KSBB Journal

The Korean Society for Biotechnology and Bioengineering (한국생물공학회)
권호 표지
DOI QR코드

DOI QR Code

Effect of Temperature and pH on Trypsin Inhibitory Activity of Ethanol Extracts from Ecklonia cava

감태 에탄올 추출물의 Trypsin 저해활성에 대한 열 및 pH의 영향

  • Jeong, Hee-Ye (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Kim, Koth-Bong-Woo-Ri (Institute of Fisheries Sciences/Pukyong National University) ;
  • Jung, Seul-A (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Kim, Hyun-Jee (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Jeong, Da-Hyun (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Lee, Ga-Yeong (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Kang, Bo-Kyeong (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Bark, Si-Woo (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Kim, Tae-Wan (Department of Food Science and Biotechnology, Andong National University) ;
  • Cho, Young-Je (School of Food Science of Biotechnology, Kyungpook National University) ;
  • Ahn, Dong-Hyun (Department of Food Science and Technology/Institute of Food Science, Pukyong National University)
  • 정희예 (부경대학교 식품공학과/식품연구소) ;
  • 김꽃봉우리 (부경대학교 수산과학연구소) ;
  • 정슬아 (부경대학교 식품공학과/식품연구소) ;
  • 김현지 (부경대학교 식품공학과/식품연구소) ;
  • 정다현 (부경대학교 식품공학과/식품연구소) ;
  • 이가영 (부경대학교 식품공학과/식품연구소) ;
  • 강보경 (부경대학교 식품공학과/식품연구소) ;
  • 박시우 (부경대학교 식품공학과/식품연구소) ;
  • 김태완 (안동대학교 식품생명공학과) ;
  • 조영제 (경북대학교 식품공학부) ;
  • 안동현 (부경대학교 식품공학과/식품연구소)
  • Received : 2012.10.10
  • Accepted : 2012.12.26
  • Published : 2012.12.31
Download PDF
⟨ Previous Next ⟩

Abstract

This study was performed to investigate the inhibitory activity of ethanol extract from Ecklonia cava (EE-EC) against trypsin and the stability of this activity under various heat and pH conditions. As a results, The EE-EC showed trypsin inhibitory activity of 77, 54, and 32% at concentrations of 5, 2.5, and 1 mg/mL and was not affected by the heat treatment conditions used in this study. Whereas trypsin inhibitory activity of EE-EC was stable in the pH range of 2-8, but decreased with pH treatment of pH 10 compared with the control. Therefore, the EE-EC could be useful as a natural and functional agent.

Keywords

References

  1. Kassel, B. (1970) Naturally occurring inhibitors of proteolytic enzymes. pp. 839-906. In: G. E. Perlman, and L. Lorand (eds.). Methods in enzymology (proteolytic enzymes). Academic Press, NY, USA.
  2. Park, J. O., K. S. Kim, and K. O. Sunwoo (1995) Purification and characterization of hemagglutinating protein from rhizome of Alisma orientale. J. Korean Soc. Food Nutr. 24: 587-593.
  3. Power, J. C. and J. W. Harper (1986) Inhibitors of Serine Proteases in Proteinase Inhibitors. pp. 55-152. In: A. J. Barrett and G. Salvesen (eds.). Research Monographs in Cell and Tissue Physiology 12, Elsevier Science Ltd., Amsterdam, NL.
  4. Laskowski, M. J. and I. Kato (1980) Protein inhibitors of proteinases. Annu. Rev. Biochem. 49: 583-626.
  5. Kennedy, A. R. (1998) Chemopreventive agents: protease inhibitors. Pharmacol. Therapeut. 78: 167-209. https://doi.org/10.1016/S0163-7258(98)00010-2
  6. Oliva, M. L. V., J. C. Souza-Pinto, I. F. C. Batista, M. S. Araujo, V. F. Silveira, E. A. Auerswald, R. Mentele, C. Eckerskorn, M. U. Sampaio, and C. A. M. Sampaio (2000) Leucaena leucocephala serine proteinase inhibitor: primary structure and action on blood coagulation, kinin release and rat paw edema. Biochim. Biophys. Acta. 1477: 64-74. https://doi.org/10.1016/S0167-4838(99)00285-X
  7. Lundquist, I., I. Ihse, and B. Amesjo (1976) Carbohydrate metabolism in normal and diabetic rats following long term oral trypsin inhibitor administration. Scand. J. Gastroentero. 11: 369-375.
  8. Mikola, J. and E. M. Suolinna (1969) Purification and properties of a trypsin inhibitor from barley. Eur. J. Biochem. 9: 655-560.
  9. Birk, Y., A. Gertler, and S. Khalef (1962) A pure trypsin inhibitor from soya beans. Biochem. J. 87: 281-284.
  10. Ye, X. Y., T. B. Ng, and P. F. Rao (2001) A bowman-birk-type trypsin-chymotrypsin inhibitor from broad beans. Biochem. Bioph. Res. Co. 289: 91-96. https://doi.org/10.1006/bbrc.2001.5965
  11. Kim, S. A., J. Kim, M. K. Woo, C. S. Kwak, and M. S. Lee (2005) Antimutagenic and cytotoxic effects of ethanol extracts from five kinds of seaweeds. J. Korean Soc. Food Sci. Nutr. 34: 451-459. https://doi.org/10.3746/jkfn.2005.34.4.451
  12. Kwon, M. J. and T. J. Nam (2006) Effects of Mesangi (Capsosiphon fulvecens) power on lipid metabolism in high cholesterol fed rats. J. Korean Soc. Food Sci. Nutr. 35: 530-535. https://doi.org/10.3746/jkfn.2006.35.5.530
  13. Fenical, W. (1983) Marine Plants: A Unique and Unexplored Resource. pp. 147-153. In Plants: The Potentials for Extracting Protein, Medicines, and Other Useful Chemicals (Workshop Proceedings). DIANE publishing, Washington, DC, USA.
  14. Lee, S. J., E. J. Song, S. Y. Lee, K. B. W. R. Kim, S. J. Kim, S. Y. Yoon, C. J. Lee, and D. H. Ahn (2009) Antioxidant activity of leaf, stem and root extracts from Orostachys japonicus and their heat and pH stabilities. J. Korean Soc. Food Sci. Nutr. 38: 1571-1679. https://doi.org/10.3746/jkfn.2009.38.11.1571
  15. Yoon, S. Y., S. Y. Lee, K. B. W. R. Kim, E. J. Song, S. J. Lee, C. J. Lee, N. B. Park, J. Y. Jung, J. H. Kwak, K. W. Nam, and D. H. Ahn (2010) Antimicrobial activity of the Sargassum fulvellum ethanol extract and the effect of temperature and pH on their activity. Korean J. Food Sci. Technol. 42: 155-159.
  16. Ryu, B. H., D. S. Kim, K. Cho, and D. B. Sin (1989) Antitumor activity of seaweeds toward Sarcoma-180. Korean J. Food Sci. Technol. 21: 595-600.
  17. Kim, J. Y., K. H. Kim, H. S. Suh, and W. C. Choi (1997) Antiinflammatory effects of new chemical compounds, HS-1580 series (HS-1580, HS-1581, HS-1582). J. Life Sci. 16: 1181-1187. https://doi.org/10.5352/JLS.2006.16.7.1181
  18. Lee, S. H., Y. Li, F. Karadeniz, M. M. Kim, and S. K. Kim (2009) $\alpha$-Glucosidase and $\alpha$--amylase inhibitory activities of phloroglucinal derivatives from edible marine brown alga, Ecklonia cava. J. Sci. Food Agr. 89: 1552-1558. https://doi.org/10.1002/jsfa.3623
  19. Jimenez-Escring, A. and C. I. Goni (1999) Nutritional evaluation and physiological effects of edible seaweeds. Arch. Latinoam. Nutr. 49: 114-120.
  20. Fukuyama, Y., Y. Nakayama, and M. Takahashi (1989) Structure of an anti-plasmin inhibitor, eckol, isolated from the brown alga Ecklonia kurome Okamura and inhibitory activities of its derivatives on plasma plasmin inhibitors. Chem. Pharm. Bull. 37: 349-353. https://doi.org/10.1248/cpb.37.349
  21. Nakamura, T., K. Nagayama, K. Uchida, and R. Tanaka (1996) Antioxidant activity of phlorotannins isolated from the brown alga Eisenia bicylis. Fisheries Sci. 62: 923-926. https://doi.org/10.2331/fishsci.62.923
  22. Kang, H. S., H. Y. Chung, J. Y. Kim, B. W. Son, H. A. Jung, and J. S. Choi (2004) Inhibitory phlorotannins from the edible brown alga Ecklonia stolonifera on total reactive oxygen species (ROS) generation. Arch. Pharm. Res. 27: 194-198. https://doi.org/10.1007/BF02980106
  23. Kang, K., Y. Park, H. J. Hwang, S. H. Kim, J. G. Lee, and H. C. Shin (2003) Antioxidative properties of brown algae polyphenolics and their perspecctives as chemopreventive agents against vascular risk factors. Arch. Pharm. Res. 26: 286-293. https://doi.org/10.1007/BF02976957
  24. Ahn, M. J., K. D. Yoon, S. Y. Min, J. S. Lee, J. H. Kim, T. G. Kim, S. H. Kim, N. K. Kim, H. Huh, and J. W. Kim (2004) Inhibition of HIV-1 reverse transcriptase and protease by phlorotannins from the brown alga Ecklonia cava. Biol. Pharm. Bull. 27: 544-547. https://doi.org/10.1248/bpb.27.544
  25. Lee, S. H., M. H. Park, S. J. Heo, S. M. Kang, S. C. Ko, J. S. Han, and Y. J. Jeon (2010) Dieckol isolated from Ecklonia cava inhibits $\alpha$-glucosidase and $\alpha$-amylase in vitro and alleviates postprandial hyperglycemia in streptozotocin-induced diabetic mice. Food Chem. Toxicol. 48: 2633-2637. https://doi.org/10.1016/j.fct.2010.06.032
  26. Yoon, N. Y., T. K. Eom, M. M. Kim, and S. K. Kim (2009) Inhibitory effect of phlorotannins isolated from Ecklonia cava on mushroom tyrosinase activity and melanin formation in mouse B16F10 melanoma cells. J. Agr. Food Chem. 57: 4124-4129. https://doi.org/10.1021/jf900006f
  27. Bu, H. J., Y. M. Ham, J. M. Kim, S. J. Lee, J. W. Hyun, and N. H. Lee (2006) Elastase and hyaluronidase inhibition activities of phlorotannins isolated from Ecklonia cava. Korean J. Pharmacogn. 37: 92-96.
  28. Hummel, B. C. W. (1959) A modified spectrophotometric determination of chymotrypsin, trypsin, and thrombin. Can. J. Biochem. Physiol. 37: 1394-1399.
  29. Kim, S. J., D. H. Kweon, and J. H. Lee (2006) Investigation of anti-oxidative activity and stability of ethanol extracts of licorice rood (Glycyrrhiza glabra). Korean J. Food Sci. Technol. 38: 584-588.
  30. Lim, E. J., Y. H. Lee, C. O. Huh, S. H. Kwon, J. Y. Kim, and Y. B. Han (2007) Rheological properties of bread dough added with Enteromorpha intenstinalis. Korean J. Food Sci. Technol. 39: 652-657.
  31. Jung, S. A., K. B. W. R. Kim, M. J. Kim, D. H. Kim, C. Sunwoo, H. J. Kim, D. H. Jeong, H. Y. Jeong, T. W. Kim, Y. J. Cho, and D. H. Ahn (2012) Trypsin inhibitory activity of water extracts from Ecklonia cava as affected by temperature and pH. J. Korean Soc. Food Sci. Nutr. 41: 840-845. https://doi.org/10.3746/jkfn.2012.41.6.840
  32. Jin, S. K., I. S. Kim, K. H. Hah, K. H. Park, I. J. Kim, and J. R. Lee (2006) Changes of pH, acidity, protease activity and microorganism on sauces using a korean traditional seasoning during cold storage. Korean J. Food Sci. Ani. Resour. 26: 159-165.
  33. Kim, K. B. W. R., D. H. Kim, C. Sunwoo, Y. K. Hong, and D. H. Ahn (2012) Effects of Curcuma aromatica extract and orange rind mixed liquor on the quality of Cypselurus agoo agoo roe treated with electrolyzed water. Korean J. Fish Aquat. Sci. 45: 122-131. https://doi.org/10.5657/KFAS.2012.0122
  34. Bitou, N., M. Ninomiya, T. Tsujita, and H. Okuda (1999) Screening of lipase inhibitors from marine algae. Lipids 34: 441-445. https://doi.org/10.1007/s11745-999-0383-7
  35. Ahn, I. S., K. Y. Park, and M. S. Do (2007) Weight control mechanisms and antiobesity functional agents. J. Korean Soc. Food Sci. Nutr. 36: 503-513. https://doi.org/10.3746/jkfn.2007.36.4.503
  36. Quiros, A. R. B., S. Frecha-Ferreiro, A. M. Vidal-Perez, and J. Lopez-Hernandez (2010) Antioxidant compounds in edible brown seaweeds. Eur. Food Res. Technol. 231: 495-498. https://doi.org/10.1007/s00217-010-1295-6
  37. Deavile, E. R., R. J. Green, I. Muller-Harvey, I. Willoughby, and R. A. Frazier (2007) Hydrolyzable tannin structures influence relative globular and random coil protein binding strengths. J. Agr. Food Chem. 55: 4554-4561. https://doi.org/10.1021/jf063770o
  38. Kawamoto, H., F. Nakatsubo, and K. Murakami (1996) Stoichiometric studies of tannin-protein co-precipitation. Phytochemistry 41: 1427-1431. https://doi.org/10.1016/0031-9422(95)00728-8
  39. Kim, K. H., S. G. Roh, C. R. Li, C. F. Jin, A. Kim, and W. C. Choi (2008) Anti-diabetic effects of banaba leaf extracts (Lagerstroemia speciosa Pers.) through solvents. J Life Sci. 18: 1305-1311. https://doi.org/10.5352/JLS.2008.18.9.1305
  40. Losso, J. N. (2008) The biochemical and functional food properties of the Bowman-Birk inhibitor. Crit. Rev. Food Sci. 48: 94-118. https://doi.org/10.1080/10408390601177589
  41. Klomklao, S., S. Benjakul, H. Kishimura, and M. Chaijan (2011) Extraction, purification and properties of trypsin inhibitor from Thai mung bean (Vigna radiata (L.) R. Wilczek). Food Chem. 129: 1348-1354. https://doi.org/10.1016/j.foodchem.2011.05.029
  42. Jung, J. Y., K. B. W. R. Kim, C. J. Lee, J. H. Kwak, M. J. Kim, D. H. Kim, C. Sunwoo, T. W. Kim, and D. H. Ahn (2011) Inhibitory effect of Ecklonia cava extracts against lipase activity and stability effect of temperature and pH on their activity. J. Korean Soc. Food Sci. Nutr. 40: 969-974. https://doi.org/10.3746/jkfn.2011.40.7.969
  43. Babar, V. S., J. K. Chavan, and S. S. Kadam (1988) Effect of heat treatments and germination on trypsin inhibitor activity and polyphenols in jack bean (Canavalia ensiformis L.DC). Plant Food Hum. Nutr. 38: 319-324. https://doi.org/10.1007/BF01091729
  44. Kadam, S. S. and R. R. Smithard (1987) Effects of heat treatments on trypsin inhibitor and hemagglutinating activities in winged bean. Plant Food Hum. Nutr. 37: 151-159. https://doi.org/10.1007/BF01092051
  45. Kim, D. H., K. B. W. R. Kim, M. J. Kim, C. Sunwoo, S. A. Jung, H. J. Kim, D. H. Jeong, T. W. Kim, Y. J. Cho, and D. H. Ahn (2012) Effects of heat, pH, and gamma irradiation treatments on lipase inhibitory activity of Sargassum thunbergii ethanol extract. J. Korean Soc. Food Sci. Nutr. 41: 566-570. https://doi.org/10.3746/jkfn.2012.41.4.566
  46. Kown, H. J., K. H. Lee, J. H. Kim, S. S. Chun, and W. S. Cho (2006) Effects of protease on the extraction and properties of the protein from silkworm pupa. J. Korean Soc. Appl. Biol. Chem. 49: 304-308.
  47. Lim, S. I. (2000) Purification and characterization of protease produces by Aspergillus wentii isolated from korean traditional Meju. Korean J. Food Sci. Technol. 32: 161-167.
  48. Kim, J. B. (1998) Purification and properties of protease inhibitor from Streptomyces sp. SK-862. Korean J. Food Nutr. 11: 678-682.
  49. Ye, X. J. and T. BunNg (2009) Isolation and characterization of a trypsin inhibitor and a lectin from Glycine max cv. large black soybean. Food Sci. Biotechnol. 18: 1173-1179.