Korean Journal of Fisheries and Aquatic Sciences (한국수산과학회지)

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
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Chromatographic Fractionation of Protease Inhibitors from Fish Eggs

어류 알로부터 Protease Inhibitors의 크로마토그래피법에 의한 분획

  • Kim, Jin-Soo (Department of Seafood Science & Technology/Institute of Marine Industry, Gyeongsang National University) ;
  • Kim, Ki Hyun (Department of Seafood Science & Technology/Institute of Marine Industry, Gyeongsang National University) ;
  • Kim, Hyeon Jeong (Department of Seafood Science & Technology/Institute of Marine Industry, Gyeongsang National University) ;
  • Kim, Min Ji (Department of Seafood Science & Technology/Institute of Marine Industry, Gyeongsang National University) ;
  • Park, Sung Hwan (Department of Food & Nutrition/Institute of Marine Industry, Gyeongsang National University) ;
  • Lee, Hyun Ji (Department of Food & Nutrition/Institute of Marine Industry, Gyeongsang National University) ;
  • Heu, Min Soo (Department of Food & Nutrition/Institute of Marine Industry, Gyeongsang National University)
  • 김진수 (경상대학교 해양식품공학과/해양산업연구소) ;
  • 김기현 (경상대학교 해양식품공학과/해양산업연구소) ;
  • 김현정 (경상대학교 해양식품공학과/해양산업연구소) ;
  • 김민지 (경상대학교 해양식품공학과/해양산업연구소) ;
  • 박성환 (경상대학교 식품영양학과/해양산업연구소) ;
  • 이현지 (경상대학교 식품영양학과/해양산업연구소) ;
  • 허민수 (경상대학교 식품영양학과/해양산업연구소)
  • Received : 2013.06.11
  • Accepted : 2013.07.24
  • Published : 2013.08.31
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Abstract

A protease inhibitor from fish eggs was fractionated using chromatographic methods. The fractionation efficiency was evaluated in terms of specific inhibitory activity (SIA, U/mg), purity (fold), total inhibitory activity (TIA, U), and recovery (%). The protease inhibitor (PI) from egg extracts of skipjack tuna (ST Katsuwonus pelamis), yellowfin tuna (YT Thunnus albacares) and Alaska pollock (AP Theragra chalcogramma) was fractionated using Sephadex G-50 gel filtration and DEAE-Sepharose CL-6B anion exchange chromatography based on protein size exclusion and net charge, respectively. Fractions exhibiting strong inhibitory activity were contained in the 30-50 kDa fraction on gel filtration and in the range of 0.4-0.7 M NaCl gradient fraction on anion exchange chromatography. The respective TIA and percent recovery of the fraction obtained with gel filtration toward trypsin and $N{\alpha}$-benzoyl-L-arginine-p-nitroanilide (BAPNA) were 2,758.7 U and 29.6% for ST, 1,005.5 U and 25.6% for YT, and 1,267.5 U and 26.0% for AP. Gel filtration chromatography was more effective at fractionating PI than using ion exchange chromatography. These results suggest that fish eggs act as serine protease inhibitors and might be useful for protease inhibition in foodstuffs.

Keywords

References

  1. An H, Peters MY and Seymour TA. 1996. Roles of endogenous enzymes in surimi gelation. J Food Sci 7, 321-326.
  2. Dawson RMC, Elliot DC, Elliot WH and Jones KM. 1986. Data for biochemical research, 3rd ed., Oxford Univ Press, Oxford, UK, 417-441.
  3. Eun JB, Chung HJ and Heansberg JO. 1994. Chemical composition and microflora of channel catfish (Ictalurus punctatus) roe and swim bladder. J Agric Food Chem 42, 714-717. https://doi.org/10.1021/jf00039a022
  4. Hamann DD, Amato PM, Wu MC and Foegeding EA. 1990. Inhibition of modori (gel weakening) in surimi by plasma hydrolysate and egg white. J Food Sci 55, 665-669. https://doi.org/10.1111/j.1365-2621.1990.tb05202.x
  5. Heu MS and Ahn SH. 1999. Development and fractionation of proteolytic enzymes from inedible seafood product. J Kor Fish Soc 32, 458-465.
  6. Heu MS, Kim HS, Jung SC, Park CH, Park HJ, Yeum DM, Park HS, Kim CG and Kim JS. 2006. Food component characteristics of skipjack (Katsuwonus pelamis) and yellowfin tuna (Thunnus albacares) roes. J Kor Fish Soc 39, 1-8. https://doi.org/10.5657/kfas.2006.39.1.001
  7. Intarasirisawat R, Benjakul S and Visessanguan W. 2011. Chemical compositions of the roes from skipjack, tongol and bonito. Food Chem 124, 1328-1334. https://doi.org/10.1016/j.foodchem.2010.07.076
  8. Jeong BY, Moon SK, Jeong WG and Ohshima T. 2000. Lipid class and fatty acid compositions of wild and cultured sweet smelt Plecoglossus altivelis muscles and eggs. Fish Sci 66, 716-724. https://doi.org/10.1046/j.1444-2906.2000.00117.x
  9. Ji SJ, Lee JS, Shin JH, Park KH, Kim JS, Kim KS and Heu MS. 2011. Distribution of protease inhibitors from fish eggs as seafood processing byproducts. Kor J Fish Aquat Sci 44, 8-17. https://doi.org/10.5657/kfas.2011.44.1.008
  10. Joe SJ and Jo JH. 1993. Changes in the fatty acid composition of phospholipid in the dried and salted mullet roe during processing and storaging. J Kor Soc Food Nutr 22, 286-290.
  11. Joe SJ. 1991. Effect of drying air velocity on the quality of salted and dried mullet roe. J Kor Soc Food Nutr 20, 503-508.
  12. Jung WK, Park PJ and Kim SK. 2003. Purification and characterization of a new lection from the hard roe of skipjack tuna, Katsuwonus pelamis. Int'l J Biochem Cell Biol 35, 255-265. https://doi.org/10.1016/S1357-2725(02)00176-0
  13. Kang IS and Lanier TC. 1999. Bovine plasma protein functions in surimi gelation compared with cysteine protease inhibitors. J Food Sci 64, 842-846. https://doi.org/10.1111/j.1365-2621.1999.tb15924.x
  14. Kim HJ, Kim KH, Song SM, Kim IY, Park SH, Gu EJ, Lee HJ, Kim JS and Heu MS. 2013. Fractionation and characterization of protease inhibitors from fish eggs based on protein solubility. Kor J Fish Aquat Sci 46, 119-128. https://doi.org/10.5657/KFAS.2013.0119
  15. Kim HS, Kim JS and Heu MS. 2008. Fractionation of exopeptidase from viscera of the Argentina shortfin squid Illexargentinus. J Kor Soc Food Nutr 37, 1009-1017. https://doi.org/10.3746/jkfn.2008.37.8.1009
  16. Kim JW, Min TJ and Lee TY. 1988. Subunits and composition of carotenoprotein from Salmo salar eggs. J Kor Appl Chem 32, 377-384.
  17. Kim SM. 1996. The effect of sulfite salts on the shelf-life of lowsalted Myungranjeot (Soused roe of Alaska pollack). Kor J Food Sci Technol 28, 940-946.
  18. Lowry OH, Rosebrough NJ, Farr AL and Randall RJ. 1951. Protein measurement with Folin phenol reagent. J Biol Chem 193, 256-275.
  19. Morrissey MT, Wu JW and An H. 1993. Protease inhibitor effects on torsion measurement and autolysis of Pacific whiting surimi. J Food Sci 58, 1050-1054. https://doi.org/10.1111/j.1365-2621.1993.tb06109.x
  20. Oda S, Igarashi Y, Manaka KI, Koibuchi N, Sakai-Sawada M, Sakai M, Morisawa M, Otake H and Shimizu N. 1998. Sperm-activating proteins obtained from the herring eggs are homologous to trypsin inhibitors and synthesized in follicle cells. Dev Biol 204, 55-63. https://doi.org/10.1006/dbio.1998.9056
  21. Park JO, Kim HJ and Sung NJ. 1983. The taste compounds of the fermented cod-roe, Gadus macrocephlus - Change of nucleotides and their related compounds in cod roe. J Home Econ Assoc 21, 51-57.
  22. Preneta AZ.1989. Separation on the basis of size: Gel permeation chromatography. In : Protein purification methods a practical approach, Harris ELV and Angal S (ed.), IRL Press, Oxford, UK, 299-304.
  23. Roe S. 1989. Separation based on structure. In: Protein purification methods a practical approach, Harris ELV and Angal S (ed.), IRL Press, Oxford, UK, 200-215.
  24. Shimada K and Ogura N. 1990. Lipid changes in sea urchin gonads during storage. J Food Sci 55, 967-971. https://doi.org/10.1111/j.1365-2621.1990.tb01576.x
  25. Shina N, Tateno H, Ogawa T, Muramoto K, Saneyoshi M and Kamiya H. 2002. Isolation and characterization of L-rhamnose-binding lectins from chum salmon (Oncorhynchus keta) eggs. Fish Sci 68, 1352-1366. https://doi.org/10.1046/j.1444-2906.2002.00575.x
  26. Tsai YJ, Chang GD, Haung CJ, Chang YS and Haung FL. 1996. Purification and molecular cloning of carp ovarian cystatin. Comp Biochem Physiol B 113, 573-580. https://doi.org/10.1016/0305-0491(95)02070-5
  27. Ustadi K, Kim KY and Kim SM. 2005. Characteristics of protease inhibitor purified from the eggs of Alaska pollock (Theragrachalcogramma). J Kor Fish Soc 38, 83-88. https://doi.org/10.5657/kfas.2005.38.2.083
  28. Walker JM. 2002. Nondenaturing polyacrylamide gel electrophoresis of protein. In: The Protein Protocols Handbook, 2nd Ed. Walker JM (ed.), Huana Press, Totowa, NJ, USA, 57-60.
  29. Yamashita M and Konagaya S. 1991. Cysteine protease inhibitor in egg of chum salmon. J Biochem 110, 762-766.

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