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Abstract：
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 °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 °C for 2 h. The Km and Vmax values of the enzyme at 37 °C were determined to be 2.1 μM and 49.0 μmol 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.
摘要：
一种新型纤溶酶,BSFE1是从海洋细菌芽孢杆菌属中分离出来的。S-3685(GenBank编号：KJ023685）在南中国海发现。这种酶，分子量约为42kDa，比活性为736.4U/mg，在pH8.0的磷酸盐缓冲液中，在37°C时表现出最高的活性。纤溶酶在7.5至10.0的pH范围内保持稳定，并在37°C孵育2小时后保留了约76％的活性。该酶在37°C下的Km和Vmax值分别为2.1μM和49.0μmolmin-1mg-1。Na+增强了BSFE1的纤溶活性,Ba2+,K+,Co2+,Mn2+,Al3+,和Cu2+，虽然它被Fe3+抑制，Ca2+,Mg2+,Zn2+,和Fe2+。这些发现表明，本研究中分离的纤溶酶对纤维蛋白具有很强的亲和力。此外，我们纯化的酶显示出溶血栓酶活性。这些特征使BSFE1成为溶栓治疗的有希望的候选药物。总之,从这项研究中获得的结果表明，我们的工作在开发溶栓治疗药物方面具有潜力。
