Purification and Characterization of a Novel Fibrinolytic Enzyme from Marine Bacterium Bacillus sp. S-3685 Isolated from the South China Sea

文献类型： 外文期刊

第一作者： Ma, Zibin

作者： Ma, Zibin;Elango, Jeevithan;Wu, Wenhui;Elango, Jeevithan;Elango, Jeevithan;Hao, Jianhua

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关键词： fibrinolytic enzyme; Bacillus sp.; purification; optimum activity; thrombolysis

期刊名称：MARINE DRUGS （ 影响因子：4.9； 五年影响因子：5.2 ）

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年卷期： 2024 年 22 卷 6 期

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收录情况： SCI

摘要： A novel fibrinolytic enzyme, BSFE1, was isolated from the marine bacterium Bacillus sp. S-3685 (GenBank No.: KJ023685) found in the South China Sea. This enzyme, with a molecular weight of approximately 42 kDa and a specific activity of 736.4 U/mg, exhibited its highest activity at 37 degrees C in a phosphate buffer at pH 8.0. The fibrinolytic enzyme remained stable over a pH range of 7.5 to 10.0 and retained about 76% of its activity after being incubated at 37 degrees C for 2 h. The K-m and V-max values of the enzyme at 37 degrees C were determined to be 2.1 mu M and 49.0 mu mol min(-1) mg(-1), respectively. The fibrinolytic activity of BSFE1 was enhanced by Na+, Ba2+, K+, Co2+, Mn2+, Al3+, and Cu2+, while it was inhibited by Fe3+, Ca2+, Mg2+, Zn2+, and Fe2+. These findings indicate that the fibrinolytic enzyme isolated in this study exhibits a strong affinity for fibrin. Moreover, the enzyme we have purified demonstrates thrombolytic enzymatic activity. These characteristics make BSFE1 a promising candidate for thrombolytic therapy. In conclusion, the results obtained from this study suggest that our work holds potential in the development of agents for thrombolytic treatment.

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