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Purification and characterization of a novel angiotensin-I converting enzyme (ACE) inhibitory peptide derived from enzymatic hydrolysate of grass carp protein
- Source :
-
Peptides . Jan2012, Vol. 33 Issue 1, p52-58. 7p. - Publication Year :
- 2012
-
Abstract
- Abstract: Peptides inhibiting angiotensin-I converting enzyme (ACE, EC. 3.4.15.1) are possible cures of hypertension. Food-derived ACE-inhibitory peptides are particularly attractive because of reduced side effects. Previously, we reported ACE-inhibitory activity of grass carp protein hydrolysates. In this work, we report steps for purifying the ACE-inhibitory peptide from the hydrolysate and its biochemical properties. Following steps of ultrafiltration, macroporous adsorption resin, and two steps of reversed phase high performance liquid chromatography (RE-HPLC), a single Val-Ala-Pro (VAP) tripeptide was identified. The tripeptide with excellent ACE-inhibitory activity (IC50 value of 0.00534mg/mL) was a competitive ACE inhibitor and stable against both ACE and gastrointestinal enzymes of pepsin and chymotrypsin. This is the first report of food-derived VAP. The identified unique biochemical properties of VAP may enable the application of grass carp protein hydrolysates as a functional food for treatments of hypertension. The developed purification conditions also allow the production of VAP for pharmaceutical applications. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 01969781
- Volume :
- 33
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Peptides
- Publication Type :
- Academic Journal
- Accession number :
- 70385893
- Full Text :
- https://doi.org/10.1016/j.peptides.2011.11.006