ACE-inhibitory peptides from bovine caseins released with peptidases from <i>Maclura pomifera</i> latex

In 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 (SDSPAGE) indicated that the caseins were considerably degraded after a 10-min reaction. The d...

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Detalles Bibliográficos
Autores principales:	Corrons, María Alicia, Liggieri, Constanza Silvina, Trejo, Sebastián Alejandro, Bruno, Mariela Anahí
Formato:	Articulo
Lenguaje:	Inglés
Publicado:	2017
Materias:	Biología Maclura pomifera Plant peptidase Hydrolysate ACE-inhibitory peptide
Acceso en línea:	http://sedici.unlp.edu.ar/handle/10915/117257
Aporte de:	SEDICI (UNLP) de Universidad Nacional de La Plata

id	I19-R120-10915-117257
record_format	dspace
institution	Universidad Nacional de La Plata
institution_str	I-19
repository_str	R-120
collection	SEDICI (UNLP)
language	Inglés
topic	Biología Maclura pomifera Plant peptidase Hydrolysate ACE-inhibitory peptide
spellingShingle	Biología Maclura pomifera Plant peptidase Hydrolysate ACE-inhibitory peptide Corrons, María Alicia Liggieri, Constanza Silvina Trejo, Sebastián Alejandro Bruno, Mariela Anahí ACE-inhibitory peptides from bovine caseins released with peptidases from <i>Maclura pomifera</i> latex
topic_facet	Biología Maclura pomifera Plant peptidase Hydrolysate ACE-inhibitory peptide
description	In 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 (SDSPAGE) 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 highperformance 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.
format	Articulo Articulo
author	Corrons, María Alicia Liggieri, Constanza Silvina Trejo, Sebastián Alejandro Bruno, Mariela Anahí
author_facet	Corrons, María Alicia Liggieri, Constanza Silvina Trejo, Sebastián Alejandro Bruno, Mariela Anahí
author_sort	Corrons, María Alicia
title	ACE-inhibitory peptides from bovine caseins released with peptidases from <i>Maclura pomifera</i> latex
title_short	ACE-inhibitory peptides from bovine caseins released with peptidases from <i>Maclura pomifera</i> latex
title_full	ACE-inhibitory peptides from bovine caseins released with peptidases from <i>Maclura pomifera</i> latex
title_fullStr	ACE-inhibitory peptides from bovine caseins released with peptidases from <i>Maclura pomifera</i> latex
title_full_unstemmed	ACE-inhibitory peptides from bovine caseins released with peptidases from <i>Maclura pomifera</i> latex
title_sort	ace-inhibitory peptides from bovine caseins released with peptidases from <i>maclura pomifera</i> latex
publishDate	2017
url	http://sedici.unlp.edu.ar/handle/10915/117257
work_keys_str_mv	AT corronsmariaalicia aceinhibitorypeptidesfrombovinecaseinsreleasedwithpeptidasesfromimaclurapomiferailatex AT liggiericonstanzasilvina aceinhibitorypeptidesfrombovinecaseinsreleasedwithpeptidasesfromimaclurapomiferailatex AT trejosebastianalejandro aceinhibitorypeptidesfrombovinecaseinsreleasedwithpeptidasesfromimaclurapomiferailatex AT brunomarielaanahi aceinhibitorypeptidesfrombovinecaseinsreleasedwithpeptidasesfromimaclurapomiferailatex
bdutipo_str	Repositorios
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ACE-inhibitory peptides from bovine caseins released with peptidases from <i>Maclura pomifera</i> latex

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