Two novel peptides with angiotensin I converting enzyme inhibitory and antioxidative activities from Scorpaena notata muscle protein hydrolysate

Autor: Neyssene, Aissaoui, Ferid, Abidi, Julie, Hardouin, Zaineb, Abdelkafi, Naziha, Marrakchi, Thierry, Jouenne, M Nejib, Marzouki
Přispěvatelé: Institut National des Sciences Appliquées et de Technologie - Carthage (INSAT Carthage), Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Laboratoire des Venins et Biomolécules Thérapeutiques - Laboratory of Venoms and Therapeutic Biomolecules (LR11IPT08), Institut Pasteur de Tunis, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), This work was supported by the financial project of LIP‐MB Laboratory, INSAT, Carthage University, Ministry of Higher Education and Scientific Research of Tunisia.
Jazyk: angličtina
Rok vydání: 2017
Předmět:
therapeutic compounds
Protein Hydrolysates
MESH: Antioxidants/pharmacology
Muscle Proteins
angiotensin I converting enzyme inhibitory activity
Angiotensin-Converting Enzyme Inhibitors
MESH: Peptidyl-Dipeptidase A/chemistry
Peptidyl-Dipeptidase A
Antioxidants
MESH: Muscle Proteins/chemistry
MESH: Peptides/pharmacology
MESH: Peptides/chemistry
MESH: Protein Hydrolysates/chemistry
Tandem Mass Spectrometry
antioxidant peptides
Animals
MESH: Animals
Amino Acid Sequence
MESH: Chromatography
High Pressure Liquid
Chromatography
High Pressure Liquid
MESH: Amino Acid Sequence/genetics
MESH: Muscle Proteins/isolation & purification
purification and identification
hydrophilic amino acids
MESH: Tandem Mass Spectrometry
MESH: Peptides/genetics
MESH: Peptidyl-Dipeptidase A/metabolism
MESH: Angiotensin-Converting Enzyme Inhibitors/isolation & purification
Perciformes
MESH: Angiotensin-Converting Enzyme Inhibitors/chemistry
MESH: Antioxidants/isolation & purification
MESH: Muscle Proteins/pharmacology
MESH: Perciformes
MESH: Peptides/isolation & purification
Peptides
MESH: Angiotensin-Converting Enzyme Inhibitors/pharmacology
[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
protein hydrolysate
MESH: Antioxidants/chemistry
Zdroj: Biotechnology and Applied Biochemistry
Biotechnology and Applied Biochemistry, Wiley, 2017, 64 (2), pp.201-210. ⟨10.1002/bab.1478⟩
ISSN: 0885-4513
1470-8744
DOI: 10.1002/bab.1478⟩
Popis: International audience; 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.
Databáze: OpenAIRE
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