Production and characterization of cellulases derived from saprophytic fungi Penicillium bilaiae InaCC F16

Cellulases are the enzymes that hydrolyze β-1,4 glycosidic bonds in cellulose molecules into simpler molecules such as glucose. The cellulase complexes derived from microbes have been considered as a potential source for biochemical, biotechnology, and bioindustry. Thus, they are broadly used in industries for leather tanning, food, medicine, and detergent formulations. The important group of cellulase-producing fungi, such as Penicillium, is reportedly able to produce high levels of cellulase and hemicellulase complexes. This study aimed to determine the characterization and activity of cellulase enzymes produced by fungi Penicillium and analyze their cellulase activities, both qualitatively and quantitatively. The fungal strain used in this study was obtained from the Indonesian Culture Collection (InaCC) with the accession number of InaCC F15, InaCC F16, and InaCC F17. The parameters used for investigating the enzyme characteristic and activity were incubation time, index of substrate concentration on carboxymethyl cellulose (CMC), temperature, pH, and the effect of the addition of several metal ions as activators and/or inhibitors. The semi-qualitative analysis showed that the clear zone was formed in the surrounding colony of Penicillium InaCC F16 with a cellulolytic index was at 3.3. The optimum cellulase activity was obtained on two days incubation period, the temperature of 40°C, pH 5, and substrate concentration at 2%. The addition of metal ions at a concentration of 1mM showed that enzymes were activated by cations CoCl₂, CuCl₂, MgCl₂, and inhibited by NaCl and ZnCl₂.