Physiological Functionality of Various Extracts from Danmemil and Legumes

단메밀과 콩 추출물들의 생리 기능성

  • Published : 2003.12.01

Abstract

Physiological functionalities of various extracts from Danmemil and legumes were determined and its optimal extraction conditions were also investigated. Angiotensin I-converting enzyme (ACE) inhibitory activity and tyrosinase inhibitory activity of Danmemil were higher in water extracts (53%, 58%) than those of ethanol extracts. However, its electron-donating ability was the highest in ethanol extracts (72%). ACE inhibitory activity and electron-donating ability of Black bean No. 1 and Taekwangkong(one of bean) were higher in water extracts than those of ethanol extracts, whereas SOD-like activity was the highest in ethanol extracts. ACE inhibitor and tyrosinase inhibitor of Danmemil were maximally extracted when it were treated with 20 times of distilled water at 35$^{\circ}C$ for 24 h and 36 h, respectively. Its electron donating compound was maximally extracted by treatment of 50$^{\circ}C$ for 18 h. ACE inhibitor of Black bean No. 1 was extracted maximally when it was treated with distilled water (1 :20) at 20$^{\circ}C$ for 24 h, whereas the other functional compounds were maximally extracted at 20$^{\circ}C$ for 18 h.

단메밀과 콩 등으로부터 생리기능성 물질을 추출하여 건강식품을 개발하고자 먼저 물과 에탄올을 사용하여 extracts를 추출한 후 엔지오텐신 전환효소 (ACE) 저해활성과 항산화활성 및 SOD-유사활성 등을 측정하였다. 단메밀의 ACE저해 활성과 tyrosinase 저해 활성은 물 추출물에서 각각 53%와 58%로 에탄을 추출물보다 더 높았고 전자공여능은 에탄을 추출물에서 제일 높은 72%를 보였다. 검정종 1호와 태광콩의 ACE 저해 활성과 전자공여능은 물 추출물에서 높았으나 SOD-유사활성은 에탄을 추출물에서 가장 높았다. 단메밀 중의 ACE 저해물질과 tyrosinase 저해 물질들은 20배의 증류수로 35$^{\circ}C$에서 각각 24시간, 36시간 처리했을 때 가장 많이 추출되었고 전자공여능을 나타내는 항산화물질은 5$0^{\circ}C$에서 18시간 처리했을 때 가장 많이 추출되었다. 또한 검정콩 1호의 ACE 저해물질은 2$0^{\circ}C$, 24시간에서 가장 많이 추출되었으나 그 밖의 기능성 물질들은 2$0^{\circ}C$에서 18시간 추출하였을 때 가장 많이 추출되었다.

Keywords

References

  1. Korean Soc. Food Sci. Technol. : Symposium of health-aid food, Abstract(1997)
  2. Folkow, B., Johansson, B. and Mellander, S. : The comparative effect of angiotension and nonadrenaline on consecutive vascular section. Acta. Physiol. Scand., 53, 99-104(1961) https://doi.org/10.1111/j.1748-1716.1961.tb02267.x
  3. Ferreira, S.H., Bartelt, D.C. and Greene, L.J. : Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom. Biochemistry, 9, 2583-2592(1970) https://doi.org/10.1021/bi00815a005
  4. Cushman, D.W., Cheung, H.S., Saba, E.F. and Ondetti, M. A. : Design of potent competitive inhibitors of angiotensinconverting enzyme. Carboxylalkanoyl and mercaptoalkanoyl amino acids. Biochemistry, 16, 5484-5495(1977) https://doi.org/10.1021/bi00644a014
  5. Oshima, G., Shimabukuro, H. and Nagasawa, K. : Peptide inhibitors of angiotensin I -converting enzyme II digests of gelatin by bacterial collagenase. Biochim. Biophys. Acta., 566, 128-137(1979) https://doi.org/10.1016/0005-2744(79)90255-9
  6. Maruyama, S. and Suzuki, H. : A peptide inhibitor of angiotensin I converting enzyme in the tryptic hydrolysate of casein. Agric. BioI. Chem., 46, 1393-1394(1982) https://doi.org/10.1271/bbb1961.46.1393
  7. Mullaly, M, Meisle, H. and FitzGerald, R. J. : Synthetic peptides corresponding to a-lactalbumin and p-Iactoglobulin sequences with angiotensin- I -converting enzyme inhibitory activity. BioI. Chem. Hoppe-Seyler, 377, 259 - 260(1996) https://doi.org/10.1515/bchm3.1996.377.4.259
  8. Rhyu, M.R, Nam, Y.J. and Lee, H.Y. : Screening of angiotensin I - converting enzyme inhibitors in cereals and legumes. Foods and Biotechnology, 4, 334-337(1996)
  9. Marks, D., Marks, A. and Smith, C. : Basic medical biochemistry, Williams and Wikins, Baltimore., p.107-110(1996)
  10. Kim, S.H., Choi, N.S., Lee, W.Y., Lee, J.W. and Kim, D.H.: Isolation of Bacillus strains secreting fibrinolytic enzymes from Doen-jang, Kor. J. Microbiol., 34, 87 -90(1998)
  11. Choi, N.S., Seo, S.Y. and Kim, S.H. : Screening of mushrooms having fibrinolytic activity, Kor. J. Food Sci. Technol., 31. 553 - 557(1999)
  12. Kim, Y.T. : Characteristics of fibrinolytic enzyme produced by Bacillus sp. isolated from Chungkookjang. Sejong Univ. Ph. D. Thesis(1995)
  13. Kim, W. K, Choi, K. H., Kim, Y. T., Park, H. H., Lee, Y. S., Oh, H. I., Kim, I. B. and Lee, S. Y. : Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strains CK 11-4 screened from chungkookjang, Appl. Environ. Microbiol., 62, 2482-2488(1996)
  14. Kim, S.M, Kim, E.J., Jo, Y.S. and Sung, S.K. : Antioxidant activities of pine leaves extracts from different extraction methods, KoreanJ Food Sci. Technol., 31, 527-532(1999)
  15. Lee, G.Y., Kim, J.H., Sohn, J.R and Lee, J.S. : Detection and extraction condition of physiological functional compounds from bran of Heugjinju byeo rice. Kor. J. Postharvest Sci. Technol., 8, 296-301(2001)
  16. Kang, W.H., Park, Y.G., Oh, S.Y. and Moon, K.D. : Functionalities of extracts from pine leaves and ssug. Korean J Food Sci. Technol., 27, 978-984(1996)
  17. Kwon, T.B. : Development of functional foods by using mernil. Report of research project of Hanlim junior college(93-L-0019) on Ministry of Science and Technology(1993)
  18. Sohn, H.S. : Current research aspect of soybean and its products. 2003 Meeting of the Federation of Korean Nutritional Societies ; Symposium of development and research aspects of health functional food. Abstracts. 28-38(2003)
  19. Kim, H.J., Kim, J.H., Shon, J.R and Lee, J.S. : Antihypertensive angiotensin I -converting enzyme inhibitory activity of various extracts from some rice brans. J. Nationol Sci. of Paichai Univ. 13, 251-259(2003)
  20. Cushman, D.W. and Cheung, H.S. : Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochemical, Pharmacology, 20, 1637-1648(1971) https://doi.org/10.1016/0006-2952(71)90292-9
  21. Fayek, K.I. and EI-Sayed, S.T. : Purification and properties of fibrinolytic enzyme from Bacillus subtilis, Zeit. fur Allgem. Mikrobiol, 20, 375 - 382(1980) https://doi.org/10.1002/jobm.3630200603
  22. Marklund, S. and Marklund, G. : Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase, Eur. J. Biochem., 47, 469-474(1974)
  23. Blois, MS. : Antioxidant determination by use of stable free radical, Nature, 191, 1199-1203(1985) https://doi.org/10.1038/1911199a0
  24. Lee, J.S., Lee, S.H., Kwon, S.J., Ahn, C. and Yoo, J.Y. : Enzyme activities and physiological functionality of yeasts from traditional meju. Kor. J. Food Sci. Technol., 25, 448452(1997)
  25. Sung, C.K. and Cho, S.H. : Studies on the purification and characteristics of tyrosinase from Diospyros kaki Thunb. Kor. Biochem. J., 25, 79-87(1992)