title: Novel angiotensin I-converting enzyme inhibitory peptides isolated from Alcalase hydrolysate of mung bean protein.
abstract: 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 microM, 82.4 microM and 13.4 microM, respectively.
authors: College of Animal Science and Technology, Jiangxi Agricultural University, Nanchang, Jiangxi 330045, P.R. China. liguanh@163.com
authors: Guan-Hong
authors: GH
authors: Li
authors: Ju-Zhen
authors: JZ
authors: Wan
authors: Guo-Wei
authors: GW
authors: Le
authors: Yong-Hui
authors: YH
authors: Shi