Antioxidant and angiotensin-I converting enzyme inhibitory peptides from Hippocampus abdominalis

Bioactive peptides isolated from edible marine sources have been used as nutraceuticals and functional foods. The present study focuses on the alcalase hydrolysate of Hippocampus abdominalis for the isolation of antioxidative and angiotensin-I converting enzyme (ACE) inhibitory peptides. Initially,...

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Bibliographic Details
Published in:European food research & technology 2019-02, Vol.245 (2), p.479-487
Main Authors: Kim, Hyun-Soo, Je, Jun-Geon, Ryu, Bomi, Kang, Nalae, Shanura Fernando, I. P., Jayawardena, Thilina U., Asanka Sanjeewa, K. K., Oh, Jae-Young, Lee, Tae-Gee, Jeon, You-Jin
Format: Article
Language:English
Subjects:
Agriculture
Analytical Chemistry
Angiotensin
Antihypertensives
Antioxidants
Biological activity
Biotechnology
Chemistry
Chemistry and Materials Science
Chromatography
Conversion
Enzymes
Food Science
Forestry
Functional foods & nutraceuticals
Gel filtration
Hemiarthrus abdominalis
High performance liquid chromatography
Hippocampus
Hippocampus abdominalis
Hydrogen bonding
Hydrolysates
Liquid chromatography
Mass spectrometry
Mass spectroscopy
Molecular docking
Original Paper
Peptides
Proteolysis
Scavenging
Subtilisin
Ultrafiltration
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Summary:Bioactive peptides isolated from edible marine sources have been used as nutraceuticals and functional foods. The present study focuses on the alcalase hydrolysate of Hippocampus abdominalis for the isolation of antioxidative and angiotensin-I converting enzyme (ACE) inhibitory peptides. Initially, the H. abdominalis alcalase hydrolysate (HA) was separated using ultrafiltration (MWCO = 5 kDa), and have obtained the fraction, HA-III (MW ≤ 5 kDa), with strong bioactivity. This was further separated using gel filtration chromatography (Sephadex G-10) and reverse-phase high-performance liquid chromatography (RP-HPLC). The active Sephadex G-10 fraction was analyzed by the Q-TOF mass spectrometry, nine peptides were identified within the molecular mass range between 757.8 and 990.1 Da. Three peptides, GIIGPSGSP, IGTGIPGIW, and QIGFIW, showed strong ACE inhibitory activity and alkyl radical-scavenging activity. Molecular docking studies revealed that the ACE inhibitory activity of the three active peptides is mainly due to hydrogen bonding interactions and active site interactions between active peptides and ACE. This study demonstrated that the active peptides derived from H. abdominalis can be isolated and the proteolytic hydrolysates of it are potential antioxidant and antihypertensive agents.
ISSN:1438-2377
1438-2385
DOI:10.1007/s00217-018-3179-0