BMB Reports

Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
권호 표지
DOI QR코드

DOI QR Code

Purification and Characterization of a Collagenolytic Protease from the Filefish, Novoden modestrus

  • Kim, Se-Kwon (Department of Chemistry, Pukyong National University) ;
  • Park, Pyo-Jam (Department of Chemistry, Pukyong National University) ;
  • Kim, Jong-Bae (Department of Sea-Food Science and Technology, Kunsan National University) ;
  • Shahidi, Fereidoon (Memorial University of Newfoundland)
  • Published : 2002.03.31
Download PDF
⟨ Previous Next ⟩

Abstract

A serine collagenolytic protease was purified from the internal organs of filefish Novoden modestrus, by ammonium sulfate, ion-exchange chromatography on a DEAE-Sephadex A-50, ion-exchange rechromatography on a DEAE-Sephadex A-50, and gel filtration on a Sephadex G-150 column. The molecular mass of the filefish serine collagenase was estimated to be 27.0 kDa by gel filtration and SDS-PAGE. The purified collagenase was optimally active at pH 7.0-8.0 and $55^{\circ}C$. The purified enzyme was rich in Ala, Ser, Leu, and Ile, but poor in Trp, Pro, Tyr, and Met. In addition, the purified collagenolytic enzyme was strongly inhibited by N-P-toluenesulfonyl-L-lysine chloromethyl ketone (TLCK), diisopropylfluorophosphate (DFP), and soybean trypsin inhibitor.

Keywords

References

  1. Barthomoeuf, C., Pourrat, H. and Pourrat, A. (1992) Collagenolytic activity of a new semi-alkaline protease from Aspergillus niger. J. Ferment. Bioeng. 73, 233-236. https://doi.org/10.1016/0922-338X(92)90168-T
  2. Bjarnason, J. B. and Fox, J. W. (1994) Hemorrhagic metalloproteinases from snake venoms. Phannacol. Ther. 62, 325-372. https://doi.org/10.1016/0163-7258(94)90049-3
  3. Bond, J. S. and Butler, P. E. (1987) Intracellular proteases. Annu. Rev. Biochem. 56, 333-364. https://doi.org/10.1146/annurev.bi.56.070187.002001
  4. Bond, M. D. and Van Wart, H. E. (1984a) Characterization of the individual collagenases from Clostridium histolyticum. Biochemistry 23, 3085-3091. https://doi.org/10.1021/bi00308a036
  5. Bond, M. D. and Van Wart, H. E. (1984b) Purification and separation of individual collagenases of Clostridium histolyticum using red dye ligand chromatography. Biochemistry 23, 3077-3085. https://doi.org/10.1021/bi00308a035
  6. Cawston, T. E. and Murphy, G. (1981) Mammalian collagenases. Methods Enzymol. 80, 711-722. https://doi.org/10.1016/S0076-6879(81)80054-7
  7. Chen, Y. L., Lu, P. J. and Tsai, I. H. (1991) Collagenolytic activity of crustacean midgut serine proteases: comparison with the bacterial and mammalian enzymes. Comp. Biochem Physiol. 100B, 763-768.
  8. Eisen, A. Z., Henderson, K. O., Jeffrey, J. J. and Bradshaw, R. A.(1973) A collagenolytic protease from the hepatopancreas of the fiddler crab, Uca pugilator. Purification and properties. Biochemistry 12, 1814-1822. https://doi.org/10.1021/bi00733a024
  9. Gross, J. and Lapiere, C. M. (1962) Collagenolytic activity in amphibian tissues: a tissue culture assay. Proc. Natl. Acad. Sci. USA 48, 1014-1022. https://doi.org/10.1073/pnas.48.6.1014
  10. Harris, E. D. and Vater, C. A. (1982) Vertebrate collagenases. Methods Enzymol. 82, 423-452. https://doi.org/10.1016/0076-6879(82)82077-6
  11. Hugli, T. E. and Moore, S. (1972) Determination of the tryptophan content of proteins by ion exchange chromatography of alkaline hydrolysates. J. BioI. Chem. 247, 2828-2834.
  12. Hurion, N., Fromentin, H. and Keil B. (1979) Specificity of the collagenolytic enzyme from the fungus Entomophthora coronata: comparison with the bacterial collagenase from Achromobacter iophagus. Arch. Biochem. Biophys. 192, 438-445. https://doi.org/10.1016/0003-9861(79)90113-9
  13. Kim, Y. T. and Kim, S. K. (1991) Purification and characterization of the collagenase from the tissue of filefish, Novoden modestrus. Korean Biochem. J. 24,401-409.
  14. Kim, Y. T. and Kim, S. K. (1996) Purification and characterization of extracellular collagenase from Vibrio mimicus. Korean J. Life Sci. 6, 241-249.
  15. Klimova, O. A., Borukhov, S. I., Solovyeva, N. I., Balaevskaya, T. O. and Strongin, A. Y. (1990) The isolation and properties of collagenolytic proteases from crab hepatopancreas. Biochem. Biophys. Res. Comm. 166, 1411-1420. https://doi.org/10.1016/0006-291X(90)91024-M
  16. Krist jansson, M. M., Cudmundsdottir, S., Fox, J. W. and Bjarnason, J. B. (1995) Characterization of a collagenolytic serine proteinase from the Atlantic cod (Gadus morhua). Comp. Biochem. Physiol. 110B,707-717.
  17. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680- 685. https://doi.org/10.1038/227680a0
  18. Lecroisey, A., Boulard, C. and Keil, B. (1979) Chemical and enzymatic characterization of the collagenase from the insect Hypoderma lineatum. Eur. J. Biochem 101, 385-393. https://doi.org/10.1111/j.1432-1033.1979.tb19730.x
  19. Lecroisey, A. and Keil, B. (1985) Specificity of the collagenase from the insect Hypoderma lineatum. Eur. J. Biochem. 152, 123-130. https://doi.org/10.1111/j.1432-1033.1985.tb09171.x
  20. Lecroisey, A., Gilles, A. M., De Wolf, A. and Keil, B. (1987) Complete amino acid sequence of the collagenase from the insect Hypoderma lineatum. J. BioI. Chem. 262,7546-7551.
  21. Lowry, O. H., Rosebrough, A. L., Farr, A. L. and Randall, R. J. (1951) Protein measurement with the Folin-phenol reagent. J. Biol. Chem. 193, 165-175.
  22. Lu, P. J., Liu, H. C. and Tsai, I. H. (1990) The midgut trypsins of shrimp (Penaeus monodon). High efficiency toward native protein substrates including collagens. Biol. Chem. Hoppe-Seyler 371, 851-859. https://doi.org/10.1515/bchm3.1990.371.2.851
  23. Makinen, K. K. and Makinen, P. L. (1987) Purification and properties of an extracellular collagenolytic protease produced by the human oral bacterium Bacillus cereus (Strain Sco 67). J. Biol. Chem 262, 12488-12495.
  24. Matsuhita, O., Yoshibara, K., Katayama, S. I., Minami, J. and Okabe, A. (1994) Purification and characterization of a Clostridium perjringes 120 kilodalton collagenase and nucleotide sequence of the corresponding gene. J. Bacteriol. 176, 149-156. https://doi.org/10.1128/jb.176.1.149-156.1994
  25. Moore, S. and Stein, W. (1954) A modified ninhydrin reagent for the photometric detennination of amino acids and related compounds. J. Biol. Chem. 211, 907-913.
  26. Muramatsu, T. and Kariuchi, H. (1978) Proteolytic activity of extracts from the hepatopancreas of shrimp, ParahaUporus sibogae (De Man). Bull. Jap. Soc. Sci. Fish. 44,171-174. https://doi.org/10.2331/suisan.44.171
  27. Nagano, H. and To, K. A. (1999) Purification of collagenase and specificity of its related enzyme from Bacillus subtilis FS-2. Biosci. Biotechnol. Biochem. 63, 181-183.
  28. Neurath, H. (1984) Evolution of proteolytic enzymes. Science 224, 350-357. https://doi.org/10.1126/science.6369538
  29. Nguyen, T. T., Dumas, J. and Keil-Dlouha, V. (1988) New achromobacter collagenase and its immunological relationship with a vertebrate collagenase. Biochim Biophys. Acta 955, 43-49. https://doi.org/10.1016/0167-4838(88)90177-X
  30. Peterkofsky, B. (1982) Bacterial collagenase. Methods Enzymol. 82, 453-471. https://doi.org/10.1016/0076-6879(82)82078-8
  31. Roy, P., Colas, B. and Durand, P. (1996) Purification, kinetical and molecular characterizations of a serine collagenolytic protease from green shore crab (Carcinus maenas) digestive gland. Comp. Biochem. Physiol. 115B, 87-95.
  32. Sakharov, I. Y. and et Litvin, F. E. (1992) Substrate specificity of collagenolytic proteases from the hepatopancreas of the Kamchatka crab. Biochemistry (USSR) 57, 44-49.
  33. Sakharov, I. Y., Litvin, F. E. and Artyukov, A. A. (1992) Physicochemical properties of collagenolytic protease C of the Kamchatka crab. Biochemistry (USSR) 57, 28-32.
  34. Sellers, A. and Murphy, G. (1981) Collagenolytic enzymes and their naturally occurring inhibitors. Int. Rev. Connect. Tissue Res. 9, 151-190. https://doi.org/10.1016/B978-0-12-363709-3.50010-3
  35. Stricklin, G. P., Bauer, E. A., Jeffrey, J. J. and Eisen, A. Z. (1977) Human skin collagenase: isolation of precursor and active forms from both fibroblast and organ cultures. Biochemistry 16, 1607-1615. https://doi.org/10.1021/bi00627a013
  36. Takeuchi, H., Shibano, Y., Morhara, K., Fukushima, J., Inami, S., Keil, B., Gilles, A. M., Kawamoto, S. P. and Okuda, K. (1992) Structural gene and complete amino acid sequence of Vibrio alginolyticus collagnase. Biochem. J. 281, 703-708. https://doi.org/10.1042/bj2810703
  37. Turkiewicz, M., Galas, E. and Kalinowska, H. (1991) Collagenolytic serine proteinase from Euphasia superba Dana (Antarctic krill). Comp. Biochem. Physiol. 99B, 359-371.
  38. Van Wormhoudt, A., Le Chevalier, P. and Sellos, D. (1992) Purification, biochemical characterization and N-tenninal sequence of a serine-protease with chymotrypsic and collagenolytic activities in a tropical shrimp, Penaeus vannamei (Crustacea, Decapoda). Comp. Biochem. Physiol. 103B, 675-680.
  39. Yoshinaka, R., Sato, M., Itoko, M., Yamashita, M. and Ikeda, S. (1986) Purification and characterization of a collagenolytic serine proteinase from the catfish pancreas. J. Biochem. 99, 459-467. https://doi.org/10.1093/oxfordjournals.jbchem.a135500
  40. Yoshinaka, R., Sato, M., Yamashita, M., Itoko, M. and Ikeda, S. (1987) Specificity of the collagenolytic serine proteinase from the pancreas of the catfish (Parasilarus asotus). Comp. Biochem. Physiol. 88B, 557-561.

Cited by

  1. Purification and Biochemical Properties of Glutathione S-Transferase from Lactuca sativa vol.38, pp.2, 2005, https://doi.org/10.5483/BMBRep.2005.38.2.232
  2. Functional Annotation and Analysis of Expressed Sequence Tags from the Hepatopancreas of Mitten Crab (Eriocheir sinensis) vol.11, pp.3, 2009, https://doi.org/10.1007/s10126-008-9146-1
  3. Low molecular weight serine protease from the viscera of sardinelle (Sardinella aurita) with collagenolytic activity: Purification and characterisation vol.124, pp.3, 2011, https://doi.org/10.1016/j.foodchem.2010.06.096
  4. Effect of season and fishing ground on the activity of cathepsin B and collagenase in by-products from cod species vol.39, pp.1, 2006, https://doi.org/10.1016/j.lwt.2004.11.006
  5. Development of an in Vitro Assay for the Proteolytic Processing of the CDP/Cux Transcription Factor vol.36, pp.4, 2003, https://doi.org/10.5483/BMBRep.2003.36.4.390
  6. PURIFICATION AND CHARACTERIZATION OF A SERINE PROTEINASE FROM THE TUNA PYLORIC CAECA vol.26, pp.6, 2002, https://doi.org/10.1111/j.1745-4514.2002.tb00768.x
  7. Purification, Characterization, cDNA Cloning andIn VitroExpression of a Serine Proteinase from the Intestinal Tract of Sea Cucumber (Stichopus japonicus) with Collagen Degradation Activity vol.62, pp.20, 2014, https://doi.org/10.1021/jf500923y
  8. Characterization and Applicability of Digestive Proteinases from Hepatopancreas ofBarytelphusa cunicularis vol.25, pp.1, 2011, https://doi.org/10.1080/08905436.2011.547111
  9. Purification and Characterization of a Novel Collagenase from Bacillus pumilus Col-J vol.160, pp.1, 2010, https://doi.org/10.1007/s12010-009-8673-1
  10. Bacterial collagenases – A review 2014, https://doi.org/10.3109/1040841X.2014.904270
  11. Bioactive compounds from marine processing byproducts – A review vol.39, pp.4, 2006, https://doi.org/10.1016/j.foodres.2005.10.010