The partial characterisation of endoproteases and exoproteases from three species of entomopathogenic entomophthorales and two species of deuteromycetes

The entomopathogenic entomophthoraceae (zygomycotina) Erynia rhizospora, Erynia dipterigena, and Erynia neoaphidis and the deuteromycete Aspergillus flavus produced single novel endoproteases (pI ca. 9) with activity against trypsin and chymotrypsin substrates. In contrast, the deuteromycete Paecilomyces farinosus produced a chymotrypsin (pI ca. 10).Inhibitor studies confirmed that the mixed activities (purified by isoelectric focusing) were derived from single endoproteases. The most potent inhibitor was Chicken ovoinhibitor. Little or no inhibition was observed for P. farinosus endoprotease by any of the chemicals tested.Although the different fungi possessed a broad spectrum of aminopeptidase activity, 3 species (E. rhizospora, E. dipterigena, and A. flavus) showed a preference for leucine at the N-terminal position and 2 species (E. neoaphidis and P. farinosus) showed maximal activity against arginine. Inhibitor studies confirmed these aminopeptidases as metallo-enzymes.