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Harnessing the bioactive potential of Limonium spathulatum (Desf.) Kuntze: insights into enzyme inhibition and phytochemical profile

2023-09-26Journal article Open access
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dc.contributor.authorYoussef, Seria
dc.contributor.authorCustódio, Luísa
dc.contributor.authorRodrigues, Maria João
dc.contributor.authorPereira, Catarina
dc.contributor.authorCalhelha, Ricardo C.
dc.contributor.authorJekő, József
dc.contributor.authorCziáky, Zoltán
dc.contributor.authorBen Hamed, Karim
dc.date.accessioned2023-10-23T10:23:03Z
dc.date.available2023-10-23T10:23:03Z
dc.date.issued2023-09-26
dc.date.updated2023-10-13T12:07:50Z
dc.description.abstractThis study assessed the halophyte species <i>Limonium spathulatum</i> (Desf.) as a possible source of natural ingredients with the capacity to inhibit enzymes related to relevant human health disorders and food browning. Extracts using food-grade solvents such as water and ethanol were prepared by maceration from dried <i>L. spathulatum</i> leaves. They were evaluated for in vitro inhibition activity of enzymes such as acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), α-glucosidase, tyrosinase and lipase, related to Alzheimer’s disease, type-2-diabetes mellitus, skin hyperpigmentation, and obesity, respectively. These extracts were also appraised for in vitro acute toxicity on tumoral and non-tumoral cell lines and their chemical composition by high-performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC-ESI-MS/MS). The extracts were more effective towards BChE than AChE. The best results were obtained with the hydroethanolic and water extracts, with IC<sub>50</sub> values of 0.03 mg/mL and 0.06 mg/mL, respectively. The hydroethanolic extract had the highest capacity to inhibit α-glucosidase (IC<sub>50</sub>: 0.04 mg/mL), higher than the positive control used (acarbose, IC<sub>50</sub> = 3.14 mg/mL). The ethanol extract displayed the best inhibitory activity against tyrosinase (IC<sub>50</sub> = 0.34 mg/mL). The tested samples did not inhibit lipase and exhibited low to moderate cytotoxic activity against the tested cell lines. The hydroethanolic extract had a higher diversity of compounds, followed by the ethanol and water samples. Similar molecules were identified in all the extracts and were mainly hydroxybenzoic acids, hydroxycinnamic acids, and flavonoids. Taken together, these results suggest that <i>L. spathulatum</i> should be further explored as a source of bioactive ingredients for the food, cosmetic, and pharmaceutical industries.pt_PT
dc.description.sponsorshipProject HaloFarMs, which is part of the Partnership on Research and Innovation in the Mediterranean Area (PRIMA), funded by FCT in Portugal and the Ministry of High Education and Scientific Research in Tunisia.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifierdoi: 10.3390/plants12193391
dc.identifier.citationPlants 12 (19): 3391 (2023)pt_PT
dc.identifier.doi10.3390/plants12193391pt_PT
dc.identifier.issn2223-7747
dc.identifier.urihttp://hdl.handle.net/10400.1/20083
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relationNot Available
dc.relationMountain Research Center
dc.relationNot Available
dc.relationAlgarve Centre for Marine Sciences
dc.relationAlgarve Centre for Marine Sciences
dc.relationExploring salt tolerant plants as sources of innovative food additives
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectSea lavenderpt_PT
dc.subjectEnzyme inhibitorspt_PT
dc.subjectPhenolic compoundspt_PT
dc.subjectCytotoxicitypt_PT
dc.titleHarnessing the bioactive potential of Limonium spathulatum (Desf.) Kuntze: insights into enzyme inhibition and phytochemical profilept_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleNot Available
oaire.awardTitleMountain Research Center
oaire.awardTitleNot Available
oaire.awardTitleAlgarve Centre for Marine Sciences
oaire.awardTitleAlgarve Centre for Marine Sciences
oaire.awardTitleExploring salt tolerant plants as sources of innovative food additives
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/CEEC IND 2017/CEECIND%2F00425%2F2017%2FCP1391%2FCT0001/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F00690%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/CEEC IND 2018/CEECIND%2F01011%2F2018%2FCP1578%2FCT0002/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04326%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04326%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBAA-AGR%2F1391%2F2020/PT
oaire.citation.issue19pt_PT
oaire.citation.startPage3391pt_PT
oaire.citation.titlePlantspt_PT
oaire.citation.volume12pt_PT
oaire.fundingStreamCEEC IND 2017
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStreamCEEC IND 2018
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream3599-PPCDT
person.familyNameCustódio
person.familyNameGuerreiro Pereira
person.givenNameLuísa
person.givenNameCatarina Alexandra
person.identifierNmxO5SIAAAAJ
person.identifier.ciencia-id791B-C560-AEA2
person.identifier.ciencia-id4512-3435-689C
person.identifier.orcid0000-0003-4338-7703
person.identifier.orcid0000-0002-1131-8773
person.identifier.ridM-6101-2013
person.identifier.scopus-author-id15831018900
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.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
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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