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Characterization of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor from Saccharomyces cerevisiae  

KIM, JAE-HO (Bae Sang Myun Brewery Co., Ltd.)
LEE, DAE-HYOUNG (Department of Genetic Engineering and Bio-Medical Resource Research Center, Paichai University)
JEONG, SEOUNG-CHAN (Department of Genetic Engineering and Bio-Medical Resource Research Center, Paichai University)
CHUNG, KUN-SUB (Department of Biological Resources and Technology, Yonsei University)
LEE, JONG-SOO (Department of Genetic Engineering and Bio-Medical Resource Research Center, Paichai University)
Publication Information
Journal of Microbiology and Biotechnology / v.14, no.6, 2004 , pp. 1318-1323 More about this Journal
Abstract
This study describes the purification and characterization of a novel antihypertensive angiotensin 1­converting enzyme (ACE) inhibitory peptide from Saccharomyces cerevisiae. Maximal production of the ACE inhibitor from Saccharomyces cerevisiae was obtained from 24 h of cultivation at $30^{\circ}C$ 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 $IC_{50}$ 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.
Keywords
Antihypertension; Saccharomyces cerevisiae; angiotensin I-converting enzyme inhibitor;
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