English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/155304
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:

DC FieldValueLanguage
dc.contributor.authorJemil, Ineses_ES
dc.contributor.authorAbdelhedi, Olaes_ES
dc.contributor.authorNasri, Rimes_ES
dc.contributor.authorMora, Leticiaes_ES
dc.contributor.authorJridi, Mourades_ES
dc.contributor.authorAristoy, María Concepciónes_ES
dc.contributor.authorToldrá Vilardell, Fideles_ES
dc.contributor.authorNasri, Moncefes_ES
dc.date.accessioned2017-09-20T06:58:43Z-
dc.date.available2017-09-20T06:58:43Z-
dc.date.issued2017-06-07-
dc.identifier.citationFood Research International 100 (1): 121-133 (2017)es_ES
dc.identifier.issn0963-9969-
dc.identifier.urihttp://hdl.handle.net/10261/155304-
dc.description.abstractSardinelle protein hydrolysate (SPH), prepared by treatment with Bacillus subtilis A26 proteases, was found to exhibit antibacterial, antioxidant and ACE-inhibitory activities. SPH, with a degree of hydrolysis of 4%, was fractionated by size exclusion chromatography on a Sephadex G-25 into five major fractions (F1–F5). F2, which exhibited the highest antibacterial and ACE-inhibitory activities, and F4, which exhibited the highest antibacterial and antioxidant activities, were further fractionated by reverse phase-high performance liquid chromatography (RP-HPLC) and then analysed using nano-ESI-LC-MS/MS to identify the sequences of peptides. Eight peptides were identified in the sub-fraction F2-A, nine peptides in the sub-fraction F4-B, and 45 peptides in F4-C. Identified peptides were found to share sequences with previously described bioactive peptides based on Biopep database. The results of this study suggest that SPH is a good source of natural bioactive peptides. Hence, it can be used as a potential ingredient in nutraceutical field.es_ES
dc.description.sponsorshipThis work was funded by the Ministry of Higher Education and Scientific Research-Tunisia. Grant AGL2014-57367-R from MINECO (Spain) and FEDER funds and JAEDOC-CSIC postdoctoral contract of L.M. cofounded by the European Social Found are acknowledged. LC-MS/MS analysis was carried out in the SCSIE University of Valencia Proteomics Unit (Spain), a member of ISCIII ProteoRed Proteomics Platform.es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.relationMINECO/ICTI2013-2016/AGL2014-57367-Res_ES
dc.relation.isversionofPostprintes_ES
dc.rightsopenAccessen_EN
dc.subjectSardinella auritaes_ES
dc.subjectProtein hydrolysatees_ES
dc.subjectAntibacteriales_ES
dc.subjectAnti-ACEes_ES
dc.subjectAntioxidantes_ES
dc.subjectPeptidees_ES
dc.titleNovel bioactive peptides from enzymatic hydrolysate of Sardinelle (Sardinella aurita) muscle proteins hydrolysed by Bacillus subtilis A26 proteaseses_ES
dc.typeartículoes_ES
dc.identifier.doihttp://dx.doi.org/10.1016/j.foodres.2017.06.018-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttps://doi.org/10.1016/j.foodres.2017.06.018es_ES
dc.embargo.terms2018-06-07es_ES
dc.rights.licensehttp://creativecommons.org/licenses/by-nc-nd/4.0/es_ES
dc.contributor.funderMinisterio de Economía y Competitividad (España)es_ES
dc.contributor.funderEuropean Commissiones_ES
dc.contributor.funderConsejo Superior de Investigaciones Científicas (España)es_ES
dc.contributor.funderMinistère de l’Enseignement Supérieur et de la Recherche Scientifique (Tunisie)es_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000780es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003339es_ES
Appears in Collections:(IATA) Artículos
Files in This Item:
File Description SizeFormat 
FoodResInt_ 2017_100_121-133.pdfArtículo principal1,05 MBAdobe PDFThumbnail
View/Open
Show simple item record
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.