dc.contributor.author | Marina Alegre, María Luisa | |
dc.contributor.author | Orellana Muriana, José María | |
dc.contributor.author | Vásquez Villanueva, Romy Ángela | |
dc.contributor.author | García López, María Concepción | |
dc.date.accessioned | 2020-10-19T10:41:58Z | |
dc.date.available | 2020-10-19T10:41:58Z | |
dc.date.issued | 2019-09-18 | |
dc.identifier.bibliographicCitation | Journal of Agricultural and Food Chemistry, 2019, v. 67, n. 37, p. 10313-10320 | en |
dc.identifier.issn | 0021-8561 | |
dc.identifier.uri | http://hdl.handle.net/10017/44648 | en |
dc.description.abstract | A peptide fraction with molecular masses below 3 kDa (PSH-3 kDa) from a peach seed hydrolysate demonstrated high angiotensin converting enzyme (ACE) inhibitory activity (concentration to inhibit 50% ACE (IC50) = 16.4 mu g/mL) in our previous work. This work proposes a further study of this highly active fraction. RP-HPLC enabled two fractions (F3 and F4) with high inhibitory activity (IC50 = 2.0 +/- 0.5 and 1.2 +/- 0.2 mu g/mL, respectively) to be isolated. Peptide analysis by LC-Q-TOF-MS/MS using reverse-phase and hydrophilic interaction chromatography enabled 33 peptides within both fractions to be identified. Among them, peptide isoleucine-tyrosine-serine-proline-histidine (IYSPH) showed the highest capacity. The lack of cytotoxicity of peptides was demonstrated in three different cell lines (HeLa, HT-29, and HK-2). Oral administration of PSH-3 kDa fraction or peptide IYSPH caused a significant systolic blood pressure reduction (-30 mmHg) on spontaneously hypertensive rats after 3-6 h treatment. | en |
dc.format.mimetype | application/pdf | en |
dc.language.iso | eng | en |
dc.rights | Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) | es_ES |
dc.rights | © ACS | en |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | en |
dc.subject | peach seed hydrolysate | en |
dc.subject | ACE-inhibitory peptides | en |
dc.subject | cytotoxic assay | en |
dc.subject | in vivo assay | en |
dc.subject | hypertension | en |
dc.subject | chromatography | en |
dc.subject | mass spectrometry | en |
dc.title | Isolation and characterization of angiotensin converting enzyme inhibitory peptides from peach seed hydrolysates: in vivo assessment of antihypertensive activity | en |
dc.type | info:eu-repo/semantics/article | en |
dc.subject.eciencia | Química | es_ES |
dc.subject.eciencia | Chemistry | en |
dc.contributor.affiliation | Universidad de Alcalá. Departamento de Química Analítica, Química Física e Ingeniería Química | |
dc.date.updated | 2020-10-19T10:41:28Z | |
dc.type.version | info:eu-repo/semantics/publishedVersion | en |
dc.identifier.doi | 10.1021/acs.jafc.9b02213 | en |
dc.relation.projectID | info:eu-repo/grantAgreement/CAM//S2018%2FBAA-4393/ES/ESTRATEGIAS INTEGRADAS PARA LA MEJORA DE LA CALIDAD, LA SEGURIDAD Y LA FUNCIONALIDAD DE LOS ALIMENTOS: HACIA UNA ALIMENTACIÓN SALUDABLE/AVANSECAL-II | es_ES |
dc.relation.projectID | info:eu-repo/grantAgreement/MINECO//AGL2016-79010-R/ES/DESARROLLO DE METODOS SOSTENIBLES PARA EL APROVECHAMIENTO DE SUBPRODUCTOS DE LA INDUSTRIA ALIMENTARIA CON ELEVADO CONTENIDO PROTEICO | es_ES |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | en |
dc.identifier.uxxi | AR/0000033549 | en |
dc.identifier.publicationtitle | Journal of Agricultural and Food Chemistry | en |
dc.identifier.publicationvolume | 67 | |
dc.identifier.publicationlastpage | 10320 | |
dc.identifier.publicationissue | 37 | |
dc.identifier.publicationfirstpage | 10313 | |