A novel serine protease from B. Hansen: Characterization and fibrino(geno)lytic activities.

Protease () was isolated from B. Hansen and had a molecular mass of 70 kDa. The N-terminal sequence of showed 70-80% similarity with of subtilisin-like serine proteases from plants, but it did not show any sequence homology with known plant proteases. Serine protease inhibitors (PMSF, DFP) effectively blocked about 90% of activity. was highly activity at the pH range from 6 to 9 and temperatures from 50 °C to 80 °C, with an optimum at pH 7.0 and temperatures 70 °C. had stability in a variety of pH, temperature, surfactant and oxidizing agents. with concentration of 2.5 µg completely hydrolyzed the Aα-chain of fibrinogen within 5 min and hydrolyzed the Bβ and the γ-chain after 10 h. Fibrin also was strong hydrolyzed by with concentration of 0.3 µg. Thus, is a unique serine protease, which it had strong fibrino(geno)lytic activities.