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Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity, Antioxidant Properties, Phenolic Content and Amino Acid Profiles of Fucus spiralis L. Protein Hydrolysate Fractions

dc.contributor.authorPaiva, Lisete S.
dc.contributor.authorLima, Elisabete
dc.contributor.authorNeto, Ana I.
dc.contributor.authorBaptista, José
dc.date.accessioned2022-03-16T13:01:39Z
dc.date.available2022-03-16T13:01:39Z
dc.date.issued2017-10
dc.date.updated2022-01-28T17:58:17Z
dc.description.abstractFood protein-derived hydrolysates with multi-bioactivities such as antihypertensive and antioxidant properties have recently received special attention since both activities can play significant roles in preventing cardiovascular diseases. This study reports, for the first time, the angiotensin I-converting enzyme (ACE)-inhibition and antioxidant properties of ultrafiltrate fractions (UF) with different molecular weight ranges (<1, 1–3 and ≥3 kDa) obtained from Fucus spiralis protein hydrolysate (FSPH) digested with cellulase–bromelain. The amino acids profile, recovery yield, protein, peptide and total phenolic contents of these FSPH-UF, and the in vitro digestibility of F. spiralis crude protein were also investigated. FSPH-UF ≥3 kDa presented remarkably higher ACE-inhibition, yield, peptide and polyphenolic (phlorotannins) contents. Antioxidant analysis showed that FSPH-UF <1 kDa and ≥3 kDa exhibited significantly higher scavenging of 2,2-diphenyl-1-picrylhydrazyl radical and ferrous ion-chelating (FIC) activity. FSPH-UF ≥3 kDa had also notably higher ferric reducing antioxidant power (FRAP). Strong correlations were observed between ACE-inhibition and antioxidant activities (FIC and FRAP). The results suggest that ACE-inhibition and antioxidant properties of FSPH-UF may be due to the bioactive peptides and polyphenols released during the enzymatic hydrolysis. In conclusion, this study shows the potential use of defined size FSPH-UF for the prevention/treatment of hypertension and/or oxidative stress-related diseases.en
dc.description.sponsorshipThis study was financially supported 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. (2017). Angiotensin I-converting enzyme (ACE) inhibitory activity, antioxidant properties, phenolic content and amino acid profiles of fucus spiralis L. Protein hydrolysate fractions. “Marine Drugs”, 15(10). https://doi.org/10.3390/md15100311en
dc.identifier.doi10.3390/md15100311pt_PT
dc.identifier.issn1660-3397
dc.identifier.pmcPMC5666419
dc.identifier.pmid29027934
dc.identifier.slugcv-prod-2687107
dc.identifier.urihttp://hdl.handle.net/10400.3/6242
dc.identifier.wos000414593200018
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectEdible Brown Algaeen
dc.subjectProtein Enzymatic Hydrolysateen
dc.subjectUltrafiltrationen
dc.subjectAce-Inhibitionen
dc.subjectAntioxidant Propertiesen
dc.subjectPhlorotanninsen
dc.subjectPeptide Fractionsen
dc.subjectAmino Acids Compositionen
dc.subjectMarine Functional Foodsen
dc.subjectCardiovascular-Healthen
dc.titleAngiotensin I-Converting Enzyme (ACE) Inhibitory Activity, Antioxidant Properties, Phenolic Content and Amino Acid Profiles of Fucus spiralis L. Protein Hydrolysate Fractionsen
dc.typejournal article
dspace.entity.typePublication
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FBIA%2F00329%2F2013/PT
oaire.citation.conferencePlaceSwitzerlanden
oaire.citation.endPage18pt_PT
oaire.citation.issue(10)pt_PT
oaire.citation.startPage1pt_PT
oaire.citation.titleMarine Drugsen
oaire.citation.volume15pt_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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