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Latent production of angiotensin I‐converting enzyme inhibitors from buckwheat protein
Author(s) -
Li ChunHui,
Matsui Toshiro,
Matsumoto Kiyoshi,
Yamasaki Rikio,
Kawasaki Terukazu
Publication year - 2002
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.387
Subject(s) - pepsin , chemistry , ic50 , angiotensin converting enzyme , trypsin , enzyme , peptide , ace inhibitor , biochemistry , chymotrypsin , rice protein , renin–angiotensin system , pharmacology , enzyme inhibitor , enalaprilat , inhibitory postsynaptic potential , in vitro , endocrinology , biology , blood pressure
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 IC 50 value of 3.0 mg/ml. The activity of the protein fraction (IC 50 : 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 (IC 50 : 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%. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.