ACE Inhibitory and Antioxidant Activities of Novel Peptides from Scorpaena notata By-product Protein Hydrolysate

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• 作者：Neyssene Aissaoui ; Ferid Abidi…
• 关键词：Angiotensin ; I converting enzyme ; Antioxidant peptides ; Protein hydrolysate ; Scorpaena notata
• 刊名：International Journal of Peptide Research and Therapeutics
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：23
• 期：1
• 页码：13-23
• 全文大小：
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Biochemistry, general; Animal Anatomy / Morphology / Histology; Polymer Sciences; Pharmaceutical Sciences/Technology; Pharmacology/Toxicology; Molecular Medicine;
• 出版者：Springer Netherlands
• ISSN：1573-3904
• 卷排序：23

文摘

This study describes the isolation of angiotensin I converting enzyme and antioxidative peptides from head protein hydrolysate of red scorpionfish (Scorpaena notata) prepared by treatment with a protease from the fungus Penicillium digitatum. After ultrafiltration, three peptides were isolated by a two-step procedure: size exclusion chromatography on a Toyopearl HW-40 followed by reversed-phase high performance liquid chromatography (RP-HPLC) with a high purification yield of 2.22 mg of peptide/g of initial protein. Active peptides were then identified by nanoscale liquid chromatography coupled to tandem mass spectrometry (nanoLC/MS–MS), corresponding to the following sequences: Gln–Gln–Pro–His–Ser–Arg–Ser–Lys–Gly–Phe–Pro–Gly–Pro (1424.724 Da), Gly–Gln–Lys–Ser–Val–Pro–Glu–Val–Arg (1000.565 Da) and Val–Glu–Gly–Lys–Ser–Pro–Asn–Val (830.448 Da). Peptides D-I, E-I and F-I showed high angiotensin-I converting enzyme inhibitory activity with an IC₅₀ values of 0.98, 1.69 and 1.44 µM, respectively as well as a synergistic antioxidant activity between the different fractions. Thus, we have demonstrated that underutilized wastes can be valorized by production of peptides that can be used as potential therapeutic compounds active against oxidative stress and hypertension.