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dc.contributor.authorRodríguez-Amado, I.-
dc.contributor.authorVázquez, José Antonio-
dc.contributor.authorGonzález Fernández, Pilar-
dc.contributor.authorEsteban-Fernández, Diego-
dc.contributor.authorCarrera, Mónica-
dc.contributor.authorPiñeiro, Carmen-
dc.date.accessioned2014-10-03T08:33:05Z-
dc.date.available2014-10-03T08:33:05Z-
dc.date.issued2014-03-10-
dc.identifier.citationMarine Drugs 12(3): 1390-1405 (2014)es_ES
dc.identifier.urihttp://hdl.handle.net/10261/102893-
dc.description16 páginas, 2 tablas, 4 figuras.-- This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/)es_ES
dc.description.abstractThe aim of this work was the purification and identification of the major angiotensin converting enzyme (ACE) inhibitory peptides produced by enzymatic hydrolysis of a protein concentrate recovered from a cuttlefish industrial manufacturing effluent. This process consisted on the ultrafiltration of cuttlefish softening wastewater, with a 10 kDa cut-off membrane, followed by the hydrolysis with alcalase of the retained fraction. Alcalase produced ACE inhibitors reaching the highest activity (IC50 = 76.8 ± 15.2 μg mL−1) after 8 h of proteolysis. Sequential ultrafiltration of the 8 h hydrolysate with molecular weight cut-off (MWCO) membranes of 10 and 1 kDa resulted in the increased activity of each permeate, with a final IC50 value of 58.4 ± 4.6 μg mL−1. Permeate containing peptides lower than 1 kDa was separated by reversed-phase high performance liquid chromatography (RP-HPLC). Four fractions (A–D) with potent ACE inhibitory activity were isolated and their main peptides identified using high performance liquid chromatography coupled to an electrospray ion trap Fourier transform ion cyclotron resonance-mass spectrometer (HPLC-ESI-IT-FTICR) followed by comparison with databases and de novo sequencing. The amino acid sequences of the identified peptides contained at least one hydrophobic and/or a proline together with positively charged residues in at least one of the three C-terminal positions. The IC50 values of the fractions ranged from 1.92 to 8.83 μg mL−1, however this study fails to identify which of these peptides are ultimately responsible for the potent antihypertensive activity of these fractionses_ES
dc.description.sponsorshipThe company Frinova S.A. funded this study (Contract N° 20090732 co-financed by CDTI). The authors also thank the Unit of Information Resources for Research (URICI-CSIC) for the co-funding of this publication in Open Access format.es_ES
dc.language.isoenges_ES
dc.publisherMultidisciplinary Digital Publishing Institutees_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rightsopenAccess-
dc.subjectUltrafiltrationes_ES
dc.subjectProteolysises_ES
dc.subjectACE inhibitory peptideses_ES
dc.subjectCuttlefish byproductses_ES
dc.subjectPeptide identificationes_ES
dc.subjectHPLC-ESI-MSes_ES
dc.titleIdentification of the major ACE-inhibitory peptides produced by Eenzymatic hydrolysis of a protein concentrate from cuttlefish wastewateres_ES
dc.typeartículo-
dc.identifier.doi10.3390/md12031390-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.3390/md12031390es_ES
dc.identifier.e-issn1660-3397-
dc.rights.licensehttp://creativecommons.org/licenses/by/3.0es_ES
dc.contributor.funderConsejo Superior de Investigaciones Científicas (España)-
dc.relation.csices_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003339es_ES
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