Latent production of angiotensin I-converting enzyme inhibitors from buckwheat protein

Chun Hui Li, Toshiro Matsui, Kiyoshi Matsumoto, Rikio Yamasaki, Terukazu Kawasaki

Research output: Contribution to journalArticlepeer-review

87 Citations (Scopus)

Abstract

The latent production of angiotensin I-converting enzyme (ACE) inhibitors from tartary buckwheat (BW) was investigated, and the peptides responsible for ACE inhibition characterized. Intact buckwheat was found to exhibit ACE inhibitory activity having an IC50 value of 3.0 mg/ml. The activity of the protein fraction (IC50: 0.36 mg protein/ml) was not enhanced by pepsin treatment. Pepsin, followed by chymotrypsin and trypsin hydrolysis, resulted in a significant increase in the ACE inhibitory activity (IC50: 0.14 mg protein/ml). The rutin contained in the buckwheat did not exhibit any ACE inhibition. A single oral administration of BW digest lowered the systolic blood pressure of a spontaneously hypertensive rat. Thus, BW proteins offer a potential resource for producing ACE inhibitory peptides during the digestion process. From the di-/tri-peptide fraction (DTPF) of the BW digest, inhibitory peptides were identified. The magnitude (%) of the total ACE inhibitory contribution of each identified peptide, relative to the overall inhibition of the DTPF, was about 41%.

Original languageEnglish
Pages (from-to)267-274
Number of pages8
JournalJournal of Peptide Science
Volume8
Issue number6
DOIs
Publication statusPublished - Jun 27 2002

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

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