Microbiological Synthesis of Proteolytic Enzymes Possessing Fibrinolytic Activity

Егоров, Н.С.

doi:10.1007/978-1-4684-1659-6_8

Cited by 3 publications

(3 citation statements)

References 5 publications

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“…Some of the previous studies reported in fibrinolytic protease from actinomycetes includes Streptomyces spheroids M8 [15] and Actinomyces thermovulgaris [17]. The cloning and expression of the thermophilic Streptomyces actinokinase gene has also been reported [29].…”

Section: Resultsmentioning

confidence: 99%

Novel Fibrinolytic Protease Producing Streptomyces radiopugnans VITSD8 from Marine Sponges

Dhamodharan

Naine

et al. 2019

Marine Drugs

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Fibrinolytic enzymes have received more attention due to their medicinal potential for thrombolytic diseases. The aim of this study is to characterize the in vitro fibrinolytic nature of purified protease producing Streptomyces radiopugnans VITSD8 from marine brown tube sponges Agelas conifera. Three varieties of sponge were collected from the Rameshwaram Sea coast, Tamil Nadu, India. The fibrinolytic activity of Streptomyces sp. was screened and determined by casein plasminogen plate and fibrin plate methods respectively. The crude caseinolytic protease was purified using ammonium sulfate fractionation, affinity and ion-exchange chromatography. Based on the morphological, biochemical, and molecular characterization, the isolate VITSD8 was confirmed as Streptomyces radiopugnans. Maltose and peptone were found to be the best carbon and nitrogen sources for the production of fibrinolytic protease. The carbon and nitrogen source peptone showed (781 U/mL) enzyme activity. The optimum pH and temperature for fibrinolytic protease production was found to be 7.0 and 33 °C respectively. The purified enzyme showed a maximum specific activity of 3891 U. The blood clot lysis activity was compared with the standard, and it was concluded that a minimum of 0.18 U (10 µL) of purified protease was required to dissolve the blood clot. This is the first report which exploits the fibrinolytic protease activity of Streptomyces radiopugnans VITSD8 extracted from a marine sponge. Hence the investigation suggests a potential benefit of purified fibrinolytic protease which will serve as an excellent clot buster alternative.

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Section: Resultsmentioning

confidence: 99%

Novel Fibrinolytic Protease Producing Streptomyces radiopugnans VITSD8 from Marine Sponges

Dhamodharan

Naine

et al. 2019

Marine Drugs

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“…However, many thrombolytics that directly hydrolyze fibrin may cause severe adverse effects, such as hemorrhages and rethrombosis [3,4]. Enzymes that prevent the formation of a fibrin clot or mediate its lysis by activating plasminogen, the pre cursor of plasmin, a natural fibrinolytic enzyme of the hemostatic system, may be more promising [5,6]. Such enzymes can be produced by some micro mycetes, whose proteinases have a narrower substrate specificity than bacterial ones [6].…”

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confidence: 99%

“…The range and properties of proteinases produced by microscopic fungi vary considerably and depend not only on the taxonomic position of a particular organism, but also on the ecological group that they belong to [5,6]. Therefore, it is important to under stand the typical characteristics of enzymatic activity and substrate specificity of proteinases synthesized by micromycetes representing different ecological groups.…”

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confidence: 99%

Screening of producers of proteinases with fibrinolytic and collagenolytic activities among micromycetes

et al. 2015

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Screening for producers of proteinases with fibrinolytic (plasmin like and plasminogen activa ting) and collagenolytic activities was carried out among 83 strains of microscopic fungi belonging to various ecological groups. Entomopathogenic micromycetes secreted proteinases with higher fibrinolytic and col lagenolytic activity than saprotrophic, potentially phytopathogenic, and epiphytic strains. Micromycete strains possessing proteolytic enzymes with collagenase activity were revealed, as were the strains producing proteinases with plasmin like activity. None of the strains studied secreted proteinases possessing only plas minogen activating activity. Tolypocladium inflatum k1 was found to be a producer of extracellular proteinases with high plasminogen activating, plasmin like, and collagenolytic activities. The specific plasminogen activating activity of T. inflatum k1 was shown to be 20% higher than its plasmin like activity.Specific values of plasminogen activating (1) and plasmin like (2) fibrinolytic activity of T. inflatum k1.

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Fibrinolytic and collagenolytic activity of extracellular proteinases of the strains of micromycetes Aspergillus ochraceus L-1 and Aspergillus ustus 1

Osmolovskiy

Popova

Kreyer

et al. 2016

Moscow Univ. Biol.Sci. Bull.

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Microbiological Synthesis of Proteolytic Enzymes Possessing Fibrinolytic Activity

Cited by 3 publications

References 5 publications

Novel Fibrinolytic Protease Producing Streptomyces radiopugnans VITSD8 from Marine Sponges

Novel Fibrinolytic Protease Producing Streptomyces radiopugnans VITSD8 from Marine Sponges

Screening of producers of proteinases with fibrinolytic and collagenolytic activities among micromycetes

Fibrinolytic and collagenolytic activity of extracellular proteinases of the strains of micromycetes Aspergillus ochraceus L-1 and Aspergillus ustus 1

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