Novel angiotensin I-converting enzyme inhibitory peptides isolated from Alcalase hydrolysate of mung bean protein. |
| |
Authors: | Guan-Hong Li Ju-Zhen Wan Guo-Wei Le Yong-Hui Shi |
| |
Institution: | College of Animal Science and Technology, Jiangxi Agricultural University, Nanchang, Jiangxi 330045, P.R. China. liguanh@163.com |
| |
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. |
| |
Keywords: | angiotensin I‐converting enzyme peptides mung bean protein antihypertensive effect spontaneously hypertensive rats Alcalase |
|
|