Publication
Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate
dc.contributor.author | Paiva, Lisete S. | |
dc.contributor.author | Lima, Elisabete | |
dc.contributor.author | Neto, Ana I. | |
dc.contributor.author | Baptista, José | |
dc.date.accessioned | 2022-03-11T11:27:10Z | |
dc.date.available | 2022-03-11T11:27:10Z | |
dc.date.issued | 2016-10 | |
dc.date.updated | 2022-01-28T17:52:11Z | |
dc.description.abstract | Ulva rigida protein was hydrolysed with pepsin plus bromelain after a screening of nine enzymes for optimal proteolysis. This hydrolysate, presenting ACE-inhibitory activity with an IC₅₀ value of 0.483 mg/mL, was fractionated by ultrafiltration membranes into three molecular weight ranges (<1 kDa, 1–3 kDa and >3 kDa). The <1 kDa fraction that exhibited the highest activity (IC₅₀: 0.095 mg/mL) was purified using size-exclusion chromatography and reversed-phase high-performance liquid chromatography, yielding two active ACE-inhibitory purified peptides. Edman degradation revealed its amino acid sequences to be IP and AFL with IC₅₀ values of 0.020 and 0.023 mg/mL, respectively. Both peptides were synthesized to confirm the structure and to validate their ACE-inhibitory activities. Lineweaver–Burk plots suggest that IP acts as a non-competitive and AFL as a competitive ACE-inhibitors. Stability assays showed that both peptides are heat-stable and AFL is hydrolysed by intestinal mucosa peptidases to FL with IC₅₀ value of 0.004 mg/mL that acts as a non-competitive ACE-inhibitor. The results suggest that these peptides might have a potential use in the preparation of antihypertensive drugs or functional foods. | en |
dc.description.sponsorship | This study was financially supported by funds from CIRN (Centro de Investigação de Recursos Naturais, University of the Azores) and by cE3c funding (Ref: UID/BIA/00329/2013). Lisete Paiva was supported by a doctoral grant (Ref: M3.1.2/F/014/2011) awarded by FRC (Fundo Regional da Ciência). | en |
dc.description.version | info:eu-repo/semantics/publishedVersion | pt_PT |
dc.identifier.citation | Paiva, L., Lima, E., Baptista, J., & Neto, A. I.. (2016). Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate. “Journal of Functional Foods”, 26, 65–76. https://doi.org/10.1016/j.jff.2016.07.006 | en |
dc.identifier.doi | 10.1016/j.jff.2016.07.006 | pt_PT |
dc.identifier.issn | 1756-4646 | |
dc.identifier.slug | cv-prod-2687093 | |
dc.identifier.uri | http://hdl.handle.net/10400.3/6239 | |
dc.identifier.wos | 000386193400007 | |
dc.language.iso | eng | pt_PT |
dc.peerreviewed | yes | pt_PT |
dc.publisher | Elsevier | pt_PT |
dc.subject | ACE-inhibitory Peptides | en |
dc.subject | Enzymatic Hydrolysis | en |
dc.subject | Hypertension | en |
dc.subject | Inhibition Kinetic | en |
dc.subject | Macroalgae | pt_PT |
dc.subject | Simulated Gastrointestinal Digestion | en |
dc.title | Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate | en |
dc.type | journal article | |
dspace.entity.type | Publication | |
oaire.awardURI | info:eu-repo/grantAgreement/FCT/5876/UID%2FBIA%2F00329%2F2013/PT | |
oaire.citation.conferencePlace | Netherlands | en |
oaire.citation.endPage | 76 | pt_PT |
oaire.citation.startPage | 65 | pt_PT |
oaire.citation.title | Journal of Functional Foods | en |
oaire.citation.volume | 26 | pt_PT |
oaire.fundingStream | 5876 | |
person.familyName | Neto | |
person.givenName | Ana | |
person.identifier.ciencia-id | F412-5515-7324 | |
person.identifier.orcid | 0000-0003-0708-5636 | |
person.identifier.rid | C-1505-2010 | |
person.identifier.scopus-author-id | 7102618919 | |
project.funder.identifier | http://doi.org/10.13039/501100001871 | |
project.funder.name | Fundação para a Ciência e a Tecnologia | |
rcaap.cv.cienciaid | F015-95D2-365B | Lisete Sousa Paiva | |
rcaap.rights | openAccess | pt_PT |
rcaap.type | article | pt_PT |
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