Abstract
Lecanicillium psalliotae produced an extracellular protease (Ver112) which was purified to apparent homogeneity giving a single band on SDS-PAGE with a molecular mass of 32 kDa. The optimum activity of Ver112 was at pH 10 and 70 °C (over 5 min). The purified protease degraded a broad range of substrates including casein, gelatin, and nematode cuticle with 81% of a nematode (Panagrellus redivivus) being degraded after treating with Ver112 for 12 h. The protease was highly sensitive to PMSF (1 mM) indicating it to be a serine protease. The N-terminal amino acid residues of Ver112 shared a high degree of similarity with other cuticle-degrading proteases from nematophagous fungi which suggests a role in nematode infection.
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Yang, J., Huang, X., Tian, B. et al. Isolation and Characterization of a Serine Protease from the Nematophagous Fungus, Lecanicillium psalliotae, Displaying Nematicidal Activity. Biotechnol Lett 27, 1123–1128 (2005). https://doi.org/10.1007/s10529-005-8461-0
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DOI: https://doi.org/10.1007/s10529-005-8461-0