2012 ; 22(3):
|Author||Min-Gu Kang, Jae-Ho Kim, Byung-Hak Ahn, Jong-Soo Lee|
|Affiliation||Department of Life Science and Genetic Engineering, Paichai University, Daejeon 302-735, Korea|
|Title||Characterization of New Antihypertensive Angiotensin I-Converting Enzyme Inhibitory Peptides from Korean Traditional Rice Wine|
J. Microbiol. Biotechnol.2012 ; 22(3):
|Abstract||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.|
|Keywords||Korea traditional rice wine, angiotensin I-converting enzyme inhibitory peptide, antihypertension|
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