Article3 Biotech2017
Production, purification and characterization of fibrinolytic enzyme from Serratia sp. KG-2-1 using optimized media.
Article in 3 Biotech, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- Enhanced fibrinolytic enzyme production by Oidiodendron maius through green bioprocessing of agro-industrial residue.PloS one · 2026Article
- Novel thrombolytic protease from the rare halophile Brachybacterium paraconglomeratum: bioprocessing and in vitro application.BMC biotechnology · 2025Article
- Characterization of Fibrinolytic Enzyme from Bacillus altitudinis S-CSR 0020 and Its Clot-Degrading Capacity.Current microbiology · 2025Article
- Exploring the fibrinolytic potential of marine Actinoalloteichus caeruleus isolated from Bay of Bengal coast.BMC microbiology · 2025Article
- Purification and Characterization of a Novel Fibrinolytic Enzyme from Marine BacteriumMarine drugs · 2024Article
- Review
- Fibrin and Fibrinolytic Enzyme Cascade in Thrombosis: Unravelling the Role.Life (Basel, Switzerland) · 2023Review
- Research progress on the fibrinolytic enzymes produced from traditional fermented foods.Food science & nutrition · 2023Review
- Purification and proteomic analysis of potent fibrinolytic enzymes extracted from Lumbricus rubellus.Proteome science · 2023Article
- Development of a microbial protease for composting swine carcasses, optimization of its production and elucidation of its catalytic hydrolysis mechanism.BMC biotechnology · 2022Article
- Marine Microbial Fibrinolytic Enzymes: An Overview of Source, Production, Biochemical Properties and Thrombolytic Activity.Marine drugs · 2022Review
- Microbial Fibrinolytic Enzymes as Anti-Thrombotics: Production, Characterisation and Prodigious Biopharmaceutical Applications.Pharmaceutics · 2021Review
- Isolation, Extraction, Purification, and Characterization of Fibrinolytic Enzyme fromArchives of Razi Institute · 2021Article
- Thrombolytic Enzymes of Microbial Origin: A Review.International journal of molecular sciences · 2021Review
- Article
- Role of Fibrinolytic Enzymes in Anti-Thrombosis Therapy.Frontiers in molecular biosciences · 2021Review
- An effective combination of codon optimization, gene dosage, and process optimization for high-level production of fibrinolytic enzyme in Komagataella phaffii (Pichia pastoris).BMC biotechnology · 2020Article
- Thrombolytic Potential of Novel Thiol-Dependent Fibrinolytic Protease from Bacillus cereus RSA1.Biomolecules · 2019Article
- Enhanced production of recombinant serratiopeptidase in Escherichia coli and its characterization as a potential biosimilar to native biotherapeutic counterpart.Microbial cell factories · 2019Article
- Computational modeling of culture media for enhanced production of fibrinolytic enzyme from marine bacterium3 Biotech · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intravascular thrombosis is one of the major causes of variety of cardiovascular disorders leading to high mortality worldwide. Fibrinolytic enzymes from microbial sources possess ability to dissolve these clots and help to circumvent these problems in more efficient and safer way. In the present study, fibrinolytic protease with higher fibrinolytic activity than plasmin was obtained from Serratia sp. KG-2-1 isolated from garbage dump soil. Response surface methodology was used to study the interactive effect of concentration of maltose, yeast extract + peptone (1:1), incubation time, and pH on enzyme production and biomass. Maximum enzyme production was achieved at 33 °C after 24 h at neutral pH in media containing 1.5% Maltose, 4.0% yeast extract + peptone and other trace elements resulting in 1.82 folds increased production. The enzyme was purified from crude extract using ammonium sulfate precipitation and DEAE-Sephadex chromatography resulting in 12.9 fold purification with 14.9% yield. The purified enzyme belongs to metalloprotease class and had optimal activity in conditions similar to physiological environment with temperature optima of 40 °C and pH optima of 8. The enzyme was found to be stable in various solvents and its activity was enhanced in presence of Na
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