한국수산과학회지 (Korean Journal of Fisheries and Aquatic Sciences)

  • 제38권2호
  • /
  • Pages.83-88
  • /
  • 2005
  • /
  • 0374-8111(pISSN)
  • /
  • 2287-8815(eISSN)
한국수산과학회 (The Korean Society of Fisheries and Aquatic Science)
권호 표지
DOI QR코드

DOI QR Code

명란 단백분해효소 저해제의 특성

Characteristics of Protease Inhibitor Purified from the Eggs of Alaska pollock (Theragra chalcogramma)

  • USTADI (가자마다대학 수산학과) ;
  • 김근영 (강릉대학교 해양생명공학부) ;
  • 김상무 (강릉대학교 해양생명공학부)
  • STADI U (Department of Fisheries, Faculty of Agriculture, Gadjah Mada University) ;
  • KIM Keun Yeong (Faculty of Marine Bioscience & Technology, Kangnung National University) ;
  • KIM Sang Moo (Faculty of Marine Bioscience & Technology, Kangnung National University)
  • 발행 : 2005.04.01
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

Protease inhibitors were purified from the eggs of Alaska pollock (Theragra chalcogramma) using the following purification steps: ammonium sulfate precipitation, ion exchange, gel permeation, and high performance liquid chromatographies (HPLC). The protease inhibitor from the heated eggs of Alaska pollock was not as well purified. In addition, the heated eggs showed lower specific inhibitory activity than the unheated eggs. The purification yields after ammonium sulfate precipitation, ion exchange, and gel permeation chromatographies were 22.7$\%,\;15.3\%$,and $4.4\%$, respectively. There were two kinds of protease inhibitors on the gel permeation chromatography pattern Their molecular weights were estimated to be 66,700 and 16,000 Da, respectively. Both were classified as a cysteine protease inhibitor because of the existence of inhibiting papain, which is one of cysteine proteases.

키워드

참고문헌

  1. Abe, K., H. Kondo, Y. Emori, K. Suzuki and S. Arai. 1987. Molecular cloning of a cysteine proteinase inhibitor of rice (Oryzacystatin), homology with animal cystatins and transient expression in the ripening process of rice seed. J. Biol. Chem., 262, 16793-16797
  2. An, H., M.Y. Peters and T.A. Seymour. 1996. Roles of endogenous enzymes in surimi gelation. J. Food Sci., 7, 321-326
  3. An, H., V. Weerasinghe, T.A. Seymour and M.T. Morrissey. 1994. Cathepsin degradation of Pacific whiting surimi proteins. J. Food Sci., 59, 1013-1017, 1033 https://doi.org/10.1111/j.1365-2621.1994.tb08179.x
  4. Barrett, A.J. 1981. Cystatin, the egg white inhibitor of cysteine proteinases, Meth. Enzymol., 80, 771-777 https://doi.org/10.1016/S0076-6879(81)80059-6
  5. Barrett, A.J. 1986. Cysteine protease inhibitors of the cystatin superfamily In: Proteinase Inhibitors. Rawlings, N.D., M.E. Davies, W. Macleidt, G. Salvesen and V. Turk, Elsevier, Amesterdam, pp. 515-569
  6. Borla, O.O., C.B. Martone and J.J. Sanchez. 1998. Protease I inhibitor system in fish muscle: A comparative study. Comp. Biochem. Physiol., 119B, 101-105
  7. Boye, S.W. and T.C. Lanier. 1988. Effect of heat-stable alkaline protease activity of Atlantic menhaden (Brevoorti tyrannus) on surimi gels. J. Food Sci., 53, 1340-1342, 1398 https://doi.org/10.1111/j.1365-2621.1988.tb09272.x
  8. Bradford, M.M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 71, 248-254
  9. Cha, Y.J. and E.H, Lee. 1990. Studied on the processing of rapid fermented anchovy prepared with low salt contents by adapted microorganism. 2. Themodynamic charaterizations of microbial extracellular protease isolated from fermented fish paste. J. Korean Agric. Chem. Soc. 33, 325-329
  10. Kawabata, C. and E. Ichishima. 1997. Miltpain, new cystsine protenase from the milt of Chum salmon, Oncorhynchus keta. Comp. Biochem. Physiol., 117B, 445-452
  11. Kenney, A.J. 1999. Nomenclature and classes of peptidase. In: Proteolytic Enzymes. Sterchi, E.E. and W. Stocker eds. Springer Lab Manual, New York, pp. 1-8
  12. Laemmli, U.K. 1970. Cleavage of structure protein during the assembly of the head bacteriophage. Nature, 227, 265-275 https://doi.org/10.1038/227265a0
  13. Pandhare, J., K. Zog and V.V. Deshpande. 2002. Differential stabilities of alkaline protease inhibitor from actinomycetes: effect of various additives on thermostability. Biores. Technol., 84, 165-169 https://doi.org/10.1016/S0960-8524(02)00025-1
  14. Saeki, H., Z. Iseya, S. Sugiura and N. Seki. 1995. Gel forming characteristics of frozen surimi from Chum salmon in the presence inhibitors. J. Food Sci., 60, 917-922 https://doi.org/10.1111/j.1365-2621.1995.tb06261.x
  15. Synnes, M. 1998. Purification and characterization of two cysteine proteinase inhibitors from skin of Atlantic salmon (Salmo Salar L.). Comp. Biochem. Physiol., Part B, 121, 257-264
  16. Tsai, V.J., G.D. Chang, C.J. Huang, Y.S. Chang and F.L. Huand. 1996. Purification and molecular cloning of carp ovarian cystatin. Comp. Biochem., 113B, 573-580
  17. Visessanguan, W., S. Benjakul and H. An. 2003. Purification and characterization of cathepsin L in arrow-tooth flounder (Atheresthes stomias) muscle. Comp. Bioch. Physiol., 134, 477-487 https://doi.org/10.1016/S1096-4959(02)00293-2
  18. Weerasinghe, V.C., M.T. Morrissey and H. An. 1996. Characterization of active Components in food grade proteinase inhibitor for surimi manufacture. J. Food Chem., 44, 2584-2590 https://doi.org/10.1021/jf950589z
  19. Welling, G.W. 1989. Size exclusion HPLC of protein: a practical approach. 2nd ed. In: HPLC of macromolecules, Oliver R.W.A. and S.W. Wester. University Press, Oxford, England, pp. 77-89
  20. Yamashita, M. and S. Konagaya. 1991. Cysteine protease inhibitor in egg of Chum salmon. J. Biochem., 110, 762-766 https://doi.org/10.1093/oxfordjournals.jbchem.a123655
  21. Yamashita, M. and S. Konagaya. 1996. Molcular cloning and gene expression of Chum salmon cystatin. J. Biochem., 120, 483-487 https://doi.org/10.1093/oxfordjournals.jbchem.a021438

피인용 문헌

  1. Chromatographic Fractionation of Protease Inhibitors from Fish Eggs vol.46, pp.4, 2013, https://doi.org/10.5657/KFAS.2013.0351
  2. Recovery of serine protease inhibitor from fish roes by polyethylene glycol precipitation vol.19, pp.1, 2016, https://doi.org/10.1186/s41240-016-0016-x
  3. 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
  4. Distribution of Protease Inhibitors from Fish Eggs as Seafood Processing Byproducts vol.44, pp.1, 2011, https://doi.org/10.5657/kfas.2011.44.1.008
  5. Alkaline protease inhibitor를 생산하는 해양유래 방선균의 탐색 및 동정 vol.18, pp.4, 2005, https://doi.org/10.5352/jls.2008.18.4.482