Fibrinolytic activity and molecular identification of PB-12 isolate from Papuma Coastal at Jember regency

Abstract

Background: Coastal areas have a high bacterial diversity, which can be used as a source of pharmaceutical substances, including the fibrinolytic enzyme. Fibrinolytic enzymes can lyse blood clots by degrading the fibrin. These enzymes are important for treating circulatory disorders, e.g., pulmonary embolism, deep vein thrombosis, and myocardial infarction. Objective: This study aimed to determine the fibrinolytic activity of crude protein extract and precipitate protein of fibrinolytic bacteria PB-12 isolated from Papuma coastal, Jember district, Indonesia. Method: The molecular weight of fibrinolytic enzymes was determined by fibrin zymography, while 16s rDNA sequencing was performed to identify the PB-12 isolate. Result: The fibrinolytic activity result showed CPE at 24 hours had the highest fibrinolytic activity with a lysis diameter of 5.23 ± 0.68 mm. The fibrinolytic activity of this bacterium was contributed with ~114 kDa protein. PB-12 was identified as Bacillus aryabhattai based on 16S rRNA gene sequence. Conclusion: This is the first to report Bacillus aryabhattai as a potential fibrinolytic enzyme producer.