Abstract
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.
Highlights
As per a WHO report, about 17 million individuals are supposed to die due to cardiovascular infections
This is the first report which exploits the fibrinolytic protease activity of Streptomyces radiopugnans VITSD8 extracted from a marine sponge
Folin–Ciocalteau reagent, potassium dihydrogen phosphate, trichloroacetic acid (TCA), hydrochloric acid (HCl), ethylene-diaminetetraacetic acid (EDTA), and Tris-HCl were purchased from Sisco research laboratories (SRL, Mumbai, India)
Summary
As per a WHO report, about 17 million individuals are supposed to die due to cardiovascular infections. The frequency of the intense myocardial localized necrosis is increasing around the world [1]. Thrombus develops inside arteries, leading to thrombosis, heart stroke, and pulmonary embolism [2]. Thrombolytic treatments have become a traditional remedy regarding acute myocardial infarction (AMI). Synthetic therapeutics used in such disorders has serious adverse effects, so there is a need to investigate new and safe natural thrombolytic agents [3]. Protein treatments are turning out to be more pervasive in present day solutions for AMI. Since a wide source is available, microbial fibrinolytic enzymes have attracted a great deal of therapeutic enthusiasm during the last decade [4]
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