Identification of angiotensin I-converting enzyme inhibitory peptides derived from the peptic digest of soybean protein

Jiun Rong Chen, Takashi Okada, Koji Muramoto, Kunio Suetsuna, Suh Ching Yang

    Research output: Contribution to journalArticle

    59 Citations (Scopus)

    Abstract

    Peptidic fractions which inhibit angiotensin I-converting enzyme (ACE) were separated from peptic digests of soybean by ion exchange chromatography and gel filtration. Further separation of the peptidic fractions by ODS HPLC afforded active peptides, the amino acid sequences of which were identified by Edman's procedure as: Ile-Ala (inhibitory against ACE with an IC50 of 153 μM), Tyr-Leu-Ala-Gly-Asn-Gln (14 μM), Phe-Phe-Leu (37 μM), Ile-Tyr-Leu-Leu (42 μM), and Val-Met-Asp-Lys-Pro-Gln-Gly (39 μM). The antihypertensive activity of the soybean peptides was also investigated. Peptide fractions (2.0 g/kg body weight, oral administration) markedly lowered the blood pressure of spontaneously hypertensive rats (SHRs).

    Original languageEnglish
    Pages (from-to)543-554
    Number of pages12
    JournalJournal of Food Biochemistry
    Volume26
    Issue number6
    DOIs
    Publication statusPublished - 2002 Dec

    ASJC Scopus subject areas

    • Food Science
    • Biophysics
    • Pharmacology
    • Cell Biology

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