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Abstract

To investigate the basic information and the possibility of ACE-inhibitory peptides for antihypertension materials, goat's caisin (CN) was hydrolyzed by various proteolytic enzymes and ACE-inhibitory peptides were separated and purified. ACE-inhibition ratios of enzymatic hydrolysates of goat's CN and various characteristics of ACE-inhibitory peptides were determined. ACE-inhibition ratios of goat's CN hydrolysates were shown the highest with 87.84% by pepsin for 48 h. By Sephadex G-25 gel chromatograms, Fraction 3 from goat's CN hydrolysates by pepsin for 48 h was confirmed the highest ACE-inhibition activity. Fraction 3 g and Fraction 3 gh from peptic hydrolysates by RP-HPLC to first and second purification were the highest in ACE-inhibition activity, respectively. The most abundant amino acid was leucine (18.83%) in Fraction 3 gh of ACE-inhibitory peptides after second purification. Amino acid sequence analysis of Fraction 3 gh of ACE-inhibitory peptides was shown that the Ala-Tyr-Phe-Tyr, Pro-Tyr-Tyr and Tyr-Leu. IC$_{50}$ calibrated in peptic hydrolysates at 48 h, Fraction 3, Fraction 3 g and Fraction 3 gh from goat's CN hydrolysates by pepsin for 48 h were 29.89, 3.07, 1.85 and 0.87 g/ml, respectively. Based on the results of this experiment, goat's CN hydrolysates by pepsin were shown to have ACE-inhibitory activity.

참고문헌 (29)

  1. Brown, N. J. and D. E. Vaughan. 1998. Angiotensin-converting enzyme inhibitors. Circulation. 97:1411. 
  2. Cushman, D. W. and H. S. Cheung. 1971. Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem. Pharmacol. 20:1637. 
  3. Kohama, Y. 1988. Isolation of angiotensin converting enzyme inhibitors from tuna muscle. Biochem. Biophys. Res. Commun. 155:332. 
  4. Kohmura, M., N. N. Nio and Y. Ariyoshi. 1990. Inhibition of angiotensin converting enzyme by synthetic peptide fragment of human $\kappa$-casein. Agric. Biol. Chem. 54:835. 
  5. Mullally, M. M., H. Meisel and R. J. FitzGerald. 1997. Identification of novel angiotensin-I converting enzyme inhibitory peptide corresponding to tryptic fragment of bovine beta lactoglobulin. FEBS Lett. 402:99. 
  6. Lowry, O. H., N. J. Rosebrough, A. L. Farr and R. J. Randall. 1951. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193:265. 
  7. Miyoshi, S., H. Ishikawa, T. Kaneko, F. Fukui, H. Tanaka and S. Maruyama. 1991. Structure and activity of angiotensin converting enzyme inhibitors in an alpha-zein hydrolysate. Agric. Biol. Chem. 55:1313. 
  8. FitzGerland, R. J. and H. Meisel. 2000. Milk protein-derived peptide inhibitors of angiotensin-I-converting enzyme. Br. J. Nutr. 84:S33. 
  9. Pihlanto-Leppala, A., T. Rokka and H. Korhonen. 1998. Angiotensin I converting enzyme inhibitory peptides derived from bovine milk proteins. Int. Dairy J. 8:325. 
  10. Meisel, H. 1997. Biochemical properties of regulatory peptides derived from milk proteins. Biopolymere. 43:119. 
  11. Oukhatar, N. A., S. Bouhallab, F. Bureau, P. Arhan, J. L. Maubois and D. L. Bougle. 2000. In vitro digestion of caseinophosphopeptide-iron complex. J. Dairy Res. 67:125. 
  12. Haenlein, G. F. W. 1995. Status and prospects of the dairy goat industry in the United States. J. Anim. Sci. 74:1173. 
  13. Kim, S. B., H. S. Shin and J. W. Lim. 2004. Separation of calciumbinding protein derived from enzymatic hydrolysates of cheese whey protein. Asian-Aust. J. Anim. Sci. 17:712. 
  14. Pihlanto-Leppala, A., P. Koskinen, K. Piilola, T. Tupasela and H. Korhonen. 2002. Angiotensin-I converting enzyme inhibitory properties of whey protein digests: Concentration and characterization of active peptides. J. Dairy Res. 67:53. 
  15. Ukeda, H., H. Matsuda, H. Kuroda, K. Osajima, H. Matsufuji and Y. Osajima. 1991. Preparation and separation of angiotensin I converting enzyme inhibitory peptides. Nippon N gelkagaku Kaishi. 65:1223. 
  16. Cheung, H. S., F. L. Wang, M. A. Ondetti, E. F. Sabo and D. W. Chushman. 1980. Binding of peptides substrates and inhibitors of ACE. J. Biol. Chem. 255:401. 
  17. Miyoshi, S., H. Ishikawa and H. Tanaka. 1989. Angiotensin converting enzyme inhibitors derived from ficus carica. Agric. Biol. Chem. 53:2763. 
  18. Adler-Nissen, J. 1986. Enzymic hydrolysis of food proteins. Elservier Applied Science Publishers, New York, USA. 
  19. Hara, Y., T. Matsuzaki and T. Suzuki. 1987. Angiotensin converting enzyme inhibiting activity of tea components. Nippon Shokuhin Kogyo Gakkaishi. 61:803. 
  20. Moore, S., D. H. Spackman and W. H. Stein. 1958. Automatic recording apparatus for use in the chromatography of amino acids. Fed Proc. 17:1107. 
  21. Kim, S. B. and J. W. Lim. 2004. Calcium-binding peptides derived from tryptic hydrolysates of cheese whey protein. Asian-Aust. J. Anim. Sci. 17:1459. 
  22. Seki, E., K. Osajima, T. Matsui and Y. Osajima. 1993. Separation and purification of angiotensin converting enzyme inhibitors peptides from heated sardine meat by treatment with alkaline protease. Nippon Shokuhin Kogyo Gakkaishi. 40:783. 
  23. Adamson, N. J. and E. C. Reynolds. 1996. Characterization of casein phosphopeptides prepared using alcalase: Determination of enzyme specificity. Enzyme Microb, Tech. 19:202. 
  24. Hernandez-Ledesma, B., I. Recio, M. Ramos and L. Amigo. 2002. Preparation of ovine and caprine $\beta$-lactoglobulin hydrolysates with ACE-inhibitory activity. Identification of active peptides from caprine $\beta$-lactoglobulin hydrolysed with thermolysin. Int. Dairy J. 12:805. 
  25. Yeum, D. M., S. B. Roh, T. G. Lee, S. B. Kim and Y. H. Park. 1993. Angiotensin-I converting enzyme inhibitory activity of enzymatic hydrolysates of food proteins. J. Kor. Soc. Food Nutr. 22:226. 
  26. Sofia, V. S. and F. X. Malcata. 2000. Comparative catalytic activity of two plant proteinases upon caprine caseins in solution. Food Chem. 71:207. 
  27. Maruyama, S., K. Nakagomi, N. Tomizuka and H. Suzuki. 1985. Angiotensin I-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. II. Isolation and bradykininpotenting activity on the uterus and the ileum of rats. Agric. Biol. Chem. 49:1405. 
  28. Shimizu, M. 1994. Bioactive peptides from bovine milk proteins. Paper presented at Animal Secetions in 24th International Dairy Congress. Melbourne Sept. p. 18. 
  29. Matsumura, N., M. Fujii, Y. Takeda and T. Shimizu. 1993. Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels. Biosci. Biotech. Bioch. 57:1743. 

이 논문을 인용한 문헌 (2)

  1. 2008. "" Asian-Australasian journal of animal sciences, 21(5): 732~737 
  2. 2011. "" Fisheries and aquatic sciences, 14(4): 283~288 

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