Preparation and properties of fibrinolytic enzymes produced by Cochliobolus lunatus

Abstract

Some properties of the crude lyophilized fibrinolytic enzyme produced by Cochliobolus lunatus in surface culture were studied. Enzyme concentrations over the range from 0.16 to 10.16 mg/mL showed that concentration above a certain level ceased to be the limiting factor controlling enzyme action. At pH 6.8 and a temperature of 40 degrees C, the fibrinolytic enzyme showed maximal activity at a human fibrin concentration of 2 mg/mL. The optimum pH values for enzyme activity were 6.98 and 7.0, using Sørensen and Mcllvaine buffers, respectively. Fibrinolytic enzymes were isolated from a static culture of Cochliobolus lunatus; isolation was carried out with various agents. Ammonium sulphate yielded the highest recovered fibrinolytic activity. The fraction salted out by precipitation at 25% ammonium sulphate saturation possessed the highest recovered fibrinolytic activity compared to the ammonium sulphate, ethanol, and acetone fractions.

Thrombolytic and anticoagulant efficiencies of purified fibrinolytic enzyme produced from Cochliobolus hawaiiensis under solid‐state fermentation

“…So, numerous fungi were examined for their ability to produce fibrinases. Similar results were obtained by Abdel‐Fattah and Ismail 11 who recorded that C. lunatus was the potent fungus for fibrinolytic enzyme production.…”

“…Maximum activity of purified C. hawaiiensis fibrinolytic enzyme was recorded at a great activity at temperature range 33-41 • C with a maximum at 37 • C (Figure 2C). Our results were in complete accordance with that recorded maximal fibrinolytic activity at temperature range (37-40 • C) for Aspergillus ustus, 45 C. lunatus, 11 and R. microspores. 16 Meanwhile, a higher optimum temperature for fibrinolytic activity was also recorded at 49 • C from Neurospora sitophila.…”

“…10 Less fibrinolytic strains of filamentous fungi have been mentioned in literature. Fibrinolytic enzymes were previously extracted from Aspergillus brasiliensis, 10 Cochliobolus lunatus, 11 Fusarium pallidoroseum, 12 Fusarium sp., 13 Oidiodendron flavum, 14 Penicillium chrysogenum, 15 and Rhizopus microspores. 16 In addition, fibrinolytic enzymes are macromolecular substances that lose their activity after prolonged storage.…”

Novel Inhibitors of Trihydroxynaphthalene Reductase with Antifungal Activity Identified by Ligand-Based and Structure-Based Virtual Screening

“…Dematiaceous, or dark pigmented fungi, contain melanins in their cell walls that protect them against environmental stress and enable their survival under extreme conditions. , In addition, melanization is associated with fungal virulence and pathogenicity, and it reduces fungal susceptibility to host defense mechanisms and enables plant pathogenic species to enter into plant tissue. − The wide variety of plant and/or human pathogenic dematiceous fungi synthesize their melanins from 1,8-dihydroxynaphthalene (DHN)-melanin via the pentaketide pathway. , As the synthesis of DHN-melanin does not occur in host organisms, enzymes participating in this biosynthetic pathway represent emerging targets for the development of selective fungicides and antimycotics. One of the enzymes involved in DHN-melanin biosynthesis is trihydroxynaphthalene reductase (3HNR), which reduces 1,3,8-trihydroxynaphthalene to vermelone . Recently, we cloned, overexpressed, and purified 3HNR from C. lunata and identified its first inhibitors by biochemical screening. − …”

“…One of the enzymes involved in DHN-melanin biosynthesis is trihydroxynaphthalene reductase (3HNR), which reduces 1,3,8-trihydroxynaphthalene to vermelone. 19 Recently, we cloned, overexpressed, and purified 3HNR from C. lunata and identified its first inhibitors by biochemical screening. 20À22 To date, only a few inhibitors of 3HNR are known.…”