Microbiology and Biotechnology Letters (한국미생물·생명공학회지)

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Purification and Characterization of a Fibrinolytic Enzyme Produced by Bacillus sp. S19 from Shrimp

새우젓 유래 Bacillus sp. S19가 생산하는 혈전용해 요소의 정제 및 특성

  • 장순애 (충남대학교 식품영양학과) ;
  • 김명희 (생명공학연구소 환경생물소재연구실) ;
  • 이명선 (충남대학교 식품영양학과) ;
  • 오태광 (생명공학연구소 환경생물소재연구실) ;
  • 손천배 (충남대학교 식품영양학과)
  • Published : 2000.10.01
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Abstract

A fibrinolytic enzyme was purified to homogeneity from Bacillus sp. S19 using DEAE and CM column chromatograhies, and gel filtration with a recovery yield of 13%. Its molecular mass was estimated to be 42 kDa by SDS-PAGE. The pH and temperature optima were 8.0 and $40^{\circ}C$, respectively. The enzyme was stable up to $45^{\circ}C$ and over a pH range of 6-9. The N-terminal amino acid sequence of the enzyme was determined as Alsa-Gln-Asp-Ala-Thr-Val-Asn-Ile-Ser-Ala-Glu-Arg-Gln-Val-Ile. The fibrinolytic activity was increased by $Cu^{2+}$ while it was strongly inhibited by metal ions such as $Cd^{2+}$ and $Ba^{2+}$ . In addition, the enzyme was inhibited by EDTA, but not by PMSF, suggesting that it is a metallorprotease.

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References

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