Some properties of two purified fibrinolytic enzymes from <i>Bacillus subtilis</i> and <i>B. polymyxa</i>

Fayek, K. I.; El‐Sayed, Sanaa T.

doi:10.1002/jobm.19800200604

Cited by 3 publications

(2 citation statements)

References 7 publications

(2 reference statements)

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“…The fibrinolytic proteases isolated from the culture filtrates of Aspergillus fumigatus, 33 kDa [12], exactly correspond to the molecular mass of fibrinolytic protease purified from G. lucidum in this study. [15].…”

Section: Discussionmentioning

confidence: 99%

Purification of an Intracellular Fibrinolytic Protease from Ganoderma Lucidum Vk12 and its Susceptibility to Different Enzyme Inhibitors

Kumaran¹,

Palani²,

Nishanthi³

et al. 2011

Trop. J. Pharm Res

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Section: Discussionmentioning

confidence: 99%

Purification of an Intracellular Fibrinolytic Protease from Ganoderma Lucidum Vk12 and its Susceptibility to Different Enzyme Inhibitors

Kumaran¹,

Palani²,

Nishanthi³

et al. 2011

Trop. J. Pharm Res

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“…Hence, the search for the effective and safe thrombolytic agent from different biosources keeps growing worldwide. Study reports are available on fibrinolytic enzymes from various organisms, including Bacillus polymyxa [2], Escherichia coli [3], Pseudomonas [4], Streptomyces [5], Paenibacillus sp. IND8 [6], and Bacillus cereus IND1 [7].…”

Section: Introductionmentioning

confidence: 99%

Novel Sequential Screening and Enhanced Production of Fibrinolytic Enzyme byBacillussp. IND12 Using Response Surface Methodology in Solid-State Fermentation

Vijayaraghavan

Rajendran

Vincent

et al. 2017

BioMed Research International

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Fibrinolytic enzymes have wide applications in clinical and waste treatment. Bacterial isolates were screened for fibrinolytic enzyme producing ability by skimmed milk agar plate using bromocresol green dye, fibrin plate method, zymography analysis, and goat blood clot lysis. After these sequential screenings, Bacillus sp. IND12 was selected for fibrinolytic enzyme production. Bacillus sp. IND12 effectively used cow dung for its growth and enzyme production (687 ± 6.5 U/g substrate). Further, the optimum bioprocess parameters were found out for maximum fibrinolytic enzyme production using cow dung as a low cost substrate under solid-state fermentation. Two-level full-factorial experiments revealed that moisture, pH, sucrose, peptone, and MgSO4 were the vital parameters with statistical significance (p < 0.001). Three factors (moisture, sucrose, and MgSO4) were further studied through experiments of central composite rotational design and response surface methodology. Enzyme production of optimized medium showed 4143 ± 12.31 U/g material, which was more than fourfold the initial enzyme production (978 ± 36.4 U/g). The analysis of variance showed that the developed response surface model was highly significant (p < 0.001). The fibrinolytic enzyme digested goat blood clot (100%), chicken skin (83 ± 3.6%), egg white (100%), and bovine serum albumin (29 ± 4.9%).

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Thrombolytic Potential of Novel Thiol-Dependent Fibrinolytic Protease from Bacillus cereus RSA1

et al. 2019

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The present study demonstrates the production and thrombolytic potential of a novel thermostable thiol-dependent fibrinolytic protease by Bacillus cereus RSA1. Statistical optimization of different parameters was accomplished with Plackett-Burman design and validated further by central composite design with 30.75 U/mL protease production. Precipitation and chromatographic approaches resulted in 33.11% recovery with 2.32-fold purification. The molecular weight of fibrinolytic protease was 40 KDa and it exhibited a broad temperature and pH stability range of 20-80 • C and pH 5-10 with utmost activity at 50 • C and pH 8, respectively. The protease retained its fibrinolytic activity in organic solvents and enhanced the activity in solutions with divalent cations (Mn 2+ , Zn 2+ , and Cu 2+ ). The enzyme kinetics revealed K m and V max values of 1.093 mg/mL and 52.39 µg/mL/min, respectively, indicating higher affinity of fibrinolytic activity towards fibrin. Also, complete inhibition of fibrinolytic activity with DFP and a 2-fold increase with DTT and β-mercaptoethanol indicates its thiol-dependent serine protease nature. MALDI-TOF analysis showed 56% amino acid sequence homology with Subtilisin NAT OS = Bacillus subtilis subsp. natto. The fibrinolysis activity was compared with a commercial thrombolytic agent for its therapeutic applicability, and fibrinolytic protease was found highly significant with absolute blood clot dissolution within 4 h in in vitro conditions. The isolated fibrinolytic protease of Bacillus cereus RSA1 is novel and different from other known fibrinolytic proteases with high stability and efficacy, which might have wide medicinal and industrial application as a thrombolytic agent and in blood stain removal, respectively.Biomolecules 2020, 10, 3 2 of 23 (active protease), converting soluble fibrinogen (glycoprotein) into fibrin polymer (insoluble blood clot) [5]. Fibrin clots are hydrolyzed by plasmin [12], which is stimulated from plasminogen by plasminogen activators (PAs) [13,14]. This natural dynamic equilibrium is disturbed when the process of natural fibrin clot hydrolysis undergoes pathophysiological shambles, leading to formation of fibrin clots. Such clots may cause hindrance in the circulation of blood, causing blockage in blood vessels, ultimately leading to cardiac disorders which are life-threatening [15,16].Approaches such as use of anti-coagulant agents, anti-platelet drugs, fibrinolytic enzymes, and surgical operations are employed for the treatment of thrombosis and to dissolve the blood clots [17]. Further, there are numerous side effects which may occur following the administration of the available anti-thrombotic strategies, as well as the high expense, which limit their scope. The effects of reperfusion, urticaria (allergic reaction), and hemorrhage are the major inimical consequences of such thrombolytic approaches on human health [18,19]. Other after effects include headache, dizziness, ulcers, increased clotting time, nausea and vomiting, etc. Management of thrombosis usin...

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Some properties of two purified fibrinolytic enzymes from Bacillus subtilis and B. polymyxa

Cited by 3 publications

References 7 publications

Purification of an Intracellular Fibrinolytic Protease from Ganoderma Lucidum Vk12 and its Susceptibility to Different Enzyme Inhibitors

Purification of an Intracellular Fibrinolytic Protease from Ganoderma Lucidum Vk12 and its Susceptibility to Different Enzyme Inhibitors

Novel Sequential Screening and Enhanced Production of Fibrinolytic Enzyme byBacillussp. IND12 Using Response Surface Methodology in Solid-State Fermentation

Thrombolytic Potential of Novel Thiol-Dependent Fibrinolytic Protease from Bacillus cereus RSA1

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