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KMID : 0545120120220030339
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Journal of Microbiology and Biotechnology
2012 Volume.22 No. 3 p.339 ~ p.342
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Characterization of New Antihypertensive Angiotensin I-Converting Enzyme Inhibitory Peptides from Korean Traditional Rice Wine
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Kang Min-Gu
Kim Jae-Ho
Ahn Byung-Hak
Lee Jong-Soo
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Abstract
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This study describes the characterization of a new angiotensin I-converting enzyme (ACE) inhibitory peptide from a Korean traditional rice wine. After purification of the ACE inhibitor peptides with ultrafiltration, Sephadex G-25 column chromatography, and successively C18 and SCX solid-phase extraction, reverse-phase HPLC, and size exculsion chromatography, two types of the purified ACE inhibitors with IC50 values of 0.34 mg/ml and 1.23 mg/ml were finally obtained. The two purified ACE inhibitors (F-1 and F-2) were found to have two kinds of novel oligopeptides, showing very little similarity to other ACE inhibitory peptide sequences. The amino acid sequences of the two purified oligopeptides were found to be Gln- Phe-Tyr-Ala-Val (F-1) and Ala-Gly-Pro-Val-Leu-Leu (F-2), and their molecular masses were estimated to be 468.7 Da (F-1) and 357.7 Da (F-2), respectively. They all showed a clear antihypertensive effect on spontaneously hypertensive rats at a dosage of 500 mg/kg.
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KEYWORD
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Korea traditional rice wine, angiotensin I-converting enzyme inhibitory peptide, antihypertension
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