Biotechnology and Bioprocess Engineering:BBE

  • 제9권5호
  • /
  • Pages.400-404
  • /
  • 2004
  • /
  • 1226-8372(pISSN)
  • /
  • 1976-3816(eISSN)
한국생물공학회 (The Korean Society for Biotechnology and Bioengineering)
권호 표지

The Relationshin between ACE Inhibitory Activity and Degradations of Sulfur Containing Materials in Dolsan Leaf Mustard Juice

  • Yoo Eun-Jeong (Department of Biotechnology, Yosu National University) ;
  • Choi Myeong-Rak (Department of Biotechnology, Yosu National University) ;
  • Lim Hyun-Soo (Department of Biotechnology, Yosu National University)
  • 발행 : 2004.10.01
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

This Study was tarried out to investigate the relationship ACE inhibitory activity and degradations of sulfur containing materials in Dolsan leaf mustard juice (DLMJ). The changes of sulfur containing materials which were treated with autolysis, myrosinase, ascorbate and papain were studied, as well as the changes of ACE inhibitory activity in DLMJ. At $37^{\circ}C$, sulfur contain-ing materials by autolysis decreased most rapidly from $0.43\%$ to $0.13\%$ in the second day. Conversely. ACE inhibitory activity increased most from $66\%$ to $87\%$. in the second day at $37^{\circ}C$. As myrosinase concentrations increased more, sulfur containing materials in DLMJ decreased more. The ACE inhibitory activities at 0, 0.5, 1, 2, and 4 Units of myrosinase for 240 min later were 70, 74, 75, 82, and $85\%$, respectively. At 1 mM ascorbate. concentrations of Sulfur containing materials in DLMJ decreased more significantly on the second day than on the other days. At 1 mM ascorbate for 6 days, ACE Inhibitory activity reached a maximum of about $92\%$. And, an increase of papain concentration was noted in accordance with a decreased sulfur containing materials. The maximum rate of AEC inhibitory activity at control, 3, 6, and 12 Units of papains treatments was shown as 70, 70, 75, and $78\%$ at 60 min, respectively. These results suggested that the degradation of sulfur containing materials led to the increase of ACE inhibitory activity. Consequently, it was suggested that ACE inhibiting was significantly related to the degradatives of sulfur containing materials.

키워드

참고문헌

  1. Cheigh, H. S. and K. Y. Park (1994) Biochemical, microbiological and nutritional aspects of Kimchi (Korea fermented vegetable products). Crit. Rev. Food Sci. Nutr. 34: 175-177 https://doi.org/10.1080/10408399409527656
  2. Cho, Y. S. and S. K. Park (1990) Studies on the chemical components of Korean Brassica Juncea Cosson. Sunchon Natl. Univ. Bull. 9: 169-172
  3. Eilert. U., B. Wolters, and A. Nahrstedt (1981) The antibiotic principle of seeds of Moringa oleifera and Moringa stenopetala. Planta Med. 42: 55-61 https://doi.org/10.1055/s-2007-971546
  4. Louda, S. and S. Mole (1991) Glucosinolates. pp.123-164. In: G. A. Rosenthal and M. R. Berenbaum (eds.). Chemistry and Ecology in Herbivorous: Their Interactions with Secondary Plant Metabolites. Kluwer Academic Publisher, London, UK
  5. Cole, R. A. (1976) Isothiocyanates, nitriles, and thiocyanates as products of autolysis of glucosinolates in cruciferae. Phytochemistry 15: 759- 762 https://doi.org/10.1016/S0031-9422(00)94437-6
  6. Troyer, J. K., K S. Ketherine, and W. F. Jed (2001) Analysis of glucosinolates from broccoli and other cruciferous vegetables by hydrophilic interaction liquid chromatography. J. Chromatogr. A. 31: 1-6 https://doi.org/10.1016/S0021-9673(01)86018-0
  7. Saurabh C., S. Farkya, A. K. Srivastava, and V. S. Bisaria (2002) Bioprocess considerations for production of secondary metabolites by plant cell suspension cultures. Biosample technol. Bioprocess Eng. 7: 138-149 https://doi.org/10.1007/BF02932911
  8. Larsen, P. O. (1981) Glucosinolates in secondary plant products. pp. 35-37. In: P. K. Stumpf and E. E. Conn (eds.). Biochemistry of Plants. Vol. 7, Academic Press, New York, USA
  9. Ramachandria, M., J. Bhat, and P. K. A. Muniswaran (2002) Prediction of continuous reactors performance based on batch reactor deactivation kinetics data of immobilized lipase. Biotechnol Bioprocess Eng. 7: 225-230 https://doi.org/10.1007/BF02932975
  10. Atle, M. B. and T. R. John (1996) The myrosinaseglucosinolate system, its organisation and biochemistry. Physiol. Plant 97: 194-208 https://doi.org/10.1111/j.1399-3054.1996.tb00497.x
  11. Tsuruo, I., M. Yosida, and T. Hata (1967) Studies on the myrosinase in mustard seed.: Part I. the chromatographic behaviors of the myrosinase and some of its characteristics Agric. BioI. Chem. 31: 27-32
  12. Ohtsuru, M. and T. Hata (1979) The interaction of Lascorbic acid with the active center of myrosinase. Biochim Biophys. Acta. 567: 384-391 https://doi.org/10.1016/0005-2744(79)90124-4
  13. Lim, H. S., E. J. Yoo, and M. R. Choi (2000) Changes of physiological activity of mustard leaf during its fermentation period. J. Microbiol. Biotechnol. 10: 43-47
  14. Choi, Y Y., E. J. Yoo, H. S. Lim, D. S. Kang, N. Nishizawa, and M. R. Choi (2001) The relationship between physiological activity and cell number in Dolsan leaf mustard Kimchi. J. Food Sci. Nutr.: 117-121
  15. Curtiss, C., J. N. Chon, T. Vrobel, and J. A. Franciosa (1978) Role of the renin-angiotensin system in the systemic vasocontraction of chronic congestive heart failure. Circulation 58: 763-765 https://doi.org/10.1161/01.CIR.58.5.763
  16. Erdos, E. G. and R. A. Skidgel (1987) The angiotensin-I converting enzyme. Lab Invest. 56: 345-349
  17. Erdos, E. G. (1990) Angiotensin- I converting enzyme and the changes in our concepts through the years. Hypertension 16: 363-365 https://doi.org/10.1161/01.HYP.16.4.363
  18. Atkinson, A. B. and J. I. S. Robertson (1980) Benefits and risks in severe hypertension. Lancet 2: 105-107
  19. Yokoyama, K., H. Chiba, and M. Yoshikawa (1992) Peptide inhibitors for angiotensin-I converting enzyme from thermolysin digest of dried bonoto. Biosci. Biotechol. Biochem. 56: 1541-1543 https://doi.org/10.1271/bbb.56.1541
  20. Matsui, T. H. Matsufuji, E. Seki, K Osajima, M. Nakashima, and Y. Osajima (1993) Inhibition of angiotensin-I converting enzyme by Bacillus licheniformis alkaline protease hydrolysates derived from sardine muscle. Biosci. Biotechnol. Biochem. 57: 922-924 https://doi.org/10.1271/bbb.57.922
  21. Kohama, Y., S. Matsumoto, H. Oka, T. Teramoto, M. Okabe, and T. Mimura. (1988) Isolation and ACE-inhibitor from tuna muscle. Biochem. Biophys. Res. Commun. 155: 332-334 https://doi.org/10.1016/S0006-291X(88)81089-1
  22. Arai, S. (1996) Studies on functional foods in Japan-state of the art. Biosci. Biotechnol. Biochem. 60: 9-11 https://doi.org/10.1271/bbb.60.9
  23. Shin, C. S., K. I. Seo, K. S. Kang, C. W. Ahn, Y. G. Kim, and K. H. Shim (1996) Purification and enzymatic of myrosinase in Korean mustard seed (Brassica Juncea). J. Kor. Soc. Food Sci. Nutr. 25: 687-694
  24. Yuk, J. S., Y. H. Lim, and H. Y. Cho (2000) Purification and characterization of angiotensin I-converting enzyme inhibitors from Sinapis alba L. J Food Sci. Nutr. 5: 75-80