Angiotensin I-converting enzyme inhibitory peptides from an enzymatic hydrolysate of flounder fish (Paralichthys olivaceus) muscle as a potent anti-hypertensive agent. Issue 4 (April 2016)
- Record Type:
- Journal Article
- Title:
- Angiotensin I-converting enzyme inhibitory peptides from an enzymatic hydrolysate of flounder fish (Paralichthys olivaceus) muscle as a potent anti-hypertensive agent. Issue 4 (April 2016)
- Main Title:
- Angiotensin I-converting enzyme inhibitory peptides from an enzymatic hydrolysate of flounder fish (Paralichthys olivaceus) muscle as a potent anti-hypertensive agent
- Authors:
- Ko, Ju-Young
Kang, Nalae
Lee, Ji-Hyeok
Kim, Jin-Soo
Kim, Won-Suck
Park, Sun-Joo
Kim, Yong-Tae
Jeon, You-Jin - Abstract:
- Graphical abstract: Highlights: The two ACE inhibitory peptides were purified from hydrolysate of FFM. Hydrolysate of FFM showed an antihypertensive effect in SHR model. Hydrolysate of FFM is useful as functional foods and materials for a potent anti-hypertension. Abstract: The aim of this study was to purify peptides with anti-hypertensive properties from a hydrolysate of flounder fish muscle. Among four proteolytic hydrolysates, pepsin showed the strongest angiotensin-I converting enzyme (ACE) inhibitory activity. The pepsin hydrolysate was fractionated by ultrafiltration, gel filtration chromatography and reverse-phase high performance liquid chromatography, and two novel peptides were purified. The IC50 values of the two peptides were 79 μM and 105 μM, respectively, and the Lineweaver–Burk plots suggested that they act as a competitive and a non-competitive inhibitor of ACE, respectively. Moreover, we predicted the 3D structure of ACE and used a molecular docking program to simulate binding between ACE and the peptides. These molecular modeling results indicated strong binding and interaction energies, and systolic blood pressures were reduced by administration of both peptides in spontaneously hypertensive rats. These results suggested that the enzymatic hydrolysate of flounder fish muscle includes novel ACE inhibitory peptides that may be beneficial as a functional food for treating hypertension.
- Is Part Of:
- Process biochemistry. Volume 51:Issue 4(2016:Apr.)
- Journal:
- Process biochemistry
- Issue:
- Volume 51:Issue 4(2016:Apr.)
- Issue Display:
- Volume 51, Issue 4 (2016)
- Year:
- 2016
- Volume:
- 51
- Issue:
- 4
- Issue Sort Value:
- 2016-0051-0004-0000
- Page Start:
- 535
- Page End:
- 541
- Publication Date:
- 2016-04
- Subjects:
- Paralichthys olivaceus -- ACE inhibitory peptide -- Enzymatic hydrolysis -- Pepsin -- Hypertension
Biochemical engineering -- Periodicals
Biotechnology -- Periodicals
Biochemistry -- periodicals
Biotechnology -- periodicals
Chemical Engineering -- periodicals
Génie biochimique -- Périodiques
Biotechnologie -- Périodiques
Biochemical engineering
Biotechnology
Periodicals
660.63 - Journal URLs:
- http://www.sciencedirect.com/science/journal/13595113 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.procbio.2016.01.009 ↗
- Languages:
- English
- ISSNs:
- 1359-5113
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6849.983500
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