期刊
PEPTIDES
卷 33, 期 1, 页码 52-58出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2011.11.006
关键词
Grass carp protein hydrolysate; ACE-inhibitory peptide; Purification; Inhibition pattern; Stability against gastrointestinal enzymes
资金
- National Advanced Science and Technology (863) Key Program [2010AA023003]
- 111 Project [B07029]
- earmarked fund for Modern Agro-industry Technology Research System [NYCYTX-49]
- Hubei Provincial Ministry of Education [C2010040]
- [PCSIRT0627]
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 0.00534 mg/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. (C) 2011 Elsevier Inc. All rights reserved.
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