Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Characterization of New Antihypertensive Angiotensin I-Converting Enzyme Inhibitory Peptides from Korean Traditional Rice Wine

  • Kang, Min-Gu (Department of Life Science and Genetic Engineering, Paichai University) ;
  • Kim, Jae-Ho (Korea Food Research Institute) ;
  • Ahn, Byung-Hak (Korea Food Research Institute) ;
  • Lee, Jong-Soo (Department of Life Science and Genetic Engineering, Paichai University)
  • Received : 2011.09.14
  • Accepted : 2011.11.15
  • Published : 2012.03.28
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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 $C_{18}$ and SCX solid-phase extraction, reverse-phase HPLC, and size exculsion chromatography, two types of the purified ACE inhibitors with $IC_{50}$ 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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References

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