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KMID : 0545120040140061318
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Journal of Microbiology and Biotechnology
2004 Volume.14 No. 6 p.1318 ~ p.1323
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Characterization of Antihypertensive Angiotensin 1-Converting Enzyme Inhibitor from Saccharomyces cerevisiae
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Kim JH
Lee DH/Jeong SC/Chung KS/Lee JS
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Abstract
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This study describes the purification and characterization of a novel antihypertensive angiotensin Iconverting enzyme (ACE) inhibitory peptide from Saccharomyces cerevisiae. Maximal production of the ACE inhibitor from Saccharomyces cerevisiae was obtained from 24 h of cultivation at 30oC 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 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 clear antihypertensive effect in spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg body weight.
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