DOI QR코드

DOI QR Code

Peptide Inhibitor for Angiotensin-Converting Enzyme from Thermolysin Hydrolysate of Manila Clam Proteins

  • Lee Tae-Gee (Department of Hotel Culinary & Baking, Namdo Provincial College of Jeonnam) ;
  • Yeum Dong-Min (Department of Food Processing & Baking, Yangsan College) ;
  • Kim Young-Sook (Department of Food Processing & Baking, Yangsan College) ;
  • Yeo Saeng-Gyu (Department of Hotel Culinary Arts, Busan College of Information Technology) ;
  • Lee Yong-Woo (Division of Food Science, Dongeui Institute of Technology) ;
  • Kim Jin-Soo (Division of Marine Bioscience Institute of Marine Industry, Gyeongsang National University) ;
  • Kim In-Soo (Division of Marine Bioscience Institute of Marine Industry, Gyeongsang National University) ;
  • Kim Seon-Bong (Faculty of Food and Biotechnology, Pukyong National University)
  • Published : 2005.06.01

Abstract

A peptide that inhibits angiotensin-converting enzyme (ACE) was isolated from a hydrolysate of Manila clam (Ruditapes philippinarum) proteins prepared with thermolysin. Amino acid sequence of the peptide was determined to be Leu-Leu-Pro. Chemically synthesized Leu-Leu-Pro had an $IC_{50}\;value\;of\;158\;\mu{M}$. Peptides related to the Manila clam-derived peptide were synthesized to study the structure-activity relationships. The tetrapeptide, Leu-Leu-Pro-Pro, had a very weak effect on the enzyme. However, Leu-Leu-Pro-Asn showed no inhibitory activity.

Keywords

References

  1. Brewer, H.B., Jr., T. Fairwell, A. LaRue, R. Ronan, A. Houser and T.J. Bronzert. 1978. The amino acid sequence of human ApoA-I, an apolipoprotein isolated from high density lipoproteins. Biochem. Biophys. Res. Commun., 80, 623-630 https://doi.org/10.1016/0006-291X(78)91614-5
  2. EI-Dorry, H.A., H.G. Bull, K. Iwata, N.A. Thornberry, E.H. Cordes and R.L. Soffer. 1982. Molecular and catalytic properties of rabbit testicular dipeptidyl carboxypeptidase. J. Biol. Chem., 257, 14128-14133
  3. Ferreira, S.H., D.C. Bartelt and L.J. Greene. 1970. Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom. Biochemistry, 9, 2583-2593 https://doi.org/10.1021/bi00815a005
  4. Kinoshita, E., J. Yamakoshi and M. Kikuchi. 1993. Purification and identification of an angiotensin I-converting enzyme inhibitor from soy sauce. Biosci. Biotech. Biochem., 57, 1107-1110 https://doi.org/10.1271/bbb.57.1107
  5. Kohama, Y., S. Matsumoto, H. Oka, T. Teramoto, M. Okabe and T. Mimura. 1988. Isolation of angiotensinconverting enzyme inhibitor from tuna muscle. Biochem. Biophys. Res. Commun., 155, 332-337 https://doi.org/10.1016/S0006-291X(88)81089-1
  6. Lee, T.G., Y.B. Park, D.C. Park, D.M. Yeum, I.S. Kim, Y.S. Gu, Y.H. Park and S.B. Kim. 1998. Angiotensin converting enzyme inhibitory activity in enzymatic hydrolysates of anchovy muscle protein. J. Kor. Fish. Soc., 31, 875-881
  7. Maruyama, S., K. Nakagomi, N. Tomizuka and H. Suzuki. 1985. Angiotensin-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. II. Isolation and bradykinin-potentiating activity on the uterus and the ileum of rats. Agric. Biol. Chem., 49, 1405-1409 https://doi.org/10.1271/bbb1961.49.1405
  8. Matsui, T., H. Matsufuji, E. Seki, K. Osajima, M. Nakashima and Y. Osajima. 1993. Inhibition of angiotensin I-converting enzyme by Bacillus lichen iformis alkaline protease hydrolysates derived from sardine muscle. Biosci. Biotech. Biochem., 57, 922-925 https://doi.org/10.1271/bbb.57.922
  9. Matsumura, N., M. Fujii, Y. Takeda, K. Sugita and T. Shimizu. 1993. Angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels autolysate. Biosci. Biotech. Biochem., 57, 695-697 https://doi.org/10.1271/bbb.57.695
  10. Miyoshi, S., H. Ishikawa, T. Kaneko, F. Fukui, H. Tanaka and S. Maruyama. 1991. Structures and activity of angiotensin-converting enzyme inhibitors in an $\alpha$-zein hydrolysate. Agric. Biol. Chem., 55, 1313-1318 https://doi.org/10.1271/bbb1961.55.1313
  11. Ondetti, M.A., N.J. Williams, E.F. Sabo, J. Pluscec, E.R. Weaver and O. Kocy. 1971. Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure, and synthesis. Biochemistry, 10, 4033-4039 https://doi.org/10.1021/bi00798a004
  12. Oshima, G., H. Shimabukuro and K. Nagasawa. 1979. Peptide inhibitors of angiotensin l-converting enzyme in digests of gelatin by bacterial collagenase. Biochim. Biophys. Acta, 566, 128-137 https://doi.org/10.1016/0005-2744(79)90255-9
  13. Skeggs, L.T., W.H. Marsh, J.R. Kahn and N.P. Shumway. 1954. The existence of two forms of hypertensin. J. Exp. Med., 99, 275-282 https://doi.org/10.1084/jem.99.3.275
  14. Titani, K., A. Koide, J. Hermann, L.H. Ericsson, S. Kumar, R.D. Wade, K.A. Walsh, H. Neurath and E.H. Fischer. 1977. Complete amino acid sequence of rabbit muscle glycogen phosphorylase. Proc. Natl. Acad. Sci. USA, 74, 4762-4766
  15. Yang, H.Y.T., E.G. Erdos and Y.A. Levin. 1970. Dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochim. Biophys. Acta, 214, 374-376 https://doi.org/10.1016/0005-2795(70)90017-6

Cited by

  1. Isolation and Charaterization of Bioactive Peptides from Hwangtae (yellowish dried Alaska pollack) Protein Hydrolysate vol.13, pp.3, 2008, https://doi.org/10.3746/jfn.2008.13.3.196
  2. 오징어 간 액젓으로부터 분리된 Angiotensin Converting Enzyme 저해 Peptide의 특성 vol.39, pp.11, 2005, https://doi.org/10.3746/jkfn.2010.39.11.1654