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dc.contributor.authorKaroud, Wafaes_ES
dc.contributor.authorSila, Assaâdes_ES
dc.contributor.authorKrichen, Fatmaes_ES
dc.contributor.authorMartínez Álvarez, Óscares_ES
dc.contributor.authorBougatef, Alies_ES
dc.date.accessioned2019-02-04T08:30:19Z-
dc.date.available2019-02-04T08:30:19Z-
dc.date.issued2019-
dc.identifier.citationWaste and Biomass Valorization 10(2): 287-297 (2019)es_ES
dc.identifier.issn1877-2641-
dc.identifier.urihttp://hdl.handle.net/10261/175139-
dc.description.abstractThe present study reports the surface and antioxidant properties, as well as the angiotensin-I converting enzyme (ACE) inhibitory activity of protein hydrolysates (HHPHs) from European hake (Merluccius merluccius) heads and obtained with Savinase®. Hake heads protein hydrolysates contained high protein content between 84.75 and 87.92% and a high percentage of essential amino acids. They have a high nutritional value and could be used as supplement in poorly balanced dietary proteins. All protein hydrolysates possessed interesting surface properties, which were governed by their concentrations Hake heads protein hydrolysates displayed a high ACE inhibitory activity. The IC50 values recorded for the ACE inhibitory activity of all HHPHs varied between 0.24 and 1.4 mg/mL. Therefore, HHPHs can be used as a promising source of functional peptides with good surface and biological properties.es_ES
dc.language.isoenges_ES
dc.publisherSpringer Naturees_ES
dc.rightsclosedAccesses_ES
dc.subjectMerluccius merlucciuses_ES
dc.subjectHeadses_ES
dc.subjectProtein hydrolysateses_ES
dc.subjectSurface propertieses_ES
dc.subjectBiological activitieses_ES
dc.titleCharacterization, surface properties and biological activities of protein hydrolysates obtained from hake (Merluccius merluccius) headses_ES
dc.typeartículoes_ES
dc.identifier.doi10.1007/s12649-017-0069-9-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttps://doi.org/10.1007/s12649-017-0069-9es_ES
dc.identifier.e-issn1877-265X-
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
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