Fisheries and Aquatic Sciences

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
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The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate

  • Kim, Sung-Rae (Department of Marine Biotechnology, Gangneung-Wonju National University) ;
  • Byun, Hee-Guk (Department of Marine Biotechnology, Gangneung-Wonju National University)
  • Received : 2012.05.08
  • Accepted : 2012.07.02
  • Published : 2012.09.30
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Abstract

The purpose of this study was the purification and characterization of an angiotensin I converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates of rainbow trout Oncorhynchus mykiss muscle. After removal of lipid, the approximate composition analysis of the rainbow trout revealed 24.4%, 1.7%, and 68.3% for protein, lipid, and moisture, respectively. Among six hydrolysates, the peptic hydrolysate exhibited the highest ACE inhibitory activity. We attempted to purify ACE inhibitory peptides from peptic hydrolysate using high performance liquid chromatography on an ODS column. The $IC_{50}$ value of purified ACE inhibitory peptide was $63.9{\mu}M$. The amino acid sequence of the peptide was identified as Lys-Val-Asn-Gly-Pro-Ala-Met-Ser-Pro-Asn-Ala-Asn, with a molecular weight of 1,220 Da, and the Lineweaver-Burk plots suggested that they act as a competitive inhibitor against ACE. Our study suggested that novel ACE inhibitory peptides purified from rainbow trout muscle protein may be beneficial as anti-hypertension compounds in functional foods.

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References

  1. Association of Official Analytical Chemist (AOAC). 2000. Official Methods of Analysis. 17th ed. Association of Official Analytical Chemist, Washington, DC, US.
  2. Balti R, Nedjar-Arroume N, Bougatef A, Guillochon D and Nasri M. 2010. Three novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) using digestive proteases. Food Res Int 43, 1136-1143. https://doi.org/10.1016/j.foodres.2010.02.013
  3. Bougatef A, Balti R, Nedjar-Arroume N, Rovallec R, Adje EY, Souissi N, Lassoued I, Guillochon D and Nasri M. 2010. Evaluation of angiotensin I-converting enzyme (ACE) inhibitory activities of smooth hound (Mustelus mustelus) muscle protein hydrolysates generated by gastrointestinal proteases: identification of the most potent active peptide. Eur Food Res Technol 231, 127-135. https://doi.org/10.1007/s00217-010-1260-4
  4. Brown JA, Paley RK, Amer S and Aves SJ. 2000. Evidence for an intrarenal renin-angiotensin system in the rainbow trout, Oncorhynchus mykiss. Am J Physiol Regul Integr Comp Physiol 278, R1685- R1691. https://doi.org/10.1152/ajpregu.2000.278.6.R1685
  5. Brown NJ and Vaughan DE. 1998. Angiotensin-converting enzyme inhibitors. Circulation 97, 1411-1420. https://doi.org/10.1161/01.CIR.97.14.1411
  6. Bush K, Herny PR and Slusarchyk DS. 1984. Muraceinsmuramyl peptides produced by Norcardia orientalis as angiotensin converting enzyme inhibitors. J Antibiot 37, 330-335. https://doi.org/10.7164/antibiotics.37.330
  7. Cheung HS, Wang FL, Miguel AO, Emily FS and David WC. 1980. Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. J Biol Chem 255, 401-407.
  8. Cooper JB, Khan G, Taylor G, Tickle IJ and Blundell TL. 1990. X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 $A^{\circ}$ resolution. J Mol Biol 214, 199-222. https://doi.org/10.1016/0022-2836(90)90156-G
  9. Cushman DW and Cheung HS. 1971. Spectrophotometric assay and properties of the angiotensin-coverting enzyme of rabbit lung. Biochem Pharmacol 20, 1637-1648. https://doi.org/10.1016/0006-2952(71)90292-9
  10. Elias RJ, Kellerby SS and Decker EA. 2008. Antioxidant activity of proteins and peptides. Crit Rev Food Sci Nutr 48, 430-441. https://doi.org/10.1080/10408390701425615
  11. Fernandes JMO, Kemp GD, Molle MG and Smith VJ. 2002. Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss. Biochem J 368, 611-620. https://doi.org/10.1042/BJ20020980
  12. Fujita H, Yokoyama K and Yoshikawa M. 2000. Classification and antihypertensive activity of angiotensin I converting enzyme inhibitory peptides derived from food proteins. J Food Sci 65, 564-569. https://doi.org/10.1111/j.1365-2621.2000.tb16049.x
  13. Gokoglu N, Yerlikaya P and Cengiz E. 2004. Effects of cooking methods on the proximate composition and mineral contents of rainbow trout (Oncorhynchus mykiss). Food Chem 84, 19-22. https://doi.org/10.1016/S0308-8146(03)00161-4
  14. Hong F, Ming L, Yi S, Zhanxia L, Yongguan W and Chi L. 2008. The antihypertensive effect of peptides: a novel alternative to drugs? Peptides 29, 1062-1071. https://doi.org/10.1016/j.peptides.2008.02.005
  15. Jang SI, Marsden MJ, Secombes CJ, Choi MS, Kim YG, Kim KJ and Chung HT. 1998. Effect of glycyrrhizin on rainbow trout Oncorhynchus mykiss leukocyte responses. J Korean Soc Microbiol 33, 263-271.
  16. Je JY, Park JY, Jung WK, Park PJ and Kim SK. 2005a. Isolation of angiotensin I converting enzyme (ACE) inhibitor from fermented oyster sauce, Crassostrea gigas. Food Chem 90, 809-814. https://doi.org/10.1016/j.foodchem.2004.05.028
  17. Je JY, Park PJ, Byun HG, Jung WK and Kim SK. 2005b. Angiotensin I converting enzyme (ACE) inhibitory peptide derived from the sauce of fermented blue mussel, Mytilus edulis. Bioresour Technol 96, 1624-1629. https://doi.org/10.1016/j.biortech.2005.01.001
  18. Jiang Z, Tian B, Brodkorb A and Huo G. 2010. Production, analysis and in vivo evaluation of novel angiotensin-I-converting enzyme inhibitory peptides from bovine casein. Food Chem 123, 779-786. https://doi.org/10.1016/j.foodchem.2010.05.026
  19. Khantaphant S, Benjakul S and Ghomi MR. 2011. The effects of pretreatments on antioxidative activities of protein hydrolysate from the muscle of brownstripe red snapper (Lutjanus vitta). LWT Food Sci Technol 44, 1139-1148. https://doi.org/10.1016/j.lwt.2010.10.009
  20. Kim SY, Park PSW and Rhee KC. 1990. Functional properties of proteolytic enzyme modified soy protein isolate. J Agric Food Chem 38, 651-656. https://doi.org/10.1021/jf00093a014
  21. Korhonen H and Pihlanto A. 2006. Bioactive peptides: production and functionality. Int Dairy J 16, 945-960. https://doi.org/10.1016/j.idairyj.2005.10.012
  22. Korhonen M, Pihlanto-Leppala A and Tupasela T. 1998. Impact of processing on bioactive proteins and peptides. Trends Food Sci Technol 9, 307-319. https://doi.org/10.1016/S0924-2244(98)00054-5
  23. Lee JK, Hong S, Jeon JK, Kim SK and Byun HG. 2009. Purification and characterization of angiotensin I converting enzyme inhibitory peptides from the rotifer, Brachionus rotundiformis. Bioresour Technol 100, 5255-5259. https://doi.org/10.1016/j.biortech.2009.05.057
  24. Lee JK, Lee MS, Park HG, Kim SK and Byun HG. 2010. Angiotensin I converting enzyme inhibitory peptide extracted from freshwater zooplankton. J Med Food 13, 357-363. https://doi.org/10.1089/jmf.2009.1241
  25. Lee JK, Jeon JK and Byun HG. 2011. Effect of angiotensin I converting enzyme inhibitory peptide purified from skate skin hydrolysate. Food Chem 125, 495-499. https://doi.org/10.1016/j.foodchem.2010.09.039
  26. Li GH, Le GW, Shi YH and Shrestha S. 2004. Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects. Nutr Res 24, 469-486. https://doi.org/10.1016/j.nutres.2003.10.014
  27. Li ZH, Velisek J, Zlabek V, Grabic R, Machova J, Kolarova J and Randak T. 2010. Hepatic antioxidant status and hematological parameters in rainbow trout, Oncorhynchus mykiss, after chronic exposure to carbamazepine. Chem Biol Interact 183, 98-104. https://doi.org/10.1016/j.cbi.2009.09.009
  28. Pihlanto-Leppala A. 2000. Bioactive peptides derived from bovine whey proteins: opioid and ACE-inhibitory peptides. Trends Food Sci Technol 11, 347-356. https://doi.org/10.1016/S0924-2244(01)00003-6
  29. Pihlanto-Leppala A, Koskinen P, Piilola K, Tupasela T and Korhonen H. 2000. Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides. J Dairy Res 67, 53-64. https://doi.org/10.1017/S0022029999003982
  30. Schwaiger J, Ferling H, Mallow U, Wintermayr H and Negele RD. 2004. Toxic effects of the non-steroidal anti-inflammatory drug diclofenac. Part I. histopathological alterations and bioaccumulation in rainbow trout. Aquat Toxicol 68, 141-150. https://doi.org/10.1016/j.aquatox.2004.03.014
  31. Sheih IC, Fang TJ and Wu TK. 2009. Isolation and characterisation of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the algae protein waste. Food Chem 115, 279-284. https://doi.org/10.1016/j.foodchem.2008.12.019
  32. Simpson BK. 2000. Digestive proteinases from marine animals. In: Seafood Enzymes: Utilization and Influence on Postharvest Seafood Quality. Haard NF, Simpson BK, eds. Marcel Dekker, New York, US, pp. 531-540.
  33. Tsai JS, Lin TC, Chen JL and Pan BS. 2006. The inhibitory effects of freshwater clam (corbicula fluminea, Muller) muscle protein hydrolysates on angiotensin I converting enzyme. Process Biochem 41, 2276-2281. https://doi.org/10.1016/j.procbio.2006.05.023
  34. Wang J, Hu J, Cui J, Bai X, Du Y, Miyaguchi Y and Lin B. 2008. Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats. Food Chem 111, 302-308. https://doi.org/10.1016/j.foodchem.2008.03.059
  35. Wijesekara I and Kim SK. 2010. Angiotensin-I-converting enzyme (ACE) inhibitors from marine resources: prospects in the pharmaceutical industry. Mar Drugs 8, 1080-1093. https://doi.org/10.3390/md8041080
  36. Wijesekara I, Qian ZJ, Ryu BM, Ngo DH and Kim SK. 2011. Purification and identification of antihypertensive peptides from seaweed pipefish (Syngnathus schlegeli) muscle protein hydrolysate. Food Res Int 44, 703-707. https://doi.org/10.1016/j.foodres.2010.12.022
  37. Yu Y, Hu J, Miyaguchi Y, Bai X, Du Y and Lin B. 2006. Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from porcine hemoglobin. Peptides 27, 2950- 2956. https://doi.org/10.1016/j.peptides.2006.05.025
  38. Zhang Y, Lee ET, Devereux RB, Yeh J, Best LG, Fabsitz RR and Howard BV. 2006. Prehypertension, diabetes, and cardiovascular disease risk in a population-based sample: the strong heart study. Hypertension 47, 410-414. https://doi.org/10.1161/01.HYP.0000205119.19804.08
  39. Zhao Y, Li B, Liu Z, Dong S, Zhao X and Zeng M. 2007. Antihypertensive effect and purification of an ACE inhibitory peptide from sea cucumber gelatin hydrolysate. Process Biochem 42, 1586-1591. https://doi.org/10.1016/j.procbio.2007.08.011