Purification, biochemical, and thermal properties of fibrinolytic enzyme secreted by Bacillus cereus SRM-001.

Prep Biochem Biotechnol

b Department of Chemical Engineering , School of Bioengineering, SRM University, Kattankulathur , Tamil Nadu , India.

Published: January 2018

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.

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Source
http://dx.doi.org/10.1080/10826068.2017.1387560DOI Listing

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