Evidence that multiple proteases of Bacillus subtilis can degrade fibrin and fibrinogen.

Fibrinolytic enzyme produced by Bacillus spp. are known to possess an unique property to \ndegrade fibrin blood clots. Fibrinolytic enzyme such as nattokinase has commercial applications \nas a therapeutic agents and functional food formulation. In this study, we report an interesting \ncharacteristic feature of Bacillus subtilis BR21, a native isolate for its ability to produce multiple \nproteases that exclusively acts on fibrin and fibrinogen. The crude enzyme preparation was \nmade from the culture grown in soybean powder supplemented Luria Bertani broth. The culture \nfiltrate was found to contain proteases, that could collectively degrade fibrin and fibrinogen \neffectively. Zymogram indicated presence of six fibrinolytic proteases and these degraded all \nthe four peptide chains of fibrin rapidly. However, only Aα, Bβ chains of fibrinogen were highly \nsusceptible to the enzymes. Activity inhibition by PMSF and EDTA indicated the presence of \nserine and metallo proteases. Fibrinolytic and fibrinogenolytic activities, specifically the ability \nto degrade γ-γ′ dimer of fibrin, promises its potential as both therapeutic and prophylactic \nagents, for thrombosis related disorders as this remains undegraded in such conditions. The \nfibrinolytic ability of multiple proteases together may help in developing cheaper and effective \norally administrable thrombolytic preparations.