Oxidative enzymes from newly local strain Aspergillus iizukae EAN605 using pumpkin peels as a production substrate: Optimized production, characterization, application and techno-economic analysis.

The present study deals with optimizing, producing, characterizing, application and techno- economic analysis of oxidative enzymes [Laccase (Lac), manganese peroxidase (MnP), and lignin peroxidase (LiP)] from Aspergillus iizukae EAN605 in submerged fermentation process using pumpkin peels as a production substrate. The best operating parameters for producing Lac, MnP and LiP (6.15, 2.58 and 127.99 U mg-1 respectively) were recorded with 20 g 100 mL-1 of substrate, 4.6 mL 100 mL-1 of inoculum size at pH 5.5 after 10 days. The crude enzyme exhibited high stability at pH (3-9) and temperatures (20-60 °C). Km (Michaelis-Menten) of Lac, MnP and LiP crude enzyme was 2.25, 1.79 and 0.72 mM respectively. The decolourization of Remazol Brilliant Blue R by the crude enzyme was 84.84 %. The techno-economic analysis was assessed for a production unit with an annual operating time for enzymatic production and application is 7920 h/year and 100 m3 of the capacity. The process would produce 27,000 cm3 of crude enzyme with a price of USD 0.107 per cm3 compared to USD 1 per cm3 of the current commercial enzyme. The findings indicated that pumpkin peels have potential as a production substrate for oxidative enzymes from A. iizukae EAN605 and is economically feasible.

Asparagus byproducts as a new source of peroxidases.

Soluble peroxidase (POD) from asparagus byproducts was purified by ion exchange chromatographies, and its kinetic and catalytic properties were studied. The isoelectric point of the purified isoperoxidases was 9.1, and the optimum pH and temperature values were 4.0 and 25 °C, respectively. The cationic asparagus POD (CAP) midpoint inactivation temperature was 57 °C, which favors its use in industrial processes. The Km values of cationic asparagus POD for H2O2 and ABTS were 0.318 and 0.634 mM, respectively. The purified CAP is economically obtained from raw materials using a simple protocol and possesses features that make it advantageous for the potential use of this enzyme in a large number of processes with demonstrated requirements of thermostable POD. The results indicate that CAP can be used as a potential candidate for removing phenolic contaminants.

Laccase and other ligninolytic enzyme activities of selected strains of Trametes spp. from different localities and substrates.

Eighty-three strains belonging to three species of the genus Trametes FR. (T. versicolor, T. hirsuta and T. ochracea) collected in different localities and on different substrates were screened for laccase production. The production of other lignin-modifying enzymes--manganese peroxidase (MnP) and lignin peroxidase (LiP)--and the decolorization ability were also determined in 21 of them. Production variability was relatively high and no significant correlation was found between the origin of the strains (locality, substrate) and the enzyme production. Dikaryons of all 3 species (but not of all their strains) exhibited LiP activity, which was not detected in the respective monokaryons.