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dc.contributor.authorLassoued, Imenes_ES
dc.contributor.authorMora, Leticiaes_ES
dc.contributor.authorBarkia, Ahmedes_ES
dc.contributor.authorAristoy, María Concepciónes_ES
dc.contributor.authorNasri, Moncefes_ES
dc.contributor.authorToldrá Vilardell, Fideles_ES
dc.date.accessioned2016-10-07T11:41:22Z-
dc.date.available2016-10-07T11:41:22Z-
dc.date.issued2016-05-21-
dc.identifier.citationInternational Journal of Food Science & Technology 51 (7): 1604-1609 (2016)es_ES
dc.identifier.issn0950-542-
dc.identifier.urihttp://hdl.handle.net/10261/137905-
dc.description.abstractAngiotensin I-converting enzyme (ACE) inhibitory peptides have been searched in thornback ray (Raja clavata) muscle hydrolysed with Bacillus subtilis A26 proteases until a hydrolysis degree of 18.35%. The hydrolysate showed an IC50 of 0.83 mg mL−1. To identify peptides responsible for this activity, the extract was eluted through size-exclusion chromatography and fractions collected. The highest ACE inhibitory activity was found for fractions F2 and F3 which had IC50 of 0.42 and 0.51 mg mL−1, respectively. These fractions were analysed by nano-liquid chromatography coupled to tandem mass spectrometry (nLC-MS/MS). A total of 131 and 108 peptide sequences mainly derived from actin, myosin heavy chain and procollagen alpha 1 chain proteins were identified in fractions F2 and F3, respectively. FQPSF and LKYPI showed the best results with an IC50 of 12.56 and 27.07 μM, respectively. These results prove the potential of thornback ray muscle hydrolysate as a source of ACE inhibitory peptides.es_ES
dc.description.sponsorshipThis work was funded by a grant from the Ministry of Higher Education and Scientific Research of Tunisia and grant Prometeo/2012/001 from Conselleria d´Educació Cultura i Sport of Generalitat Valenciana, both are acknowledged. JAEDOC- CSIC postdoctoral contract cofounded by ESF to L.M. is also acknowledgedes_ES
dc.language.isoenges_ES
dc.publisherJohn Wiley & Sonses_ES
dc.relation.isversionofPostprintes_ES
dc.rightsopenAccessen_EN
dc.subjectAngiotensin I-converting enzyme inhibitory activityes_ES
dc.subjectBacillus subtilis A26 hydrolysatees_ES
dc.subjectMass spectrometryes_ES
dc.subjectProteomicses_ES
dc.subjectThornback rayes_ES
dc.titleAngiotensin I-converting enzyme inhibitory peptides FQPSF and LKYPI identified in Bacillus subtilis A26 hydrolysate of thornback ray muscle Authorses_ES
dc.typeartículoes_ES
dc.identifier.doi10.1111/ijfs.13130-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1111/ijfs.13130es_ES
dc.embargo.terms2017-05-21es_ES
dc.contributor.funderMinistère de l’Enseignement Supérieur et de la Recherche Scientifique (Tunisie)es_ES
dc.contributor.funderGeneralitat Valencianaes_ES
dc.contributor.funderConsejo Superior de Investigaciones Científicas (España)es_ES
dc.contributor.funderEuropean Commissiones_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003359es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003339es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000780es_ES
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextopen-
item.openairetypeartículo-
item.fulltextWith Fulltext-
item.languageiso639-1en-
item.cerifentitytypePublications-
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