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D000818:Animals; D000975:Antioxidants / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D002851:Chromatography, High Pressure Liquid; D009124:Muscle Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry / Q000378:metabolism; D010473:Perciformes; D011492:Protein Hydrolysates / Q000737:chemistry; D053719:Tandem Mass Spectrometry
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D000975:Antioxidants; D009124:Muscle Proteins; D010455:Peptides; D011492:Protein Hydrolysates; D007703:Peptidyl-Dipeptidase A
keywords: angiotensin I converting enzyme inhibitory activity; antioxidant peptides; hydrophilic amino acids; protein hydrolysate; purification and identification; therapeutic compounds