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Isolation and Characterization of a New Angiotensin-converting Enzyme Inhibitory Peptide from Heterobronchus bidorsalis

Isolation and Characterization of a New Angiotensin-converting Enzyme Inhibitory Peptide from... AbstractAngiotensin converting enzyme (ACE) plays an important physiological role in the regulation of blood pressure by converting angiotensin I to angiotensin II, a potent vasoconstrictor; hence, its inhibition is a major target in the prevention and treatment of hypertension. In this study a novel ACE inhibitory peptide from Heterobronchus bidorsalis (cat fish) was isolated, purified and characterized. The peptide was purified by ammonium sulphate precipitation, dialysis and gel filtration chromatography (sephadex G-50). The amino acid sequence of the seventeen amino acid peptide was found to be KHRDTSEPGACVMILYF with a final inhibitory activity of 0.07 μmol/ml and a purification fold of 2.93 having a percentage yield of 34 %. The peptide had an optimum temperature and pH of 37°C and 8.3, respectively. The ACE inhibitory activity of the peptide reduced in the presence of sodium, calcium, magnesium, and potassium ions, while EDTA increased it when compared to the control. Treatment with trypsin also increased the inhibitory activity of the peptide. The peptide exhibited a non-competitive-type of inhibition, indicating that it binds to a site other than the active site. In conclusion, peptides from H. bidorsalis may be promising ACE inhibitors that can serve as nutraceuticals or drugs for blood pressure regulation in hypertensive patients. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Biologically Active Products from Nature Taylor & Francis

Isolation and Characterization of a New Angiotensin-converting Enzyme Inhibitory Peptide from Heterobronchus bidorsalis

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Isolation and Characterization of a New Angiotensin-converting Enzyme Inhibitory Peptide from Heterobronchus bidorsalis

Abdulazeez, Mansurah; Aminu, Hussain; Ndanusa, Sulaiman; Uba, Abdullahi
Journal of Biologically Active Products from Nature , Volume 6 (3): 13 – May 3, 2016

Abstract

AbstractAngiotensin converting enzyme (ACE) plays an important physiological role in the regulation of blood pressure by converting angiotensin I to angiotensin II, a potent vasoconstrictor; hence, its inhibition is a major target in the prevention and treatment of hypertension. In this study a novel ACE inhibitory peptide from Heterobronchus bidorsalis (cat fish) was isolated, purified and characterized. The peptide was purified by ammonium sulphate precipitation, dialysis and gel filtration chromatography (sephadex G-50). The amino acid sequence of the seventeen amino acid peptide was found to be KHRDTSEPGACVMILYF with a final inhibitory activity of 0.07 μmol/ml and a purification fold of 2.93 having a percentage yield of 34 %. The peptide had an optimum temperature and pH of 37°C and 8.3, respectively. The ACE inhibitory activity of the peptide reduced in the presence of sodium, calcium, magnesium, and potassium ions, while EDTA increased it when compared to the control. Treatment with trypsin also increased the inhibitory activity of the peptide. The peptide exhibited a non-competitive-type of inhibition, indicating that it binds to a site other than the active site. In conclusion, peptides from H. bidorsalis may be promising ACE inhibitors that can serve as nutraceuticals or drugs for blood pressure regulation in hypertensive patients.

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Publisher
Taylor & Francis
Copyright
© 2016, Har Krishan Bhalla & Sons
ISSN
2231-1874
eISSN
2231-1866
DOI
10.1080/22311866.2016.1232625
Publisher site
See Article on Publisher Site

Abstract

AbstractAngiotensin converting enzyme (ACE) plays an important physiological role in the regulation of blood pressure by converting angiotensin I to angiotensin II, a potent vasoconstrictor; hence, its inhibition is a major target in the prevention and treatment of hypertension. In this study a novel ACE inhibitory peptide from Heterobronchus bidorsalis (cat fish) was isolated, purified and characterized. The peptide was purified by ammonium sulphate precipitation, dialysis and gel filtration chromatography (sephadex G-50). The amino acid sequence of the seventeen amino acid peptide was found to be KHRDTSEPGACVMILYF with a final inhibitory activity of 0.07 μmol/ml and a purification fold of 2.93 having a percentage yield of 34 %. The peptide had an optimum temperature and pH of 37°C and 8.3, respectively. The ACE inhibitory activity of the peptide reduced in the presence of sodium, calcium, magnesium, and potassium ions, while EDTA increased it when compared to the control. Treatment with trypsin also increased the inhibitory activity of the peptide. The peptide exhibited a non-competitive-type of inhibition, indicating that it binds to a site other than the active site. In conclusion, peptides from H. bidorsalis may be promising ACE inhibitors that can serve as nutraceuticals or drugs for blood pressure regulation in hypertensive patients.

Journal

Journal of Biologically Active Products from Nature – Taylor & Francis

Published: May 3, 2016

Keywords: Angiotensin converting enzyme; hypertension; Heterobronchus bidorsalis; peptide

References

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