Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/65979
Type: Artigo de periódico
Title: Evaluation of the hypotensive potential of bovine and porcine collagen hydrolysates
Author: Faria, M
da Costa, EL
Gontijo, JAR
Netto, FM
Abstract: Angiotensin-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.
Subject: angiotensin-converting enzyme
antihypertensive activity
arterial blood pressure
capillary electrophoresis
in vitro digestion
spontaneously hypertensive rat
systolic blood pressure
Country: EUA
Editor: Mary Ann Liebert Inc
Rights: embargo
Identifier DOI: 10.1089/jmf.2007.0573
Date Issue: 2008
Appears in Collections:Unicamp - Artigos e Outros Documentos

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