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

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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
Issue number6
Publication statusPublished - Dec 2002


ASJC Scopus subject areas

  • Food Science
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

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