Characterization of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor from Saccharomyces cerevisiae
Year: 2004
Type: article
Abstract: This study describes the purification and characterization of a novel antihypertensive angiotensin I-converting enzyme (ACE) inhibitory peptide from Saccharomyces cerevisiae. Maximal production of the ACE inhibitor from Saccharomyces cerevisiae was obtained from 24 h of cultivation at 30째C and its ACE inhibitory activity was increased by about 1.5 times after treatment of the cell-free extract with pepsin. After the purification of ACE inhibitory peptides with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an IC50 of 0.07 mg and 3.5% yield was obtained. The purified peptide was a novel decapeptide, showing very low similarity to other ACE inhibitory peptide sequences, and its amino acid sequence was Tyr-Asp-Gly-Gly-Val-Phe-Arg-Val-Tyr-Thr. The purified inhibitor competitively inhibited ACE and also showed a clear antihypertensive effect in spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg body weight
Authors: Jaeho Kim, Dae‐Hyoung Lee, Seoung-Chan Jeong, Kun-Sub Chung, Jong‐Soo Lee
Language: English
Subfield: Food Science
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2390435104