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An individual alginate lyase is effective in the disruption of Laminaria digitata recalcitrant cell wall

dc.contributor.authorCosta, Monica
dc.contributor.authorPio, Luís Bernardo
dc.contributor.authorBule, Pedro
dc.contributor.authorCardoso, Vânia
dc.contributor.authorAlfaia, Cristina
dc.contributor.authorCoelho, Diogo
dc.contributor.authorBrás, Joana
dc.contributor.authorFontes, Carlos M.G.A.
dc.contributor.authorPrates, José A.M
dc.date.accessioned2021-11-09T13:15:42Z
dc.date.available2021-11-09T13:15:42Z
dc.date.issued2021-05-06
dc.descriptionResearch Areas: Science & Technology - Other Topicspt_PT
dc.description.abstractIn the present study, 199 pre-selected Carbohydrate-Active enZymes (CAZymes) and sulfatases were assessed, either alone or in combination, to evaluate their capacity to disrupt Laminaria digitata cell wall, with the consequent release of interesting nutritional compounds. A previously characterized individual alginate lyase, belonging to the family 7 of polysaccharide lyases (PL7) and produced by Saccharophagus degradans, was shown to be the most efcient in the in vitro degradation of L. digitata cell wall. The alginate lyase treatment, compared to the control, released up to 7.11 g/L of reducing sugars (p< 0.001) and 8.59 mmol/100 g dried alga of monosaccharides (p< 0.001), and reduced cell wall fuorescence intensity by 39.1% after staining with Calcofuor White (p= 0.001). The hydrolysis of gel-forming polymer alginate by the alginate lyase treatment could prevent the trapping of fatty acids and release benefcial monounsaturated fatty acids, particularly 18:1c9 (p < 0.001), to the extracellular medium. However, no liberation of proteins (p > 0.170) or pigments (p > 0.070) was observed. Overall, these results show the ability of an individual alginate lyase, from PL7 family, to partially degrade L. digitata cell wall under physiological conditions. Therefore, this CAZyme can potentially improve the bioavailability of L. digitata bioactive compounds for monogastric diets, with further application in feed industry.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationCosta M, Pio L, Bule P, Cardoso V, Alfaia CM, Coelho D, Bras J, Fontes CMGA, Prates JAM. 2021. An individual alginate lyase is effective in the disruption of Laminaria digitata recalcitrant cell wall. Scientific Reports, 11(1):9706. DOI:10.1038/s41598-021-89278-1pt_PT
dc.identifier.doi10.1038/s41598-021-89278-1pt_PT
dc.identifier.issn2045-2322
dc.identifier.urihttp://hdl.handle.net/10400.5/22535
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherNature Researchpt_PT
dc.relationDisclosing the potential of seaweeds for feeding pigs and poultry
dc.relationCentre for Interdisciplinary Research in Animal Health
dc.relationImproving the nutritional value of microalgae for feeding pigs through the use of novel enzymes
dc.relation.publisherversionhttps://www.nature.com/articles/s41598-021-89278-1.pdfpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectFatty-acid profilespt_PT
dc.subjectBarley-based dietspt_PT
dc.subjectExtracellular-matrixpt_PT
dc.subjectChlorella-vulgarispt_PT
dc.subjectPhenolic-compoundspt_PT
dc.subjectNutritive-valuept_PT
dc.subjectBrownpt_PT
dc.subjectExtractionpt_PT
dc.subjectAlgaept_PT
dc.subjectFucoxanthinpt_PT
dc.titleAn individual alginate lyase is effective in the disruption of Laminaria digitata recalcitrant cell wallpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleDisclosing the potential of seaweeds for feeding pigs and poultry
oaire.awardTitleCentre for Interdisciplinary Research in Animal Health
oaire.awardTitleImproving the nutritional value of microalgae for feeding pigs through the use of novel enzymes
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/9471 - RIDTI/PTDC%2FCAL-ZOO%2F30238%2F2017/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F00276%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F126198%2F2016/PT
oaire.citation.conferencePlaceGermanypt_PT
oaire.citation.issue9706pt_PT
oaire.citation.titleScientifc Reportspt_PT
oaire.citation.volume11(1)pt_PT
oaire.fundingStream9471 - RIDTI
oaire.fundingStream6817 - DCRRNI ID
person.familyNamePereira Ribeiro Pio
person.familyNameBule
person.familyNameCardoso Lopes
person.familyNameAlfaia
person.familyNameCoelho
person.familyNameFontes
person.familyNameMestre Prates
person.givenNameLuís Bernardo
person.givenNamePedro
person.givenNameVânia Alexandra da Silva
person.givenNameCristina Maria Riscado Pereira Mateus
person.givenNameDiogo
person.givenNameCarlos
person.givenNameJosé António
person.identifier6506672592
person.identifier.ciencia-id7017-5EE9-A60A
person.identifier.ciencia-id171E-F0CF-89F7
person.identifier.ciencia-id121B-B572-2236
person.identifier.ciencia-id7C16-D8D4-40C8
person.identifier.ciencia-id6A15-C6E1-71A0
person.identifier.ciencia-idC01A-FCB3-7F99
person.identifier.ciencia-id2617-53FF-04CD
person.identifier.orcid0000-0003-2531-9926
person.identifier.orcid0000-0001-8389-7543
person.identifier.orcid0000-0001-8648-2204
person.identifier.orcid0000-0001-6151-8186
person.identifier.orcid0000-0002-1219-9753
person.identifier.orcid0000-0003-1032-5987
person.identifier.ridK-9934-2013
person.identifier.scopus-author-id7005517465
person.identifier.scopus-author-id56003169500
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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