- Detection of a Unique Fibrinolytic Enzyme in Aeromonas sp. JH1
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Han-Young Cho , Min Jeong Seo , Jeong Uck Park , Byoung Won Kang , Gi-Young Kim , Woo Hong Joo , Young-Choon Lee , Yong Kee Jeong
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J. Microbiol. 2011;49(6):1018-1021. Published online December 28, 2011
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DOI: https://doi.org/10.1007/s12275-011-1376-7
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A fibrinolytic enzyme was found in a Gram-negative bacterium, Aeromonas sp. JH1. SDS-PAGE and fibrinzymography showed that it was a 36 kDa, monomeric protein. Of note, the enzyme was highly specific for fibrinogen molecules and the hydrolysis rate of fibrinogen subunits was highest for α, β, and γ chains in that order. The first 15 amino acids of N-terminal sequence were X-D-A-T-G-P-G-G-N-V-X-T-G-K-Y, which was distinguishable from other fibrinolytic enzymes. The optimum pH and temperature of the enzyme were approximately 8.0 and 40°C, respectively. Therefore, these results provide a fibrinolytic enzyme with potent thrombolytic activity from the Aeromonas genus.
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Citations
Citations to this article as recorded by  - Purification and Characterization of a Fibrinolytic Enzyme from Marine Bacillus velezensis Z01 and Assessment of Its Therapeutic Efficacy In Vivo
Yuting Zhou, Huizhen Chen, Bo Yu, Guiguang Chen, Zhiqun Liang
Microorganisms.2022; 10(5): 843. CrossRef - Biochemical characteristics of a fibrinolytic enzyme purified from a marine bacterium, Bacillus subtilis HQS-3
Shihai Huang, Shihan Pan, Guiguang Chen, Shan Huang, Zhaofeng Zhang, Yan Li, Zhiqun Liang
International Journal of Biological Macromolecules.2013; 62: 124. CrossRef
- Biochemical Analysis of a Fibrinolytic Enzyme Purified from Bacillus subtilis Strain A1
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Won Sik Yeo , Min Jeong Seo , Min Jeong Kim , Hye Hyeon Lee , Byoung Won Kang , Jeong Uck Park , Yung Hyun Choi , Yong Kee Jeong
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J. Microbiol. 2011;49(3):376-380. Published online June 30, 2011
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DOI: https://doi.org/10.1007/s12275-011-1165-3
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A fibrinolytic enzyme from Bacillus subtilis strain A1 was purified by chromatographic methods, including DEAE Sephadex A-50 column chromatography and Sephadex G-50 column gel filtration. The purified enzyme consisted of a monomeric subunit and was estimated to be approximately 28 kDa in size by SDS-PAGE. The specific activity of the fibrinolytic enzyme was 1632-fold higher than that of the crude enzyme extract. The fibrinolytic activity of the purified enzyme was approximately 0.62 and 1.33 U/ml in plasminogen-free and plasminogen-rich fibrin plates, respectively. Protease inhibitors PMSF, DIFP, chymostatin, and TPCK reduced the fibrinolytic activity of the enzyme to 13.7, 35.7, 15.7, and 23.3%, respectively. This result suggests that the enzyme purified from B. subtilis strain A1 was a chymotrypsin-like serine protease. In addition, the optimum temperature and pH range of the fibrinolytic enzyme were 50°C and 6.0-10.0, respectively. The N-terminal amino acid sequence of the purified enzyme was identified as Q-T-G-G-S-I-I-D-P-I-N-G-Y-N, which was highly distinguished from other known fibrinolytic enzymes. Thus, these results suggest a fibrinolytic enzyme as a novel thrombolytic agent from B. subtilis strain A1.
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Citations
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Noora Barzkar
3 Biotech.2026;[Epub] CrossRef - Proteases, a powerful biochemical tool in the service of medicine, clinical and pharmaceutical
Ghadir A. Jamal, Ehsan Jahangirian, Michael R. Hamblin, Hamed Mirzaei, Hossein Tarrahimofrad, Neda Alikowsarzadeh
Preparative Biochemistry & Biotechnology.2025; 55(1): 1. CrossRef - Fibrin and Fibrinolytic Enzyme Cascade in Thrombosis: Unravelling the Role
Rajni Singh, Prerna Gautam, Chhavi Sharma, Alexander Osmolovskiy
Life.2023; 13(11): 2196. CrossRef - Microbial Fibrinolytic Enzymes as Anti-Thrombotics: Production, Characterisation and Prodigious Biopharmaceutical Applications
Chhavi Sharma, Alexander Osmolovskiy, Rajni Singh
Pharmaceutics.2021; 13(11): 1880. CrossRef - Marine microbial alkaline protease: An efficient and essential tool for various industrial applications
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International Journal of Biological Macromolecules.2020; 161: 1216. CrossRef - Potential application spectrum of microbial proteases for clean and green industrial production
Satbir Singh, Bijender Kumar Bajaj
Energy, Ecology and Environment.2017; 2(6): 370. CrossRef - Purification, biochemical, and structural characterization of a novel fibrinolytic enzyme from Mucor subtilissimus UCP 1262
Thiago Pajeú Nascimento, Amanda Emmanuelle Sales, Tatiana Souza Porto, Romero Marcos Pedrosa Brandão Costa, Leonid Breydo, Vladimir N. Uversky, Ana Lúcia Figueiredo Porto, Attilio Converti
Bioprocess and Biosystems Engineering.2017; 40(8): 1209. CrossRef - A novel Ca2+-dependent alkaline serine-protease (Bvsp) from Bacillus sp. with high fibrinolytic activity
Qipeng Cheng, Fangyan Xu, Nan Hu, Xiaoshuang Liu, Ziduo Liu
Journal of Molecular Catalysis B: Enzymatic.2015; 117: 69. CrossRef - EnterohemorrhagicEscherichia coliOmpT regulates outer membrane vesicle biogenesis
Veena Premjani, Derek Tilley, Samantha Gruenheid, Hervé Le Moual, John A. Samis
FEMS Microbiology Letters.2014; 355(2): 185. CrossRef
- Initial Acidic pH Is Critical for Mycelial Cultures and Functional Exopolysaccharide Production of an Edible Mushroom, Laetiporus sulphureus var. miniatus JM 27
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Min Jeong Seo , Min Jeong Kim , Hye Hyeon Lee , Sung Ryeal Kim , Byoung Won Kang , Jeong Uck Park , En Ju Rhu , Yung Hyun Choi , Yong Kee Jeong
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J. Microbiol. 2010;48(6):881-884. Published online January 9, 2011
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DOI: https://doi.org/10.1007/s12275-010-0410-5
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704
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We conducted a time course experiment on mycelial cultures of Laetiporus sulphureus var. miniatus. The strain showed significant survival in an initial pH range of 2.0 to 7.0 for 24 days, during which time oxalic acid was accumulated. A structural analysis of purified exopolysaccharide suggested that it contained 96.1% glucose, and the mode of linkage was mainly-4-Glcp-(1-units, with branches at the C-6 position consisting of a Glcp-(1-4) linked side chain. An exopolysaccharide purified from the acidophilic strain was added to cultured U937 cells, resulting in significantly increased transcription levels of p53 and p21 genes.
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Jiaming He, Guangchong He, Han Wei, Deqi Liu, Yanling Zheng, Chunqiao Liu
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Journal of Food Composition and Analysis.2024; 134: 106508. CrossRef - Bioactive components of Laetiporus species and their pharmacological effects
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Journal of Microbiology.2015; 53(4): 272. CrossRef - Operating conditions optimization for (+)-terrein production in a stirred bioreactor by Aspergillus terreus strain PF-26 from marine sponge Phakellia fusca
Bailiang Xu, Ying Yin, Fengli Zhang, Zhiyong Li, Lianyun Wang
Bioprocess and Biosystems Engineering.2012; 35(9): 1651. CrossRef - pH-control modes in a 5-L stirred-tank bioreactor for cell biomass and exopolysaccharide production by Tremella fuciformis spore
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- Purification and Biochemical Characterization of a 17 kDa Fibrinolytic Enzyme from Schizophyllum commune
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In Suk Park , Jeong Uck Park , Min Jeong Seo , Min Jeong Kim , Hye Hyeon Lee , Sung Ryeal Kim , Byoung Won Kang , Yung Hyun Choi , Woo Hong Joo , Yong Kee Jeong
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J. Microbiol. 2010;48(6):836-841. Published online January 9, 2011
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DOI: https://doi.org/10.1007/s12275-010-0384-3
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834
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A fibrinolytic enzyme of the mushroom, Schizophyllum commune was purified with chromatographic methods, including a DEAE-Sephadex A-50 ion-exchange column and gel filtrations with Sephadex G-75 and Sephadex G-50 columns. The analysis of fibrin-zymography and SDS-PAGE showed that the enzyme was a monomeric subunit that was estimated to be approximately 17 kDa in size. The fibrinolytic activity of the enzyme in plasminogen-rich and plasminogen-free fibrin plates was 1.25 and 0.44 U/ml, respectively. The N-terminal amino acid sequence of the purified enzyme was identified as HYNIXNSWSSFID, which was highly distinguished from known fibrinolytic enzymes. The relative activity of the purified enzyme with an addition of 5 mM EDTA, Phosphoramidon, and Bestatin was about 76, 64, and 52%, respectively, indicating that it is a metalloprotease. The optimum temperature for the purified enzyme was approximately 45°C, and over 87% of the enzymatic activity was maintained as a stable state in a pH range from 4.0 to 6.0. Therefore, our results
suggest that the potential thrombolytic agent from S. commune is a unique type of fibrinolytic enzyme.
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