DOI QR코드

DOI QR Code

어류 알의 Protease Inhibitor 활성 분포

Distribution of Protease Inhibitors from Fish Eggs as Seafood Processing Byproducts

  • 지성준 (사조산업(주)) ;
  • 이지선 (경상대학교 해양식품공학과/해양산업연구소) ;
  • 신준호 (경상대학교 해양식품공학과/해양산업연구소) ;
  • 박권현 (경상대학교 해양식품공학과/해양산업연구소) ;
  • 김진수 (경상대학교 해양식품공학과/해양산업연구소) ;
  • 김경섭 (경상대학교 식품영양학과/해양산업연구소) ;
  • 허민수 (경상대학교 식품영양학과/해양산업연구소)
  • Ji, Seong-Jun (Sajo Industries Co., LTD.) ;
  • Lee, Ji-Sun (Department of Seafood Science & Technology / Institute of Marine Industry, Gyeongsang National University) ;
  • Shin, Joon-Ho (Department of Seafood Science & Technology / Institute of Marine Industry, Gyeongsang National University) ;
  • Park, Kwon-Hyun (Department of Seafood Science & Technology / Institute of Marine Industry, Gyeongsang National University) ;
  • Kim, Jin-Soo (Department of Seafood Science & Technology / Institute of Marine Industry, Gyeongsang National University) ;
  • Kim, Kyoung-Sub (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)
  • 투고 : 2011.01.10
  • 심사 : 2011.02.11
  • 발행 : 2011.02.28

초록

To identify and examine the distribution of proteolytic inhibitory activity in crude extracts from fish eggs, and to determine the applicability of these protease inhibitors as anti-degradation agents in surimi-based products and fish meat, we compared the inhibitory activities of various extracts from fish eggs to those of commercial proteases, such as trypsin and papain. We used the optimal conditions for the screening of trypsin activity: 30 ug/uL of 0.1% trypsin and 0.6 mM Na-benzoyl-L-arginine-p-nitroanilide (BAPNA) with a pH of 8.0 at $40^{\circ}C$ for 60 min. The activities of papain and four commercial proteases were investigated after mixing with 100 ug/uL enzymes and 0.3% casein with a pH of 8.0 at $40^{\circ}C$ for 60 min. We performed a screening assay to detect the inhibitory activity (%) of crude extracts from eight species of fish eggs against the target proteases trypsin and papain. The assay revealed a wide distribution of trypsin and papain inhibitors in fish eggs. The specific inhibitory activities (11.6.28.6 U/mg) of crude extracts from fish eggs against trypsin and BAPNA substrate were higher than that (0.64 U/mg) of egg whites, used as a commercial inhibitor. The inhibitory activities of crude extracts from fish eggs against trypsin, and of egg whites against casein substrate (1.94.4.51 U/mg), were higher than those of papain (0.24.1.57 U/mg) and commercial protease (0.04.0.32 U/mg). The extracts from fish eggs were rich in protease inhibitors that exhibited strong inhibitory activity against trypsin, a serine protease, and papain, a cysteine protease.

키워드

참고문헌

  1. Angelova L, Dalgalarrondo M, Kinkov I, Danova A, Kirilov N, Serkedjieva J, Chobert J, Haertle T and Ivanova I. 2006. Purification and characterization of a protease inhibitor from Streptomyces chromofuscus 34-1 with antiviral activity. Biochem Biophys Acta 1760, 1210-1216. https://doi.org/10.1016/j.bbagen.2006.03.002
  2. Anson ML. 1938. The estimation of pepsin, trypsin, papain and cathepsin with hemoglobin. J Physiol 22,79-89.
  3. Birk Y. 1994. Protein proteinase inhibitors in legume seeds. Arch Am Nutr 44, 26-30
  4. Bjrek L, Akesson P, Bohus M, Trojnar J, OLafson M and Grubb A. 1989. Bacterial growth blocked by synthetic peptide based on the structure of a human proteinase inhibitor. Nature 337, 385-386. https://doi.org/10.1038/337385a0
  5. Borla OO, Martone CB and Sanchez JJ. 1998. Protease I inhibitor system in fish muscle: A comparative study. Comp Biochem Physiol B 119, 101-105. https://doi.org/10.1016/S0305-0491(97)00282-4
  6. Cao M, Osatomi K, Matsuda R, Ohkubo M, Hara K and Ishihara T. Purification and a novel serine proteinase inhibitor from the skeletal muscle of white croaker (Argyrosomus argentatus). Biochem Biophys Res Comm 272, 485-489. https://doi.org/10.1006/bbrc.2000.2803
  7. Choi JH, Park PJ and Kim SK. 2002. Purification and characterization of a trypsin inhibitor from the egg of skipjack tuna Katsuwonus pelamis. Fish Sci 68, 1367-1373. https://doi.org/10.1046/j.1444-2906.2002.00576.x
  8. Clereszko A, Kwasnik M, Dabrowski K, Poros B and Glogowski J. 2000. Chromatographic separation of trypsin-inhibitory activity of rainbow trout blood and deminal plasma. Fish Shellfish Immunol 10, 91-94. https://doi.org/10.1006/fsim.1999.0223
  9. Dixon M and Webb EC. 1979. Enzymes; enzyme inhibition and activation. 3rd ed. Longman Group Ltd., London, U.K., 332-381.
  10. Ee KY, Zhao J, Rehman A and Agboola S. 2008. Characterization of trypsin and a-chymotrypsin inhibitors in Austrailian wattle seed (Acacia victoriae Bentham). Food Chem 107, 337-343. https://doi.org/10.1016/j.foodchem.2007.08.025
  11. Erlanger BF, Kokowsky N and Cohen W. 1961. The preparation and properties of two new chromogenic substrates of trypsin. Arch Biochem Biophys 95, 271-278. https://doi.org/10.1016/0003-9861(61)90145-X
  12. Erlanger BF, Edel F and Cooper AG. 1966. The action of chymotrypsin on two new chromogenic substrates. Arch Biochem Biophys 155, 206-210.
  13. Eguchi M. 1993. Protein protease inhibitors in insects and comparison with mammalian inhibitors. Comp Biochem Physiol B 105, 449-456. https://doi.org/10.1016/0300-9629(93)90417-3
  14. Hamann DD, Amato PM, Wu MC and Foegeding EA. 1990. Inhibition of modiri (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
  15. Hara K and Ishimura T. 1987. Purification and characterization of serine proteinase inhibitor from carp Cyprinus carpio ordinary muscle. Agric Biol Chem 51 153-159. https://doi.org/10.1271/bbb1961.51.153
  16. Hara K, Nakaoka H, Nosaki Y, Tabata Y and Ishihara T. 1985. Purification and characterization of serine proteinase inhibitor from white croaker Argyrosomus argentatus ordinary muscle. Bull Jap Soc Sci Fish 51, 1029-1036. https://doi.org/10.2331/suisan.51.1029
  17. Heu MS and Ahn SH. 1999. Development and fractionation of proteolytic enzymes from inedible seafood product. J Kor Fish Soc 32, 458-465.
  18. 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
  19. Kim KY, Ustadi K and Kim SM. 2006. Characteristics of the protease inhibitor purified from chum salmon (Oncorhynchus keta) eggs. Food Sci Biotechnol 15,28-32.
  20. Laskowski M and Kato I. 1980. Protein inhibitors of proteinases. Ann Rev Biochem 49, 593-626.
  21. Nagashima Y, Takeda M, Ohta I, Shimakura K and Shiomi K. 2004. Purification and properties of proteinaceous trypsin inhibitors in the skin mucus of pufferfish Takifugu pardalis. Comp Biochem Physiol B 138, 103-110. https://doi.org/10.1016/j.cbpc.2004.03.001
  22. Lenney CJ. 1979. Thermostable endogenous inhibitors of cathepsins B and H. Eur J Biochem 101, 153-161. https://doi.org/10.1111/j.1432-1033.1979.tb04227.x
  23. Lowry OH, Rosebrough NJ, Farr AL and Randall RJ. 1951. Protein measurement with Folin phenol reagent. J Biol Chem 193, 256-275.
  24. Martone CB, Busconi L, Folco E and Sanchez JJ. 1991. Detection of a trypsin-like serine protease and its endogenous inhibitor in hake skeletal muscle. Arch Biochem Biophys 289, 1-5. https://doi.org/10.1016/0003-9861(91)90433-J
  25. 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
  26. Nonaka J. 1976. Suisanchokuhinkaku. SeaFood Goseisagogoseigaku, Tokyo, Japan, 56-60.
  27. Oda S, Igarashi Y, Manaka KI, Koibuchi N, Sakai-Sawada M, Sakai M, Morisawa M, Otake H and Shimizu N. 1998. Sperm-activaring 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
  28. Olenen A, Kalkkinen N and Paulin L. 2003. A new type of cysteine proteinase inhibitor the salrin gene from Atlantic salmon (Salmo salar L) and Arctic charr (Salvelinus alpinus). Biochemie 1, 1-5.
  29. Potempa J, Korzus E and Travis J. 1994. The seprin superfamily of proteinase inhibitors; structure, function, and regulation. J Biol Chem 269, 15957.
  30. Rawlings ND. 2004. Evolutionary families of peptidase inhibitors Biochem J 378, 705-716. https://doi.org/10.1042/BJ20031825
  31. Richardson M. 1990. Seed storage proteins: the enzyme inhibitors. In Methods in plant Biochemistry, Amino Acid, Proteins and Nucleic Acids, Vol. 5. Rogers L J. (eds). Academic Press, New York, U.S.A., 259-305.
  32. Ritonja A, Machleidt W and Barret AJ. 1985. Amino acid sequence of the intracellular cysteine protease inhibitor cystatin B from human liver. Biochem Biophys Res Commum 131, 1187-1192. https://doi.org/10.1016/0006-291X(85)90216-5
  33. Saitoh E, Isemura S, Chiba A, Oka S and Odani S. 2005. A novel cysteine protease inhibitor with lectin activity from the epidermis of the Japanese eel Anguilla japonica. Comp Biochem Physiol part B 141, 103-109. https://doi.org/10.1016/j.cbpc.2005.02.002
  34. Sangorrin MP, Folco EJ, Martone CM and Sanchez JJ. 2001. Purification and characterization of a protease inhibitor from white croaker skeletal muscle (Micropogon opercularis). Intl J Biochem Cell Biol 33, 691-699. https://doi.org/10.1016/S1357-2725(01)00054-1
  35. Sen LJ and Whitaker JR. 1973. Some properties of a ficin-papain inhibitor from avian egg white. Arch Biochem Biophys 158, 623-632. https://doi.org/10.1016/0003-9861(73)90554-7
  36. Synnes M. 1998. Purification and characterization of two cysteine proteinase inhibitors from the skin of Atlantic salmon (Salmo salar L.). Comp Biochem Physiol B 121, 257-264.
  37. Toyohara H, Makinodan Y and Ikeda S. 1988. Detection of a cysteine protease inhibitor in carp muscle. Nippon Suisan Gakkaishi 54, 157-163. https://doi.org/10.2331/suisan.54.157
  38. 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
  39. Ustadi K, Kim KY and Kim SM. 2005a. Characteristics of protease inhibitor purified from the eggs of Alaska pollock (Theragra chalcogramma). J Kor Fish Soc 38, 83-88. https://doi.org/10.5657/kfas.2005.38.2.083
  40. Ustadi K, Kim Y and Kim SM. 2005b. Purification and identification of a protease inhibitor from glassfish (Liparis tankai) eggs. J Agric Food Chem 53, 7667-7672. https://doi.org/10.1021/jf0482459
  41. Ustadi K, You SG and Kim SM. 2006. Purification, characterization and inhibitory activity of glassfish (Liparis tankai) egg high molecular weight inhibitor against papain and cathepsin. J Micorbiol Biotechnol 16, 524-530.
  42. Weder JKP. 1985. Chemistry of legume protease inhibitors and their use in taxonomy. Qual Plant Foods Hum Nutr 35, 183-195. https://doi.org/10.1007/BF01092194
  43. Yamashita M and Konagaya S. 1990. High activities of cathepsin B, D, H and L in the white muscle of chum salmon in spawning migration. Comp Biochem Physiol B 95, 149-152. https://doi.org/10.1016/0300-9629(90)90024-M
  44. Yamashita M and Konagaya S. 1991a. A comparison of cystatin activity in various tissues of chum salmon (Oncorhynchus keta) between feeding and spawning migrations. Comp Biochem Physiol A 100, 749-751. https://doi.org/10.1016/0300-9629(91)90402-X
  45. Yamashita M and Konagaya S. 1991b. Cysteine protease inhibitor in egg of chum salmon. J Biochem 110, 762-766. https://doi.org/10.1093/oxfordjournals.jbchem.a123655
  46. Ylonen A, Rinne A, Herttuainen J, Bogwald J, Jarvinen M and Kalkkinen N. 1999. Atlantic salmon (Salmo salar L.) skin contains a novel kininogen and another cystein proteinase inhibitor. Eur J Biochem 266, 1066-1072. https://doi.org/10.1046/j.1432-1327.1999.00950.x

피인용 문헌

  1. Fractionation and Characterization of Protease Inhibitors from Fish Eggs Based on Protein Solubility vol.46, pp.2, 2013, https://doi.org/10.5657/KFAS.2013.0119
  2. Chromatographic Fractionation of Protease Inhibitors from Fish Eggs vol.46, pp.4, 2013, https://doi.org/10.5657/KFAS.2013.0351