Serine protease (PubMed:10103041, PubMed:7763554). Hydrolyzes azocasein (PubMed:10103041). Cleaves peptide bonds of the oxidized insulin B chain preferably at 15-Leu-|-Tyr-16, but also at 4-Gln-|-His-5 and 24-Phe-|-Phe-25, and to a lesser extent at 5-His-|-Leu-6 and 25-Phe-|-Tyr-26. Hydrolyzes amide bonds between amino acids and 7-amino-4-methylcoumarin (AMC) in vitro (PubMed:7763554). Inhibited by 0.1 mM diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), chymostatin and elastatinal. Not inhibited by N-alpha-p-tosyl-L-lysine chloromethylketone (TLCK), N-tosyl-L-phenylalanyl chloromethyl ketone (TPCK) or N-carbobenzoxy-L-phenylalanine chloromethylketone (ZPCK). Active at pH 7 (up to 40 degrees Celsius for 30 min) and at pH 11 (up to 25 degrees Celsius). Protease activity is retained up to 40 degrees Celsius for 30 min, but completely inactivated at 50 degrees Celsius (at pH 7). Activity is retained up to 25 degrees Celsius, and completely inactivated at 40 degrees Celsius (at pH 11). Expression is induced in mycelia after 24 hours of growth. Maximal expression is reached at about 42 hours and expression is slightly decayed after 48 hours. Causes an allergic reaction in human. Binds to IgE. Belongs to the peptidase S8 family.