Open AccessBacillus tequilensis Isolated from Fermented Intestine of Holothuria Scabra Produces Fibrinolytic Protease with Thrombolysis Activity
Author(s) -
Nur Hidayati,
Nurrahman Nurrahman,
Hayatun Fuad,
Hendra Munandar,
Dewi Seswita Zilda,
Aditya Rahman Ernanto,
Amin Samiasih,
Oedjijono Oedjijono,
Stalis Norma Ethica
Publication year - 2021
Publication title -
iop conference series. earth and environmental science
Language(s) - English
Resource type - Journals
eISSN - 1755-1307
pISSN - 1755-1315
DOI - 10.1088/1755-1315/707/1/012008
Subject(s) - protease , proteases , microbiology and biotechnology , biology , fibrinolytic agent , fibrinolysis , nattokinase , thrombolysis , biochemistry , fermentation , enzyme , food science , tissue plasminogen activator , medicine , myocardial infarction
Among essential treatment of cardiovascular disorders are fibrinolytic proteases. Most thrombolysis agents are fibrinolytic enzymes from group of bacterial proteases. This work reports a potent bacterium isolated from fermented intestine of H. scabra , which could produce fibrinolytic protease with high thrombolysis activity. Bacterial selection was conducted based on proteolytic and fibrinolytic activities indicated as clear zone on skim milk and fibrin agar media, respectively. Crude proteases from the selected bacterial isolates were subjected to thrombolytic activity test based on gravimetric method, which results were confirmed after 7 repetitions. As result, 4 fibrinolytic protease-producing bacterial isolates HFSI-3, HFSI-4, HFSI-5 and HFSI-8 were obtained. Among them, HFSI-5 isolate identified as Bacillus tequilensis on the basis of the 16S rRNA gene sequencing and morphological properties produced crude protease with the highest thrombolytic activity. The thrombolytic activity of crude protease produced by B. tequilensis HFSI-5 is worthy of comparing to that of standard fibrinolytic enzyme Nattokinase showing its potential as thrombolysis agent.