The Korean Journal of Mycology (한국균학회지)

The Korean Society of Mycology (한국균학회)
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Screening New Antihypertensive Angiotensin I-Converting Enzyme Inhibitor -Producing Yeast and Optimization of Production Condition

항고혈압성 안지오텐신 전환효소 저해제를 생산하는 새로운 효모의 선별 및 저해물질 최적 생산조건

  • Kang, Min-Gu (Department of Life Science and Genetic Engineering, Paichai University) ;
  • Kim, Ha-Kun (Department of Life Science and Genetic Engineering, Paichai University) ;
  • Yi, Sung-Hun (Korea Food Research Institute) ;
  • Lim, Sung-Il (Korea Food Research Institute) ;
  • Lee, Jong-Soo (Department of Life Science and Genetic Engineering, Paichai University)
  • Received : 2011.11.08
  • Accepted : 2011.11.14
  • Published : 2011.12.01
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Abstract

Forty eight strains of yeast were cultured in potato dextorse(PD) broth at $30^{\circ}C$ for 24 hr and centrifuged with 12,000 rpm for 20 min. After concentrated the cultures, antihypertensive angiotensin I-converting enzyme(ACE) inhibitory activities of its concentrates were investigated. Among them, the concentrates from Saccharomyces cerevisiae Y183-3 showed the highest ACE inhibitory activity of 71.8%. The ACE inhibitor from Saccharomyces cerevisiae Y183-3 was maximally produced when Saccharomyces cerevisiae Y183-3 cultured in PD broth at $30^{\circ}C$ for 36 hr.

항고혈압 효능이 우수하며 부작용이 없는 새로운 고혈압 예방 소재를 개발하고자 한국 식품연구원에서 분리, 동정한 48종의 효모들의 PD broth 배양 농축물들을 대상으로 angiotensin 전환효소(ACE) 저해활성을 조사하여 활성이 우수한 효모들을 선정한 다음 ACE 저해물질의 생산 최적 조건을 검토하였다. ACE 저해활성은 Saccharomyces cerevisiae Y183-3 균주의 PD broth 배양 농축물이 71.8%의 가장 높은 ACE 저해활성을 보여 최종 우수 균주로 선발하였다. 그리고 이 Y183-3 효모를 $30^{\circ}C$에서 36시간 PD broth에 배양했을 때 ACE 저해물질이 가장 많이 생산되었다.

Keywords

References

  1. 이대형, 김재호, 정종천, 공원식, 유영복, 박정식, 유창현, 이종수. 2003. 각종 버섯류로부터 안지오텐신 전환효소 저해제의 탐색. 한국균학회지. 31:148-154 https://doi.org/10.4489/KJM.2003.31.3.148
  2. 김재호, 이대형, 최신양, 이종수. 2002. 전통민속주의 생리기능성 탐색. 한국식품과학회지. 34:118-122.
  3. Cushman D. W. and Cheung H.S. 1971. Spectrophotometic assay and properties of angiotensin-converting enzyme of rabbit lung. Biochem. Pharmacol. 20:1637-1648 https://doi.org/10.1016/0006-2952(71)90292-9
  4. Ganong, W. F. 1997. Review od medical physiology. Appleton and Lange (New jersey, USA) pp. 425-460
  5. Jang, J. H., Jeong, S. C., Kim, J. H., Lee, Y. H. Ju, Y. C. and Lee, J. S. 2011. Characterization of new antihypertensive angiotensin I-converting enzyme inhibitory peptide from Pleurotus cornucopiae. Food Chemistry 127:412-418 https://doi.org/10.1016/j.foodchem.2011.01.010
  6. Jeong, S. C., Kim, J. H., Kim, N. M. and Lee, J. S. 2005. Production of antihypertensive angiotensin I-converting enzyme inhibitor from Malassezia pachydermatis G-14. Myicobiol. 33:142-146. https://doi.org/10.4489/MYCO.2005.33.3.142
  7. Koo, K. C., Lee, D. H., Kim, J. H., Yu, H. E., Park, J. S. and Lee, J. S. 2006. Production and characterization of antihypertensive angiotensin I-converting enzyme inhibitor from Pholiota adiposa. J. Microbiol. Biotechnol. 16:757-763.
  8. Kim, J. H., Lee, D. H., Jeong, S. C., Chung, K. S. and Lee, J. S. 2004. Characterization of antihypertensive angiotensin I-convertong enzyme inhibitor from Saccharomyces cerevisiae. J. Microbiol. Biotechnol. 14:1318-1323.
  9. Lee, D. H., Lee D. H. and Lee, J. S. 2007. Characterization of new antidementia ${\beta}-secretase$ inhibitory peptide from Saccharomyces cerevisiae. Enzyme and Microbiol Technol. 42:83-88. https://doi.org/10.1016/j.enzmictec.2007.08.003
  10. Lee, D. H., Kim, J. H., Park, J. S., Choi, Y. J. and Lee, J. S. 2004. Isolation and characterization of a novel angiotensin I-converting enzyme inhibitory peptide derived from the edible mushroom Tricholoma giganteum. Peptides 25:621-627. https://doi.org/10.1016/j.peptides.2004.01.015
  11. Maruyama, S., Miyoshi, S. and Tanaka, H. 1989. Angiotensin Iconverting enzyme inhibitor derived from Ficus carica. Agric. Biol. Chem. 53:2763-2769. https://doi.org/10.1271/bbb1961.53.2763
  12. Rhyu, M. R., Nam, Y. I. and Lee, H. Y. 1996. Screening of angiotensin I-converting enzyme inhibitors in cereals and legumes. Food & Biotechnol. 5:334-337
  13. Saito Y., Wanezaki, K., Kawato, A. and Imayasu, S. 1994. Structure and activity of angiotensin I-converting enzyme inhibitory peptides from sake and sake lees. Biosci. Biotech. Biochem. 58:1767-1771. https://doi.org/10.1271/bbb.58.1767
  14. Satio, Y., Nakamura, K., Kawato, A. and Imayasu, S. 1992. Angiotensin I-converting enzyme inhibitors in sake and its by products. Nippon Nogeikagakukaishi 66:1081-1087. https://doi.org/10.1271/nogeikagaku1924.66.1081
  15. Soffer, R. L., 1976. Angiotensin I-converting enzyme and the regulation of vasoactive peptides. Annu. Rev. Biochem. 45:73-94. https://doi.org/10.1146/annurev.bi.45.070176.000445

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