DOI QR코드

DOI QR Code

Isolation and Charaterization of Bioactive Peptides from Hwangtae (yellowish dried Alaska pollack) Protein Hydrolysate

  • Cho, San-Soon (Department of Food Science and Technology, Kongju National University) ;
  • Lee, Hyo-Ku (Department of Food Science and Technology, Kongju National University) ;
  • Yu, Chang-Yeon (Division of Applied Plants Science, Kangwon National University) ;
  • Kim, Myong-Jo (Division of Applied Plants Science, Kangwon National University) ;
  • Seong, Eun-Soo (Bioherb Research Institute, Kangwon National University) ;
  • Ghimire, Bimal Kumar (Bioherb Research Institute, Kangwon National University) ;
  • Son, Eun-Hwa (Department of Herbal Medicine Resource, Kangwon National University) ;
  • Choung, Myoung-Gun (Department of Herbal Medicine Resource, Kangwon National University) ;
  • Lim, Jung-Dae (Department of Herbal Medicine Resource, Kangwon National University)
  • Published : 2008.09.30

Abstract

Hwangtae, dried Alaska pollack, is a major storage product in the fish processing industry. Hwangtae is prepared by removing the internal organs and drying outdoors during the cold witner months by allowing it to thaw during the daytime and re-freeze at night under sub-zero ($-10^{\circ}C$) conditions and gradually dry from December until the next April for around 5 months from Myungtae. In this study, ground Hwangtae was hydrolyzed using two proteolytic enzymes (pepsin and alcalase) which produced five soluble active peptides from Hwangtae (yellowish dried Pollack, Theragra chalcogramma) protein. Two different peptides with strong antioxidative activity were isolated from the hydrolysate using consecutive chromatographic methods of Sephadex G-25 gel, ion-exchange chromatography on a Sepharose-Sephadex C-25 gel, and high-performance liquid chromatography. The isolated peptides, APO1 and APO2, were composed of 16 and 13 amino acid residues, respectively. Both peptides contained a Gly residue at the C-terminus and the repeating motif Gly-Pro-Hyp. The peptide with a molecular weight less than 1,000 Daltons (APACE) obtained from enzymatic hydrolysates of Hwangtae exhibited the highest ACE inhibitory activity. The APACE peptides was composed of 4 amino acid residues (Gly-Leu-Leu-Pro). These results suggest that Hwangtae hydrolysates could be a good source of peptides with ACE inhibitory activity. Biochemical analysis indicated that two 70 kDa peptides (APG1 and APG2) isolated from the hydrolysate had gelatinoytic activity, which was shown to be a calcium dependent protease type as showed by gelatin SDS PAGE.

Keywords

References

  1. Burr ML, Fehily AM, Gilbert JF, Rogers S, Holliday RM, Sweetnam PM, Elwood PC, Deadmann NM. 1989. Effects of changes in fat fish and fibre intakes on death and myocardial reinfarction: diet and reinfarction trial (DART). Lancet 2: 757-761 https://doi.org/10.1016/S0140-6736(89)90828-3
  2. Iwaniak A, Minkiewicz P. 2007. Protein as the source of physiologically and functionally active peptides. Acta Sci Pol Tehcnol Aliment 6: 5-15
  3. Korhonen H, Pihlanto A. 2003. Food-derived bioactive peptides: Opportunities for designing future foods. Curr Pharm Des 9: 1297-1308 https://doi.org/10.2174/1381612033454892
  4. Branen AL. 1975. Toxicology and biochemistry of butylated hydroxyanisole and butylated hydroxytoluene. J Am Oil Chem Soc 52: 59-63 https://doi.org/10.1007/BF02901825
  5. Osawa T, Namiki M. 1985. Natural antioxidants isolated from Eucalyptus leaf waxes. J Agric Food Chem 33: 777-780 https://doi.org/10.1021/jf00065a001
  6. Chung IK, Kim HS, Kang TK, Choi YJ, Choi JD, Kim JS, Heu MS. 2006. Preparation and functional properties of enzymatic oyster hydrolysate. J Korean Soc Food Sci Nutr 35: 919-925 https://doi.org/10.3746/jkfn.2006.35.7.919
  7. Jun SY, Park PJ, Jung WK, Kim SK. 2004. Purification and characterization of an antioxidative peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein. Eur Food Res Technol 219: 20-26 https://doi.org/10.1007/s00217-004-0882-9
  8. Kim SE, Kim YT, Byun HG, Nam KS, Joo DS, Shahidi F. 2001. Isolation of characterization of antioxdative peptides from gelatin hydrolysate of Alaska pollack skin. J Agri Food Chem 49: 1984-1989 https://doi.org/10.1021/jf000494j
  9. Je JY, Park PJ, Kim SK. 2005. Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate. Food Res Int 38: 45-50 https://doi.org/10.1016/j.foodres.2004.07.005
  10. Kannel WB. 1996. Blood pressure as a cardiovascular risk factor. J Am Med Assoc 275: 1571-1576 https://doi.org/10.1001/jama.275.20.1571
  11. Raia JJ Jr, Barone JA, Byerly WG, Lacy CR. 1990. Angiotensin converting enzyme inhibitors: a comparative review. The Annals of Pharmacotherapy 24: 506-525
  12. Antonios TF, MacGregor GA. 1995. Angiotensin converting enzyme inhibitors in hypertension: potential problems. J Hypertens (Suppl) 13: 11-16 https://doi.org/10.1097/00004872-199509003-00003
  13. Joo DS, Cho SY. 2007. Physocemical properties of carrageenan hydrolysate by organic acids. J Korean Soc Food Sci Nutr 36: 262-268 https://doi.org/10.3746/jkfn.2007.36.3.262
  14. Ukeda H, Matsuda H, Osajima K, Matsufuji H, Matsui T, Osajima Y. 1992. Peptides from peptic hydrolysate of heated sardine meat that inhibit angiotensin I-converting enzyme. Nippon Nogeikagaku Kaishii 66: 25-29 https://doi.org/10.1271/nogeikagaku1924.66.25
  15. Oh HS, Kim JS, Heu MS. 2007. Preparation of fuctional seasoning sauce using enzymatic hydrolysate from skipjack tuna cooking drip. J Korean Soc Food Sci Nutr 36: 766-772 https://doi.org/10.3746/jkfn.2007.36.6.766
  16. Murray BA, FitzGerald RJ. 2007. Angiotensin converting enzyme inhibitory peptides derived from food Proteins: biochemistry, bioactivity and production. Curr Pharm Des 13: 773-791 https://doi.org/10.2174/138161207780363068
  17. Sathivel S, Bechtel PJ, Babbitt J, Prinyawiwatkul W, Negulescu II, Reppond KD. 2004. Properties of protein powders from arrowtooth flounder (Atheresthes stomias) and herring (Clupea harengus) by-product. J Agric Food Chem 52: 5040-5046 https://doi.org/10.1021/jf0351422
  18. Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685 https://doi.org/10.1038/227680a0
  19. Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 19: 248-254 https://doi.org/10.1016/0003-2697(76)90527-3
  20. Heussen C, Dowdle EB. 1980. Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulphate and copolymerized substrates. Anal Biochem 72: 248-254 https://doi.org/10.1016/0003-2697(76)90527-3
  21. Osawa T, Namiki M. 1985. Natural antioxidant isolated from Eucalyptus leaf waxes. J Agric Food Chem 33: 777-780 https://doi.org/10.1021/jf00065a001
  22. Cushman DW, Cheung HS. 1971. Spectrophotometric assay and properties of the angiotensin converting enzyme of rabbit lung. Biochem Pharmacol 20: 1637-1648 https://doi.org/10.1016/0006-2952(71)90292-9
  23. Karawita R, Park PJ, Siriwardhana N, Jeon BT, Moon SH, Ahn DK, Cho SK, Jeon YJ. 2005. Angiotensin-I converting enzyme inhibitory activity of Elk (Cervus elaphus) velvet anther. J Food Sci Nutr 10: 239-243 https://doi.org/10.3746/jfn.2005.10.3.239
  24. Liu LL, Pigott GM. 1981. Preparation and use of inex pensive crude pepsin for enzyme hydrolysis of fish. J Food Sci 46: 1569-1572 https://doi.org/10.1111/j.1365-2621.1981.tb04223.x
  25. Tarky W, Agarwala OP, Pigott GM. 1973 Protein hydrolysate from fish waste. J Food Sci 38: 917-918 https://doi.org/10.1111/j.1365-2621.1973.tb02113.x
  26. Quaglia GB, Orban E. 1987. Enzymatic solubilisation of proteins of sardine (Sardina pilchardus) by commercial proteases. J Sci Food Agric 38: 263-269 https://doi.org/10.1002/jsfa.2740380310
  27. Adler-Nissen J. 1986. Enzymic Hydrolysis of Food Proteins, Elsevier Applied Science Publishers, Barking, UK
  28. Stetler-Stevenson WG, Krutzsch HC, Wacher MP, Margulies IMK, Liotta LA. 1989. The activation of human type-IV collagenase proenzyme-sequence identification of the major conversion product following organomercurial activation. J Biol Chem 264: 1353-1356
  29. Koshikawa N, Yasumitsu H, Umeda M, Miyazaki K. 1992. Multiple secretion of matrix serine proteinases by human gastric carcinoma cell-lines. Cancer Res 52: 5046-5053
  30. Okada Y, Gonoji Y, Naka K, Tomita K, Nakanishi I, Iwata K, Yamashita K, Hayakawa T. 1992. Matrix metalloproteinase 9 (92 kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. J Biol Chem 267: 21712-21719
  31. Uchida K, Kawakishi S. 1992. Sequence-dependant reactivity of histidine-containing peptides with copper (II)/ascorbate. J Agric Food Chem 40: 13-16 https://doi.org/10.1021/jf00013a003
  32. Murase H, Nagao A, Terao J. 1993. Antioxidant and emulsifying activity of N-(long-chain-acyl) histidine and N-(long chain-acyl) carnosine. J Agric Food Chem 41: 1601-1604 https://doi.org/10.1021/jf00034a014
  33. Park PJ, Jung WK, Nam KS, Shahidi F, Kim SK. 2001. Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin-free egg yolk. J Am Oil Chem Soc 78: 651-656 https://doi.org/10.1007/s11746-001-0321-0
  34. Titani K, Koide A, Hermann J, Ericssion LH, Kumar S, Wade RD, Walsh KA, Neurath H, Fisher EH. 1977. Complete amino acid sequence of rabbit muscle glycogen phophorylase. Proc Natl Acad Sci USA 74: 4762-4766 https://doi.org/10.1073/pnas.74.11.4762
  35. Lee TG, Yeum DM, Kim YS, Yeo SG, Lee YW, Kim JS, Kim IS, Kim SB. 2005. Peptide inhibitor for agiotensin converting enzyme form thermolysin hydrolysate of Manila Clam protein. J Fish Sci Technol 8: 109-112 https://doi.org/10.5657/fas.2005.8.2.109
  36. Marcuse R. 1962. The effect of some amino acids on the oxidation of linoleic acid and its methyl ester. J Am Oil Chem Soc 39: 97-103 https://doi.org/10.1007/BF02631680
  37. Karel M, Tannenbaum SR, Wallace DH, Maloney H. 1966. Autooxidation of methyl linoleate in freeze-dried model systems. Effects of added amino acids. J Food Sci 31: 892-896 https://doi.org/10.1111/j.1365-2621.1966.tb03266.x
  38. Yamaguchi N. 1971. Studies on antioxidative activities of amino compounds on fats and oils. Part I. Oxidation of methionine during course of autoxidation of linoleic acid. Nippon Shokuhin Kogyo Gakkaishi 18: 313-318 https://doi.org/10.3136/nskkk1962.18.313
  39. Byun HG, Kim SK. 2001. Purification and characterization of angiotensin I-converting enzyme (ACE) inhibitory activity from Alaska pollack (Theranga chalcogramma) skin. Proc Biochem 36: 1155-1162 https://doi.org/10.1016/S0032-9592(00)00297-1

Cited by

  1. Marine bioactive peptides: Types, structures, and physiological functions vol.33, pp.1, 2017, https://doi.org/10.1080/87559129.2015.1137311
  2. Development and biological activities of marine-derived bioactive peptides: A review vol.2, pp.1, 2010, https://doi.org/10.1016/j.jff.2010.01.003
  3. Protein hydrolysates from Bluefin Tuna (Thunnus thynnus) heads as influenced by the extent of enzymatic hydrolysis vol.17, pp.4, 2012, https://doi.org/10.1007/s12257-012-0053-y
  4. The biological activities of fish peptides and methods of their isolation vol.38, pp.6, 2012, https://doi.org/10.1134/S1063074012060090
  5. Marine bioactive compounds and health promoting perspectives; innovation pathways for drug discovery vol.50, 2016, https://doi.org/10.1016/j.tifs.2016.01.019
  6. Separation of Iron-Binding Peptides from Shrimp Processing By-products Hydrolysates vol.4, pp.8, 2011, https://doi.org/10.1007/s11947-010-0416-3
  7. Evidence of Anti-Proliferative Activities in Blue Mussel (Mytilus edulis) By-Products vol.11, pp.4, 2013, https://doi.org/10.3390/md11040975
  8. An Antihypertensive Peptide from Tilapia Gelatin Diminishes Free Radical Formation in Murine Microglial Cells vol.59, pp.22, 2011, https://doi.org/10.1021/jf202837g
  9. Purification and identification of antihypertensive peptides from seaweed pipefish (Syngnathus schlegeli) muscle protein hydrolysate vol.44, pp.3, 2011, https://doi.org/10.1016/j.foodres.2010.12.022
  10. Bacteriological properties and health-related biochemical components of fermented fish sauce: An overview vol.32, pp.2, 2016, https://doi.org/10.1080/87559129.2015.1057844
  11. Physicochemical Properties of Isolated Peptides from Hwangtae (yellowish dried pollack) Protein Hydrolysate vol.13, pp.3, 2008, https://doi.org/10.3746/jfn.2008.13.3.204
  12. Microalgae as a Potential Source of Bioactive Food Compounds vol.9, pp.3, 2008, https://doi.org/10.12944/crnfsj.9.3.18