Purification and characterization of a new fungalysin-like metallopeptidase from the culture filtrate of a plant worm, Nomuraea atypicola

A new protease was purified from the culture filtrate of a plant worm, Nomuraea atypicola. The activity of the protease was suppressed by metalloprotease inhibitors such as EDTA and 1,10-phenanthroline, suggesting that it might be a metalloprotease. Its molecular mass was estimated to be 48 kDa by SDS-PAGE, and its optimal pH and temperature were pH 8.5–9.0 and 40 °C, respectively. The N-terminal amino acid sequence of the metalloprotease was similar to those of fungalysin metallopeptidases of the M36 family from fungi such as Coccidioides posadasii, Pyrenophora tritici-repentis, and Arthroderma gypseum, supporting the idea that it is a fungalysin-like metallopeptidase.

► A new protease was purified from the culture filtrate of a plant worm, Nomuraea atypicola.
► The activity of the protease was suppressed by several known metalloprotease inhibitors.
► The N-terminal amino acid sequence of the N. atypicola protease was similar to those of fungalysin metallopeptidases of the M36 family from fungi.