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    J Pept Sci. 2006 Aug;12(8):509-14.

    Novel angiotensin I-converting enzyme inhibitory peptides isolated from Alcalase hydrolysate of mung bean protein.

    Li GH, Wan JZ, Le GW, Shi YH.

    Source

    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.

    Copyright (c) 2006 European Peptide Society and John Wiley & Sons, Ltd.

    PMID:
    16680798
    [PubMed - indexed for MEDLINE]

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