A novel fibrinolytic protease from Streptomyces sp. CS684

Simkhada, Jaya Ram; Mander, Poonam; Cho, Seung‐Sik; Yoo, Jin Cheol

doi:10.1016/j.procbio.2009.08.010

Cited by 93 publications

(51 citation statements)

References 25 publications

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“…The activity and stability of Streptomyces sp. CS684 fibrinolytic enzyme showed shear activity loss in acidic and basic environment (Simkhada et al 2010). In contrast, fibrinolytic proteases from B. subtilis A26 (Agrebi et al 2009) and B. amyloliquefaciens An6 (Agrebi et al 2010) showed stability over a broad range of acidic and alkaline pH.…”

Section: Discussionmentioning

confidence: 93%

“…Similarly, fibrinolytic enzymes from B. amyloliquefaciens An6 (Agrebi et al 2010) and Streptomyces sp. CS684 (Simkhada et al 2010) have been reported to be inhibited by EDTA.…”

Section: Discussionmentioning

confidence: 99%

“…Thrombosis, manifested in the form of embolism, myocardial infarction, stroke and other cardiac disorders is one of the major causes of CVDs (Mahajan et al 2012). Under pathophysiological disorders, dynamic balance between the formation and degradation of fibrin is disturbed, leading to accumulation of fibrin causing thrombosis (Simkhada et al 2010). Therapy for the treatment of acute thrombosis requires intravenous administration of highly specific fibrinolytic agents, which target the preformed fibrin clot hydrolysing the thrombus and restoring the blood flow to the area of ischemia.…”

Section: Introductionmentioning

confidence: 99%

“…Therapy for the treatment of acute thrombosis requires intravenous administration of highly specific fibrinolytic agents, which target the preformed fibrin clot hydrolysing the thrombus and restoring the blood flow to the area of ischemia. Although various fibrinolytic agents such as tissue plasminogen activator (t-PA, EC 3.4.21.68), urokinase 3.4.21.73), and bacterial plasminogen activator streptokinase (EC 3.4.24.29) are being extensively investigated (Simkhada et al 2010) and used widely but most of these thrombolytic agents have got serious limitations such as low fibrin specificity, excessively expensive cost of clinical applications, short half-life, and undesired side effects such as gastrointestinal bleeding, resistance to repercussion and allergic reactions (Mahajan et al 2012). Therefore, search for novel thrombolytic agents which are safer, costeffective and more efficient is in progress.…”

Section: Introductionmentioning

confidence: 99%

“…Most of the studies on fibrinolytic proteases involved purification and characterization of enzymes (Mahajan et al 2012) with relatively a fewer reports on optimization of enzyme production (Mukherjee and Rai 2011). Literature shows that studies on fungal fibrinolytic proteases have been more emphasized than bacterial ones (Simkhada et al 2010). Biochemical and physiological diversity of bacteria may enhance the scope of targeting better fibrinolytic proteases for potential therapeutic applications.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Optimization of fibrinolytic protease production from Bacillus subtilis I-2 using agro-residues

Bajaj¹,

Singh²,

Khullar³

et al. 2014

Braz. arch. biol. technol.

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show abstract

Section: Discussionmentioning

confidence: 93%

“…Similarly, fibrinolytic enzymes from B. amyloliquefaciens An6 (Agrebi et al 2010) and Streptomyces sp. CS684 (Simkhada et al 2010) have been reported to be inhibited by EDTA.…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Optimization of fibrinolytic protease production from Bacillus subtilis I-2 using agro-residues

Bajaj¹,

Singh²,

Khullar³

et al. 2014

Braz. arch. biol. technol.

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The biotechnological potential of fibrinolytic enzymes in the dissolution of endogenous blood thrombi

Kotb

2014

Biotechnology Progress

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Formation of endogenous thrombi in blood vessels is one of the leading causes of death in our modern life. According to data provided by the World Health Organization (WHO) in 2000, heart diseases are responsible for 29% of the total mortality rate in the world. For this, a tremendous amount of research has been done in the area of prevention and treatment of these diseases. The classical therapy of these thrombi relies upon the use of antiplatelets, anticoagulants, or even surgeries. Relatively recently, the fibrinolytic enzymes produced by microorganisms, snakes, earthworms, insects, plants, and other organisms are being successfully used in the treatment of blood clots, especially with regard to the direct dissolving action on fibrin in tandem with less cost and side effects in comparison with the first-generation thrombolytic agents, streptokinase and urokinase. Furthermore, recombinant DNA technology has succeeded in improving and decreasing the undesirable effects of the first generation of enzymes. Recombinant PAs or rt-PAs like alteplase, retelase, saruplase, tenecteplase, lanoteplase, and desmoteplase became available in the drug markets with advantages of less binding loci with PAI-1 to avoid degradation while providing faster and more complete reperfusion in a greater number of patients with less risk of bleeding and intracranial hemorrhage. This review is the first to cover all the natural and recombinant thrombolytic agents used in enzyme therapy.

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Screening and characterization of protease producing actinomycetes from marine saltern

Suthindhiran

Jayasri

Dipali

et al. 2013

J. Basic Microbiol.

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In the course of systematic screening program for bioactive actinomycetes, an alkaline protease producing halophilic strain Actinopolyspora sp. VITSDK2 was isolated from marine saltern, Southern India. The strain was identified as Actinopolyspora based on its phenotypic and phylogenetic characters. The protease was partially purified using ammonium sulfate precipitation and subsequently by DEAE cellulose column chromatography. The enzyme was further purified using HPLC and the molecular weight was found to be 22 kDa as determined by SDS-PAGE analysis. The purified protease exhibited pH stability in a wide range of 4-12 with optimum at 10.0. The enzyme was found to be stable between 25 and 80 °C and displayed a maximum activity at 60 °C. The enzyme activity was increased marginally in presence of Mn(2+) , Mg(2+) , and Ca(2+) and decreased in presence of Cu(2+) . PMSF and DFP completely inhibited the activity suggesting it belongs to serine protease. Further, the proteolytic activity was abolished in presence of N-tosyl-L-lysine chloromethyl ketone suggesting this might be chymotrypsin-like serine protease. The protease was 96% active when kept for 10 days at room temperature. The results indicate that the enzyme belong to chymotrypsin-like serine protease exhibiting both pH and thermostability, which can be used for various applications in industries.

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A novel fibrinolytic protease from Streptomyces sp. CS684

Cited by 93 publications

References 25 publications

Optimization of fibrinolytic protease production from Bacillus subtilis I-2 using agro-residues

Optimization of fibrinolytic protease production from Bacillus subtilis I-2 using agro-residues

The biotechnological potential of fibrinolytic enzymes in the dissolution of endogenous blood thrombi

Screening and characterization of protease producing actinomycetes from marine saltern

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