A DNA encoding fibrinolytic enzyme(FE) was amplified from Bacillus sp.nov SK006 using PCR.Sequencing showed open reading frame is composed of 828 bp encoding a putative protein of 276 amino acid residues.The cDNA was cloned into an expression vector pET-22b(+) and expressed in Escherichia coli BL21(DE3).The recombinant protein was purified to electrophoretical homogeneity by affinity chromatography using Chelating Sepharose Fast Flow resin.The purified recombinant FE had an approximate molecular weight of 28 ku by SDS-PAGE analysis.