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KMID : 0545120010110050845
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Journal of Microbiology and Biotechnology
2001 Volume.11 No. 5 p.845 ~ p.852
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Purification and Characterization of a Fibrinolytic Enzyme from Bacillus sp. KDO-13 Isolated from Soybean Paste
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Lee, Si Kyung
Bae, Dong Ho/Kwon, Tae Jong/Lee, Soo Bok/Lee, Hyung Hoan/Park, Jong Hyun/Heo, Seok
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Abstract
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A microorganism producing fibrinolytic enzyme was isolated from Korean traditional soybean paste and identified as Bacillus sp. KDO-13. The fibrinolytic enzyme was purified to homogeneity by ammonium sulfate fractionation, ion-exchange chromatography on DEAE-celluose, and gel chromatography on Sephadex G-100 of the culture supernatant of Bacillus sp. KDO-13. The molecular weight of the purified enzyme was estimated to be 44,000 by SDS-PAGE. The optimum pH and temperature for the enzyme activity were pH 8.0 and 50℃, respectively. The enzyme activity was relatively stable at pH 7.0-9.0 and temperature below 50℃. The activity of the enzyme was inhibited by Al^3+ and Hg^2+, but activated by Co^2+ and Ni^2+. In addition, the enzyme activity was potently inhibited by EDTA and ο-phenanthroline. The purified enzyme could completely hydrolyze a fibrin substrate within 6 h in vitro, and had a low K_m value for fibrin hydrolysis. It was concluded that the purified enzyme was a metalloprotease with relatively high specificity for fibrinolysis, and thus, could be applied as an effective thrombolytic agent.
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