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Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate

dc.contributor.authorPaiva, Lisete S.
dc.contributor.authorLima, Elisabete
dc.contributor.authorNeto, Ana I.
dc.contributor.authorBaptista, José
dc.date.accessioned2022-03-11T11:27:10Z
dc.date.available2022-03-11T11:27:10Z
dc.date.issued2016-10
dc.date.updated2022-01-28T17:52:11Z
dc.description.abstractUlva 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.sponsorshipThis 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.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationPaiva, 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.2016.07.006en
dc.identifier.doi10.1016/j.jff.2016.07.006pt_PT
dc.identifier.issn1756-4646
dc.identifier.slugcv-prod-2687093
dc.identifier.urihttp://hdl.handle.net/10400.3/6239
dc.identifier.wos000386193400007
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.subjectACE-inhibitory Peptidesen
dc.subjectEnzymatic Hydrolysisen
dc.subjectHypertensionen
dc.subjectInhibition Kineticen
dc.subjectMacroalgaept_PT
dc.subjectSimulated Gastrointestinal Digestionen
dc.titleIsolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysateen
dc.typejournal article
dspace.entity.typePublication
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FBIA%2F00329%2F2013/PT
oaire.citation.conferencePlaceNetherlandsen
oaire.citation.endPage76pt_PT
oaire.citation.startPage65pt_PT
oaire.citation.titleJournal of Functional Foodsen
oaire.citation.volume26pt_PT
oaire.fundingStream5876
person.familyNameNeto
person.givenNameAna
person.identifier.ciencia-idF412-5515-7324
person.identifier.orcid0000-0003-0708-5636
person.identifier.ridC-1505-2010
person.identifier.scopus-author-id7102618919
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.cv.cienciaidF015-95D2-365B | Lisete Sousa Paiva
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication5a4f5ed1-4800-4d46-932d-b4063eaa8d14
relation.isAuthorOfPublication.latestForDiscovery5a4f5ed1-4800-4d46-932d-b4063eaa8d14
relation.isProjectOfPublication7eec27e2-98c2-484f-a596-8df735e12eb3
relation.isProjectOfPublication.latestForDiscovery7eec27e2-98c2-484f-a596-8df735e12eb3

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