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

• Published in: Marine drugs Vol. 22; no. 6; p. 267
• Main Authors: Ma, Zibin, Elango, Jeevithan, Hao, Jianhua, Wu, Wenhui
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 10.06.2024; MDPI
• Subjects: Aluminum; Aquatic Organisms; Bacillus; Bacillus - enzymology; Bacillus sp; Bacteria; Bats; Calcium ions; Carbon dioxide; Care and treatment; China; Chromatography; Cobalt; Complications and side effects; Enzymatic activity; Enzyme activity; Enzymes; Fibrin; Fibrin - metabolism; Fibrinolytic Agents - chemistry; Fibrinolytic Agents - isolation & purification; Fibrinolytic Agents - pharmacology; fibrinolytic enzyme; Health aspects; Heart attack; Hydrogen-Ion Concentration; Magnesium; Marine bacteria; Microorganisms; Molecular Weight; Oceans and Seas; optimum activity; Phosphates; Prevention; Proteins; purification; Risk factors; Temperature; Thrombolysis; Thrombosis; Venous thrombosis; Water purification; Zinc; China; South China Sea; thrombolysis; fibrinolytic enzyme; optimum activity; Bacillus sp; purification
• ISSN: 1660-3397; 1660-3397
• DOI: 10.3390/md22060267

A novel fibrinolytic enzyme, BSFE1, was isolated from the marine bacterium 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 K and V values of the enzyme at 37 °C were determined to be 2.1 μM and 49.0 μmol min mg , respectively. The fibrinolytic activity of BSFE1 was enhanced by Na , Ba , K , Co , Mn , Al , and Cu , while it was inhibited by Fe , Ca , Mg , Zn , and Fe . 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.