Purification and characterization of a novel angiotensin-I converting enzyme (ACE) inhibitory peptide derived from enzymatic hydrolysate of grass carp protein

► The first report of food-derived Val-Ala-Pro (VAP) tripeptide. ► Excellent ACE-inhibitory activity of VAP (IC50 value of 0.00534mg/mL). ► VAP is a competitive ACE inhibitor. ► VAP is stable against ACE and digestive enzymes. ► Purification of VAP from hydrolysate of grass carp protein was achieved...

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Veröffentlicht in:	Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2012-01, Vol.33 (1), p.52-58
Hauptverfasser:	Chen, Jiwang, Wang, Yimei, Zhong, Qixin, Wu, Yongning, Xia, Wenshui
Format:	Artikel
Sprache:	eng
Schlagworte:	ACE-inhibitory peptide adsorption adverse effects angiotensin I angiotensin-converting enzyme inhibitors Angiotensin-Converting Enzyme Inhibitors - isolation & purification Angiotensin-Converting Enzyme Inhibitors - pharmacology Animals Carp Carps Chromatography, High Pressure Liquid - methods chymotrypsin Chymotrypsin - metabolism Ctenopharyngodon idella Enzymes Filtration functional foods gastrointestinal system grass carp Grass carp protein hydrolysate Grasses Hydrolysates Hydrolysis hypertension Inhibition pattern Inhibitors Inhibitory Concentration 50 pepsin Pepsin A - metabolism Peptides Peptides - isolation & purification Peptides - metabolism Peptides - pharmacology protein hydrolysates Proteins Purification reversed-phase high performance liquid chromatography Stability against gastrointestinal enzymes ultrafiltration
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