Purification and characterization of angiotensin converting enzyme-inhibitory peptides derived from Stichopus horrens: stability study against the ACE and inhibition kinetics
Stichopus horrens is the most popular species of sea cucumber due to strong beliefs of its numerous medicinal properties. In this study, ACE-inhibitory peptides of S. horrens generated through enzymatic hydrolysis using Alcalase were isolated. Three peptides EVSQGRP, CRQNTLGHNTQTSIAQ and VSRHFASYAN...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier BV
2016
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| Online Access: | http://psasir.upm.edu.my/id/eprint/53701/1/Purification%20and%20characterization%20of%20angiotensin%20converting%20enzyme-inhibitory%20peptides%20derived%20from%20Stichopus%20horrens.pdf |
| _version_ | 1796975937753972736 |
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| author | Forghani, Bita Zarei, Mohammad Ebrahimpour, Afshin Philip, Robin Bakar, Jamilah Abdul Hamid, Azizah Saari, Nazamid |
| author_facet | Forghani, Bita Zarei, Mohammad Ebrahimpour, Afshin Philip, Robin Bakar, Jamilah Abdul Hamid, Azizah Saari, Nazamid |
| author_sort | Forghani, Bita |
| collection | UPM |
| description | Stichopus horrens is the most popular species of sea cucumber due to strong beliefs of its numerous medicinal properties. In this study, ACE-inhibitory peptides of S. horrens generated through enzymatic hydrolysis using Alcalase were isolated. Three peptides EVSQGRP, CRQNTLGHNTQTSIAQ and VSRHFASYAN were found to exhibit high inhibition potency with IC50 values of 0.05, 0.08 and 0.21 mM, respectively. It was found that the EVSQGRP, VSRHFASYAN and SAAVGSP exhibiting mixed inhibition patterns were susceptible to degradation by ACE as well, suggesting that the mixed-mode inhibition could be a result of new generated peptide fragments while CRQNTLGHNTQTSIAQ inhibited ACE in a non-competitive manner. In-vivo ACE inhibition studies showed that 400 mg/kg of Alcalase-generated proteolysate stabilized the blood pressure in normotensive rats. These results suggest that the hydrolysed protein components of S. horrens possess bioactive peptides that can be exploited as functional food ingredients against hypertension. |
| first_indexed | 2024-03-06T09:18:36Z |
| format | Article |
| id | upm.eprints-53701 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2024-03-06T09:18:36Z |
| publishDate | 2016 |
| publisher | Elsevier BV |
| record_format | dspace |
| spelling | upm.eprints-537012018-01-08T10:25:56Z http://psasir.upm.edu.my/id/eprint/53701/ Purification and characterization of angiotensin converting enzyme-inhibitory peptides derived from Stichopus horrens: stability study against the ACE and inhibition kinetics Forghani, Bita Zarei, Mohammad Ebrahimpour, Afshin Philip, Robin Bakar, Jamilah Abdul Hamid, Azizah Saari, Nazamid Stichopus horrens is the most popular species of sea cucumber due to strong beliefs of its numerous medicinal properties. In this study, ACE-inhibitory peptides of S. horrens generated through enzymatic hydrolysis using Alcalase were isolated. Three peptides EVSQGRP, CRQNTLGHNTQTSIAQ and VSRHFASYAN were found to exhibit high inhibition potency with IC50 values of 0.05, 0.08 and 0.21 mM, respectively. It was found that the EVSQGRP, VSRHFASYAN and SAAVGSP exhibiting mixed inhibition patterns were susceptible to degradation by ACE as well, suggesting that the mixed-mode inhibition could be a result of new generated peptide fragments while CRQNTLGHNTQTSIAQ inhibited ACE in a non-competitive manner. In-vivo ACE inhibition studies showed that 400 mg/kg of Alcalase-generated proteolysate stabilized the blood pressure in normotensive rats. These results suggest that the hydrolysed protein components of S. horrens possess bioactive peptides that can be exploited as functional food ingredients against hypertension. Elsevier BV 2016-01 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/53701/1/Purification%20and%20characterization%20of%20angiotensin%20converting%20enzyme-inhibitory%20peptides%20derived%20from%20Stichopus%20horrens.pdf Forghani, Bita and Zarei, Mohammad and Ebrahimpour, Afshin and Philip, Robin and Bakar, Jamilah and Abdul Hamid, Azizah and Saari, Nazamid (2016) Purification and characterization of angiotensin converting enzyme-inhibitory peptides derived from Stichopus horrens: stability study against the ACE and inhibition kinetics. Journal of Functional Foods, 20. pp. 276-290. ISSN 1756-4646; ESSN: 2214-9414 http://www.sciencedirect.com/science/article/pii/S1756464615005228 10.1016/j.jff.2015.10.025 |
| spellingShingle | Forghani, Bita Zarei, Mohammad Ebrahimpour, Afshin Philip, Robin Bakar, Jamilah Abdul Hamid, Azizah Saari, Nazamid Purification and characterization of angiotensin converting enzyme-inhibitory peptides derived from Stichopus horrens: stability study against the ACE and inhibition kinetics |
| title | Purification and characterization of angiotensin converting enzyme-inhibitory peptides derived from Stichopus horrens: stability study against the ACE and inhibition kinetics |
| title_full | Purification and characterization of angiotensin converting enzyme-inhibitory peptides derived from Stichopus horrens: stability study against the ACE and inhibition kinetics |
| title_fullStr | Purification and characterization of angiotensin converting enzyme-inhibitory peptides derived from Stichopus horrens: stability study against the ACE and inhibition kinetics |
| title_full_unstemmed | Purification and characterization of angiotensin converting enzyme-inhibitory peptides derived from Stichopus horrens: stability study against the ACE and inhibition kinetics |
| title_short | Purification and characterization of angiotensin converting enzyme-inhibitory peptides derived from Stichopus horrens: stability study against the ACE and inhibition kinetics |
| title_sort | purification and characterization of angiotensin converting enzyme inhibitory peptides derived from stichopus horrens stability study against the ace and inhibition kinetics |
| url | http://psasir.upm.edu.my/id/eprint/53701/1/Purification%20and%20characterization%20of%20angiotensin%20converting%20enzyme-inhibitory%20peptides%20derived%20from%20Stichopus%20horrens.pdf |
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