Evaluation of the hypotensive potential of bovine and porcine collagen hydrolysates

dc.creatorFaria, M
dc.creatorda Costa, EL
dc.creatorGontijo, JAR
dc.creatorNetto, FM
dc.date2008
dc.dateSEP
dc.date2014-11-17T13:08:44Z
dc.date2015-11-26T17:38:08Z
dc.date2014-11-17T13:08:44Z
dc.date2015-11-26T17:38:08Z
dc.date.accessioned2018-03-29T00:19:44Z
dc.date.available2018-03-29T00:19:44Z
dc.identifierJournal Of Medicinal Food. Mary Ann Liebert Inc, v. 11, n. 3, n. 560, n. 567, 2008.
dc.identifier1096-620X
dc.identifierWOS:000259677200024
dc.identifier10.1089/jmf.2007.0573
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/65979
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/65979
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/65979
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1286121
dc.descriptionAngiotensin-converting enzyme (ACE) inhibitory activity and antihypertensive activity of bovine and porcine collagen hydrolysates in spontaneously hypertensive rats (SHR) were investigated. The hydrolyzed collagens were subjected to ultrafiltration using membranes with cutoffs of 30-50 kDa (permeate PI), 5-8 kDa (permeate P2), or 1-2 kDa (permeate P3) in order to obtain products with a narrower range of molecular size. The hydrolyzed bovine and porcine collagens and their permeates showed low ACE inhibitory activity (50% inhibitory concentration [IC50] = 5.42-15.58 mg of protein/mL). However, after in vitro gastrointestinal digestion, a significant increase in the ACE inhibitory potency of the hydrolyzed collagens was observed (IC50 = 0.97-4.02 ing of protein/mL). Permeates had a higher ACE inhibitory activity and hypotensive activity than non-ultrafiltered hydrolysates. The P I permeate of bovine and porcine collagen and the P3 fraction of the porcine collagen hydrolysate exhibited the best anti hypertensive activity in vivo, promoting a maximum reduction in blood pressure of 22 mm Hg, 21.33 mm Hg, and 21.33 mm Hg, respectively, while lisinopril promoted a maximum reduction of 51.00 mm Hg. These results suggest that the commercial collagen hydrolysates of bovine and porcine origin may be a potential source of bioactive peptides.
dc.descriptiono TEXTO COMPLETO DESTE ARTIGO, ESTARÁ DISPONÍVEL À PARTIR DE AGOSTO DE 2015.
dc.description11
dc.description3
dc.description560
dc.description567
dc.languageen
dc.publisherMary Ann Liebert Inc
dc.publisherNew Rochelle
dc.publisherEUA
dc.relationJournal Of Medicinal Food
dc.relationJ. Med. Food
dc.rightsembargo
dc.sourceWeb of Science
dc.subjectangiotensin-converting enzyme
dc.subjectantihypertensive activity
dc.subjectarterial blood pressure
dc.subjectcapillary electrophoresis
dc.subjectin vitro digestion
dc.subjectspontaneously hypertensive rat
dc.subjectsystolic blood pressure
dc.subjectI-converting-enzyme
dc.subjectInhibitory Peptides
dc.subjectWhey-protein
dc.subjectStructural-analysis
dc.subjectDigestion
dc.subjectSkin
dc.titleEvaluation of the hypotensive potential of bovine and porcine collagen hydrolysates
dc.typeArtículos de revistas


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