Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Articles Article Faculty Publications -Articles Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Purification and evaluating in vitro activity of a fibrinolytic protease produced by a mangrove isolate Bacillus subtilis AIBL_AMSB2_M7E32 Subject The topic of the resource Bacillus subtilis AIBL_AMSB2_M7E32; Fibrinolytic enzymes; In vitro activity; Intravascular thrombosis; Purification Description An account of the resource 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. 2024 Bhavana Sompalli and Alok Malaviya. Creator An entity primarily responsible for making the resource Sompalli B.; Malaviya A. Source A related resource from which the described resource is derived Journal of Applied Biology and Biotechnology, Vol-12, No. 5, pp. 237-242. Publisher An entity responsible for making the resource available Open Science Publishers LLP Inc. Date A point or period of time associated with an event in the lifecycle of the resource 2024-01-01 Identifier An unambiguous reference to the resource within a given context <a href="https://doi.org/10.7324/JABB.2024.175220" target="_blank" rel="noreferrer noopener">https://doi.org/10.7324/JABB.2024.175220</a> <br /><br /><a href="https://www.scopus.com/inward/record.uri?eid=2-s2.0-85200682422&amp;doi=10.7324%2FJABB.2024.175220&amp;partnerID=40&amp;md5=03118cb98c0a7ab1e2dc4b23b8719a5e" target="_blank" rel="noreferrer noopener">https://www.scopus.com/inward/record.uri?eid=2-s2.0-85200682422&amp;doi=10.7324%2fJABB.2024.175220&amp;partnerID=40&amp;md5=03118cb98c0a7ab1e2dc4b23b8719a5e</a> Rights Information about rights held in and over the resource All Open Access; Gold Open Access Relation A related resource ISSN: 2347212X Format The file format, physical medium, or dimensions of the resource Online Language A language of the resource English Type The nature or genre of the resource Article Coverage The spatial or temporal topic of the resource, the spatial applicability of the resource, or the jurisdiction under which the resource is relevant Sompalli B., Applied and Industrial Biotechnology Laboratory, CHRIST (Deemed-to-be University), Karnataka, Bangalore, India; Malaviya A., Department of Life Sciences, CHRIST (Deemed-to-be University), Karnataka, Bangalore, India