Basidiomycetes harbour a hidden treasure of proteolytic diversity.
This survey is the first to investigate the proteolytic potential of a large number of basidiomycetes. Aqueous extracts of 43 basidiomycetes were investigated for their content of proteolytic activities, using gelatin zymography. The activities were characterised qualitatively using class specific inhibitors. All four catalytic classes of proteases were present, with 4% of all activities classified as aspartic, 5% as cysteine, 6% as metallo and 22% as serine proteases, while the remaining activities could not be assigned unambiguously. The majority of the latter were not inhibited by any of the inhibitors used and were termed insensitive. Different proteolytic activities are evenly distributed among members of all orders of basidiomycetes, although some taxa are a richer source of proteases than others. A significant number of the cysteine protease activities shown here have not previously been reported in basidiomycetes. The fungal cysteine and serine protease inhibitors, clitocypin and CNSPI (Clitocybe nebularis serine protease inhibitor), both inhibited a number of activities and even a few activities that were otherwise insensitive to all other inhibitors used, hence indicating their potential for a regulatory role. The number and diversity of proteases in basidiomycetes are seen to be remarkable and encourage further investigation.
Sabotic
Jerica
J
Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Jamova 39, SI-1000 Ljubljana, Slovenia.
Trcek
Tatjana
T
Popovic
Tatjana
T
Brzin
Joze
J
D001487:Basidiomycota / Q000201:enzymology*; D005656:Fungal Proteins / Q000302:isolation & purification* / Q000378:metabolism; D005780:Gelatin / Q000378:metabolism; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism*
D005656:Fungal Proteins; D005780:Gelatin; D010447:Peptide Hydrolases