Least hemolytic, 12.6 kDa, plasmin-like fibrinolytic protease from marine Penicillium steckii KU1.
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| Format: | Artículo científico |
| Language: | en |
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International journal of biological macromolecules
2024
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| author | Kunhiraman, Swapna Haridas, Madhathilkovilakathu Basheer, Soorej M Chellappan, Sreeja Abdulhameed, Sabu |
| author_facet | Kunhiraman, Swapna Haridas, Madhathilkovilakathu Basheer, Soorej M Chellappan, Sreeja Abdulhameed, Sabu Kunhiraman, Swapna Haridas, Madhathilkovilakathu Basheer, Soorej M Chellappan, Sreeja Abdulhameed, Sabu |
| collection | PubMed - marine biology |
| contents | Least hemolytic, 12.6 kDa, plasmin-like fibrinolytic protease from marine Penicillium steckii KU1. Kunhiraman, Swapna Haridas, Madhathilkovilakathu Basheer, Soorej M Chellappan, Sreeja Abdulhameed, Sabu Penicillium Fibrinolysin Hydrogen-Ion Concentration Hemolysis Molecular Weight Kinetics Fibrinolytic Agents Temperature Aquatic Organisms Animals Substrate Specificity A novel fibrinolytic enzyme, from the marine fungus Penicillium steckii KU1, was purified to electrophoretic homogeneity. The fibrinolytic protease was purified to 13.56 times with a specific activity of 57.64 U/mg and final yield of 13.93 %. It was found to be a monomeric protein of 12.6 kDa, having optimum activity at 30 °C and pH 8.0. It is a plasmin-like enzyme, showing resemblance to ATP-dependent zinc metalloprotease with isoelectric point (pI) 8.0. Its activity is enhanced by Zn, and inhibited by ethylenediaminetetraacetic acid (EDTA), Co and Fe. The enzyme interaction with substrate azocasein was endothermic and with inhibitor EDTA exothermic. The K, V, K and catalytic efficiency of the enzyme for azocasein were determined to be 142.71 μg mL, 285.71 μg min mL, 6.35 S and 4.45 × 10 S μg mL respectively. It hydrolyzed all three chains of fibrinogen within 9 h, and dissolved fibrin completely within 24 h. 2 mg/mL enzyme could dissolve blood clot completely within 30 min, with negligible hemolysis (2.60 %). Lowering the immunogenicity by the application of natural or engineered small proteins is a strategy to enhance the safety and efficacy of thrombolytic therapy. Hence, the present 12.6 kDa, plasmin-like fibrinolytic enzyme appears worthy of further investigations towards a thrombolytic therapeutic. |
| format | Artículo científico |
| id | pubmed_39571871 |
| institution | PubMed |
| language | en |
| publishDate | 2024 |
| publisher | International journal of biological macromolecules |
| record_format | pubmed |
| spellingShingle | Least hemolytic, 12.6 kDa, plasmin-like fibrinolytic protease from marine Penicillium steckii KU1. Kunhiraman, Swapna Haridas, Madhathilkovilakathu Basheer, Soorej M Chellappan, Sreeja Abdulhameed, Sabu Penicillium Fibrinolysin Hydrogen-Ion Concentration Hemolysis Molecular Weight Kinetics Fibrinolytic Agents Temperature Aquatic Organisms Animals Substrate Specificity Least hemolytic, 12.6 kDa, plasmin-like fibrinolytic protease from marine Penicillium steckii KU1. Kunhiraman, Swapna Haridas, Madhathilkovilakathu Basheer, Soorej M Chellappan, Sreeja Abdulhameed, Sabu Penicillium Fibrinolysin Hydrogen-Ion Concentration Hemolysis Molecular Weight Kinetics Fibrinolytic Agents Temperature Aquatic Organisms Animals Substrate Specificity A novel fibrinolytic enzyme, from the marine fungus Penicillium steckii KU1, was purified to electrophoretic homogeneity. The fibrinolytic protease was purified to 13.56 times with a specific activity of 57.64 U/mg and final yield of 13.93 %. It was found to be a monomeric protein of 12.6 kDa, having optimum activity at 30 °C and pH 8.0. It is a plasmin-like enzyme, showing resemblance to ATP-dependent zinc metalloprotease with isoelectric point (pI) 8.0. Its activity is enhanced by Zn, and inhibited by ethylenediaminetetraacetic acid (EDTA), Co and Fe. The enzyme interaction with substrate azocasein was endothermic and with inhibitor EDTA exothermic. The K, V, K and catalytic efficiency of the enzyme for azocasein were determined to be 142.71 μg mL, 285.71 μg min mL, 6.35 S and 4.45 × 10 S μg mL respectively. It hydrolyzed all three chains of fibrinogen within 9 h, and dissolved fibrin completely within 24 h. 2 mg/mL enzyme could dissolve blood clot completely within 30 min, with negligible hemolysis (2.60 %). Lowering the immunogenicity by the application of natural or engineered small proteins is a strategy to enhance the safety and efficacy of thrombolytic therapy. Hence, the present 12.6 kDa, plasmin-like fibrinolytic enzyme appears worthy of further investigations towards a thrombolytic therapeutic. |
| title | Least hemolytic, 12.6 kDa, plasmin-like fibrinolytic protease from marine Penicillium steckii KU1. |
| topic | Penicillium Fibrinolysin Hydrogen-Ion Concentration Hemolysis Molecular Weight Kinetics Fibrinolytic Agents Temperature Aquatic Organisms Animals Substrate Specificity |
| url | https://pubmed.ncbi.nlm.nih.gov/39571871/ |