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Exploring the Multifaceted Potential of a Peptide Fraction Derived from Saccharomyces cerevisiae Metabolism

2023-08-18Artigo científico Acesso aberto
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dc.contributor.authorBranco, Patrícia
dc.contributor.authorMaurício, Elisabete Muchagato
dc.contributor.authorCosta, Ana
dc.contributor.authorVentura, Diogo
dc.contributor.authorRoma-Rodrigues, Catarina
dc.contributor.authorDuarte, Maria Paula
dc.contributor.authorFernandes, Alexandra R.
dc.contributor.authorPrista, Catarina
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.institutionDCV - Departamento de Ciências da Vida
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.institutionMEtRICS - Centro de Engenharia Mecânica e Sustentabilidade de Recursos
dc.contributor.pblMDPI - Multidisciplinary Digital Publishing Institute
dc.date.accessioned2023-11-10T22:11:16Z
dc.date.available2023-11-10T22:11:16Z
dc.date.issued2023-08-18
dc.descriptionFunding Information: The present work was financed by Research Unit, Linking Landscape, Environment, Agriculture and Food (LEAF), in the scope of the project LEAF. The authors thank to LEAF and to FCT for the financial support of this work. Publisher Copyright: © 2023 by the authors.
dc.description.abstractThe rising demand for minimally processed, natural, and healthier food products has led to the search for alternative and multifunctional bioactive food components. Therefore, the present study focuses on the functional proprieties of a peptide fraction derived from Saccharomyces cerevisiae metabolism. The antimicrobial activity of the peptide fraction is evaluated against various foodborne pathogens, including Candida albicans, Candida krusei, Escherichia coli, Listeria monocytogenes, and Salmonella sp. The peptide fraction antioxidant properties are assessed using FRAP and DPPH scavenging capacity assays. Furthermore, the peptide fraction’s cytotoxicity is evaluated in colorectal carcinoma and normal colon epithelial cells while its potential as an antidiabetic agent is investigated through α-amylase and α-glucosidase inhibitory assays. The results demonstrate that the 2–10 kDa peptide fraction exhibits antimicrobial effects against all tested microorganisms, except C. krusei. The minimal inhibitory concentration for E. coli, L. monocytogenes, and Salmonella sp. remains consistently low, at 0.25 mg/mL, while C. albicans requires a higher concentration of 1.0 mg/mL. Furthermore, the peptide fraction displays antioxidant activity, as evidenced by DPPH radical scavenging activity of 81.03%, and FRAP values of 1042.50 ± 32.5 µM TE/mL at 1.0 mg/mL. The peptide fraction exhibits no cytotoxicity in both tumor and non-tumoral human cells at a concentration up to 0.3 mg/mL. Moreover, the peptide fraction presents anti-inflammatory activity, significantly reducing the expression of the TNFα gene by more than 29.7% in non-stimulated colon cells and by 50% in lipopolysaccharide-stimulated colon cells. It also inhibits the activity of the carbohydrate digestive enzymes α-amylase (IC50 of 199.3 ± 0.9 µg/mL) and α-glucosidase (IC20 of 270.6 ± 6.0 µg/mL). Overall, the findings showed that the peptide fraction exhibits antibacterial, antioxidant, anti-inflammatory, and antidiabetic activity. This study represents a step forward in the evaluation of the functional biological properties of S. cerevisiae bioactive peptides.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent17
dc.format.extent1678325
dc.identifier.doi10.3390/antibiotics12081332
dc.identifier.issn2079-6382
dc.identifier.otherPURE: 75829374
dc.identifier.otherPURE UUID: ee984a81-a4d7-4b3e-b39f-5f735aae25ed
dc.identifier.otherScopus: 85169043785
dc.identifier.otherWOS: 001056168800001
dc.identifier.otherPubMed: 37627752
dc.identifier.otherPubMedCentral: PMC10451726
dc.identifier.otherORCID: /0000-0003-2054-4438/work/151392214
dc.identifier.urihttp://hdl.handle.net/10362/159836
dc.identifier.urlhttps://www.scopus.com/pages/publications/85169043785
dc.language.isoeng
dc.peerreviewedyes
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04129%2F2020/PT
dc.relationLinking Landscape, Environment, Agriculture and Food
dc.relationApplied Molecular Biosciences Unit
dc.relationApplied Molecular Biosciences Unit
dc.relationInstitute for Health and Bioeconomy
dc.relationMechanical Engineering and Resource Sustainability Center
dc.relationMechanical Engineering and Resource Sustainability Center
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04077%2F2020/PT
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04077%2F2020/PT
dc.subjectanti-inflammatory activity
dc.subjectantidiabetic activity
dc.subjectantimicrobial peptides
dc.subjectantioxidant activity
dc.subjectbioactive metabolites
dc.subjectbiopreservatives
dc.subjectfoodborne pathogens
dc.subjectSaccharomyces cerevisiae
dc.subjectMicrobiology
dc.subjectBiochemistry
dc.subjectPharmacology, Toxicology and Pharmaceutics(all)
dc.subjectMicrobiology (medical)
dc.subjectInfectious Diseases
dc.subjectPharmacology (medical)
dc.subjectSDG 3 - Good Health and Well-being
dc.titleExploring the Multifaceted Potential of a Peptide Fraction Derived from Saccharomyces cerevisiae Metabolismen
dc.title.subtitleAntimicrobial, Antioxidant, Antidiabetic, and Anti-Inflammatory Propertiesen
dc.typejournal article
degois.publication.issue8
degois.publication.titleAntibiotics
degois.publication.volume12
dspace.entity.typePublication
oaire.awardNumberUIDB/04129/2020
oaire.awardNumberUIDP/04378/2020
oaire.awardNumberUIDB/04378/2020
oaire.awardNumberLA/P/0140/2020
oaire.awardNumberUIDB/04077/2020
oaire.awardNumberUIDP/04077/2020
oaire.awardTitleLinking Landscape, Environment, Agriculture and Food
oaire.awardTitleApplied Molecular Biosciences Unit
oaire.awardTitleApplied Molecular Biosciences Unit
oaire.awardTitleInstitute for Health and Bioeconomy
oaire.awardTitleMechanical Engineering and Resource Sustainability Center
oaire.awardTitleMechanical Engineering and Resource Sustainability Center
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04129%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04378%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04378%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/LA%2FP%2F0140%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04077%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04077%2F2020/PT
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
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project.funder.identifierhttp://doi.org/10.13039/501100001871
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rcaap.rightsopenAccess
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