ABSTRACT
The production of proteases by white rot fungi, such as those of the genus Pleurotus, is related to the degradation of wood proteins, the substrate on which these fungi grow in the environment. From the point of view of production, they are still little explored for this purpose. A selection of agro-industrial residues highlighted corn bagasse as the best substrate for solid-state protease production using the basidiomycete Pleurotus pulmonarius. The enzyme production was maximized through a factorial design, where the enzyme activity increased from 137.8 ± 1.9 to 234.1 ± 2.7 U/mL. Factors such as temperature stability, pH, and chemical reagents were evaluated. The optimum temperature was 45 °C, showing low thermal stability at higher temperatures. The enzyme inhibition occurred by Mn2+ (50.3%) and Ba2+ (76.4%); SDS strongly inhibited the activity (82.4%), while pepstatin A partially inhibited (56%), suggesting an aspartic protease character. Regarding pH, the highest protease activity was obtained at pH 5.5. Partial characterization resulted in apparent values of the KM and Vmax constants of 0.61 mg/mL and 1.79 mM/min, respectively.(AU)
