One of the main causes of heart-related problems globally is intravascular thrombosis. Microbial fibrinolytic proteases play a very crucial role in the management of thrombosis. Plasminogen activators and plasmin-like proteins, which are fibrinolytic enzymes of microbial origin, hydrolyze thrombin with great efficacy and without causing noticeable side effects. These fibrinolytic enzymes can also be manufactured efficiently and economically in huge quantities within a short period. However, the search for novel fibrinolytic enzymes demands difficult purification procedures, as well as physicochemical and structural-functional properties that provide information about their mode of action. In this study, the strain named Bacillus subtilis AIBL_AMSB2_M7E32, isolated from the Coringa mangrove soils, was shown to produce a fibrinolytic enzyme. The enzyme was purified by a four-step purification process that resulted in a 43.33-fold purification with a specific activity of 6368.20 (U/mg). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the purified enzyme was a protein of about 28 kDa and showed fibrinolytic activity on a zymogram. In vitro assay on blood clots revealed that the purified enzyme could lyse the blood effectively by a percentage of 72.96 ± 0.16a%, indicating that the enzyme could be used as a fibrinolytic agent. Furthermore, an observation for enzyme stability and its in vivo activity studies would be necessary for its application in the market.
Key words: Keywords: Bacillus subtilis AIBL_AMSB2_M7E32, Fibrinolytic enzymes, Intravascular thrombosis, In vitro activity, Purification.
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