Premium
Novel angiotensin I‐converting enzyme inhibitory peptides isolated from Alcalase hydrolysate of mung bean protein
Author(s) -
Li GuanHong,
Wan JuZhen,
Le GuoWei,
Shi YongHui
Publication year - 2006
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.758
Subject(s) - hydrolysate , chemistry , chromatography , sephadex , peptide , enzyme , ic50 , hydrolysis , mung bean , biochemistry , in vitro , food science
Mung bean protein isolates were hydrolyzed for 2 h by Alcalase. The generated hydrolysate showed angiotensin I‐converting enzyme (ACE) inhibitory activity with the IC 50 value of 0.64 mg protein/ml. Three kinds of novel ACE inhibitory peptides were isolated from the hydrolysate by Sephadex G‐15 and reverse‐phase high performance liquid chromatography (RP‐HPLC). These peptides were identified by amino acid composition analysis and matrix assisted‐laser desorption/ionization time‐of‐flight tandem mass spectrometry (MALDI‐TOF MS/MS), as Lys‐Asp‐Tyr‐Arg‐Leu, Val‐Thr‐Pro‐Ala‐Leu‐Arg and Lys‐Leu‐Pro‐Ala‐Gly‐Thr‐Leu‐Phe with the IC 50 values of 26.5 µ M , 82.4 µ M and 13.4 µ M , respectively. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.