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In this paper, we investigate the characterization and evaluation of the antifungal protease activity from a halotolerant strain M3-16 ofBacillus pumilus, earlier isolated from a shallow salt lake in Tunisia. Protease enzyme was highly induced by the pathogen testedin vitro (27.4 U/ml). This is the first report on high salt-tolerant protease fromB. Pumilus, since it was active at high salinity (from 5 to 30% NaCl, w/v) as well as in the absence of salinity. This enzyme showed optimal activity at 60 °C and pH 8. At 80 °C and 30 min, the enzyme retained up to 91% and it showed stability over a wide pH range (from pH 5 to 11). The enzyme was found to be monomer with an estimated molecular mass of 31 kDa. The amino acid sequence showed high similarity (94%) to ATP-dependent protease fromB. Pumilus strain ATCC 7061. Thus, our alkaline thermostable and high salt-tolerant protease induced by a phytopathogenic fungus, could be useful for application in diverse areas such as biotechnology alimentary and agronomy industries.

High salt-tolerant protease from a potential biocontrol agentBacillus pumilus M3-16