%0 Journal Article %A Narasimhan, Manoj Kumar %A Ethiraj, Selvarajan %A Krishnamurthi, Tamilarasan %A Rajesh, Mathur %D 2018 %T Purification, biochemical, and thermal properties of fibrinolytic enzyme secreted by Bacillus cereus SRM-001 %U https://tandf.figshare.com/articles/journal_contribution/Purification_biochemical_and_thermal_properties_of_fibrinolytic_enzyme_secreted_by_i_Bacillus_cereus_i_SRM-001/5573518 %R 10.6084/m9.figshare.5573518.v2 %2 https://ndownloader.figshare.com/files/9686899 %K Bacillus cereus %K biochemical properties %K fibrinolytic enzyme %K serine protease %K thermal properties %X

The discovery of microbial fibrinolytic enzymes is essential to treat cardiovascular diseases. This study reports the discovery of a fibrinolytic enzyme secreted by Bacillus cereus SRM-001, a microorganism isolated from the soil of a chicken waste-dump yard. The B. cereus SRM-001 was cultured and the secreted fibrinolytic enzyme purified to show that it is a ∼28 kDa protein. The purified enzyme was characterized for its kinetics, biochemical and thermal properties to show that it possesses properties similar to plasmin. A HPLC-MS/MS analysis of trypsin digested protein indicated that the fibrinolytic enzyme shared close sequence homology with serine proteases reported for other Bacillus sp. The results show that the B. cereus SRM-001 secreted enzyme is a ∼28 kDa serine protease that possesses fibrinolytic potential.

%I Taylor & Francis