Angiotensin I-converting enzyme inhibitory peptides derived from wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats

Minoru Sato, Takao Hosokawa, Toshiyasu Yamaguchi, Toshiki Nakano, Koji Muramoto, Takashi Kahara, Katsura Funayama, Akio Kobayashi, Takahisa Nakano

Research output: Contribution to journalArticlepeer-review

205 Citations (Scopus)

Abstract

Seven kinds of angiotensin I-converting enzyme (ACE) inhibitory peptides were isolated from the hydrolysates of wakame (Undaria pinnatifida) by Protease S "Amano" (from Bacillus stearothermophilus) by using three-step high-performance liquid chromatography (HPLC) on a reverse-phase column. These peptides were identified by amino acid composition analysis, sequence analysis, and liquid chromatography-mass spectrometry (LC-MS), as Val-Tyr (IC50 = 35.2 μM), Ile-Tyr (6.1 μM), Ala-Trp (18.8 μM), Phe-Tyr (42.3 μM), Val-Trp (3.3 μM), Ile-Trp (1.5 μM), and Leu-Trp (23.6 μM). These peptides have resistance against gastrointestinal proteases in vitro. Each peptide was determined to have an antihypertensive effect after a single oral administration in spontaneously hypertensive rats (SHR). Among them, the blood pressure significantly decreased by Val-Tyr, Ile-Tyr, Phe-Tyr, and Ile-Trp in a dose of 1 mg/kg of body weight (BW). The present study showed that antihypertensive effect in the hydrolysates of wakame by Protease S "Amano" was attributed to these peptides.

Original languageEnglish
Pages (from-to)6245-6252
Number of pages8
JournalJournal of Agricultural and Food Chemistry
Volume50
Issue number21
DOIs
Publication statusPublished - 2002 Oct 9

Keywords

  • Angiotensin I-converting enzyme
  • Antihypertension
  • Digestive resistance
  • Identification
  • Isolation
  • LC-MS
  • Peptide
  • Spontaneously hypertensive rat
  • Undaria pinnatifida
  • Wakame

ASJC Scopus subject areas

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)

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