Production, Purification and Characterization of Catalase from Aspergillus Fumigatus

Creative Commons License

Aggez C., Yüzügüllü Karakuş Y.

Open Access Journal of Microbiology and Biotechnology, vol.7, no.4, pp.1-9, 2022 (Peer-Reviewed Journal)


This study describes production, purification, and characterization of catalase enzyme from Aspergillus fumigatus. The crude enzyme extract was obtained from A. fumigatus on 7th day of cultivation of cells grown at 37 °C and 155 rpm in 1-liter YpSs medium containing 1% (w/v) glucose and 0.5 mM H2 O2 . Then, the enzyme was successfully purified 24-fold with 55% recovery. The molecular weight was found ~70 kDa by SDS-PAGE. The optimum reaction temperature of the enzyme was established as 60 °C and the pH was 7.0. Km and Vmax values were calculated as 7.4 mM and 1250 μM min-1, respectively. Stability tests have shown that the enzyme can remain active in a wide range of pH (4.0-9.0). Thermal stability of catalase was between 30 °C and 50 °C. The enzyme also presented stability against various solvents including ethanol, methanol, acetone, and dimethyl sulfoxide depending on the concentration and incubation time. The biochemical properties of the enzyme (low Km value, stability against varying pH and organic solvents, etc.) indicate that it can function as a good biocatalyst in different industrial applications.