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dc.provenanceCONICET-
dc.creatorCorrons, María Alicia-
dc.creatorLiggieri, Constanza Silvina-
dc.creatorTrejo, Sebastian Alejandro-
dc.creatorBruno, Mariela Anahí-
dc.date2018-06-21T17:01:49Z-
dc.date2018-06-21T17:01:49Z-
dc.date2017-03-
dc.date2018-06-21T13:01:19Z-
dc.date.accessioned2019-04-29T15:37:42Z-
dc.date.available2019-04-29T15:37:42Z-
dc.date.issued2017-03-
dc.identifierCorrons, María Alicia; Liggieri, Constanza Silvina; Trejo, Sebastian Alejandro; Bruno, Mariela Anahí; ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex; Elsevier Science; Food Research International; 93; 3-2017; 8-15-
dc.identifier0963-9969-
dc.identifierhttp://hdl.handle.net/11336/49568-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/298045-
dc.descriptionIn work reported here, a proteolytic extract prepared from Maclura pomifera latex was employed to hydrolyze bovine caseins. Densitograms of Tricine–sodium-dodecyl-sulfate–polyacrylamide-gel electrophoresis (SDS-PAGE) indicated that the caseins were considerably degraded after a 10-min reaction. The degree of hydrolysis determined by the 2,4,6-trinitrobenzenesulfonic-acid method was 17.1���0.7% after 180�min of digestion. The concentration of small peptides increased with hydrolysis time, and analysis by reverse-phase high-performance liquid chromatography (RP HPLC) and mass spectrometry, revealed a virtually unchanged peptide profile. These results suggested that those proteases were highly specific, as only certain peptide bonds were cleaved. The hydrolysate of 180�min displayed the highest inhibition of angiotensin-converting enzyme (ACE) showing an IC50 of 1.72���0.25�mg/mL, and the analysis of the peptide fractionation in this hydrolysate by RP HPLC exhibited two peaks responsible for that activity. Fragmentation analysis through the use of iterated matrix-assisted–laser-desorption-ionization–time-of-flight mass spectrometry (MALDI-TOF/TOF MS/MS) with the aid of bioinformatics tools enabled us to deduce two peptide sequences—one, YQEPVLGPVRGPFPIIV, having been previously reported as an ACE-inhibitor; the other, RFFVAPFPE, as yet undescribed. The presence of bioactive peptides in these casein hydrolysates argues for their potential use in the development of functional foods.-
dc.descriptionFil: Corrons, María Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina-
dc.descriptionFil: Liggieri, Constanza Silvina. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina-
dc.descriptionFil: Trejo, Sebastian Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina-
dc.descriptionFil: Bruno, Mariela Anahí. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherElsevier Science-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1016/j.foodres.2017.01.003-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0963996917300042-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.source.urihttp://hdl.handle.net/11336/49568-
dc.subjectACE-INHIBITORY PEPTIDE-
dc.subjectHYDROLYSATE-
dc.subjectMACLURA POMIFERA-
dc.subjectPLANT PEPTIDASE-
dc.subjectBiotecnología Industrial-
dc.subjectBiotecnología Industrial-
dc.subjectINGENIERÍAS Y TECNOLOGÍAS-
dc.titleACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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