Investigation of Seasonal Dynamism of Peroxidase from Strains of Aspergillus sp.

Peroxidases A and B production were carried out from Aspergillus tamari and fumigates respectively isolated from petroleum hydrocarbon spilled soil. Physicochemical properties of the respective soil showed pH of 4.45 and 6.5 for soils from point 1 and II respectively and higher conductivity of 613 and 1013 (Ω-1 Cm-1), respectively when compared with the control sample. Dissolved mineral of Cl-, SO4, K, Ca, Mg in the respective soil samples from the petroleum spilled sites was significantly high when compared with the control experiment except for soil sample I which showed a relative low phosphate concentration of 1,23 in the presence of the control experiment, respectively. TOC and TOM contents were 87.91, 119.04; 108.13 and 146.42 mg/g for soil sample I, and III, respectively. In all the tested parameters, the experimented soils were significantly high than the control soil sample. Molecular tests (18S rDNA.) were used to identify the pure isolates of Aspergillia. Studies on the effect of the incubation period on the production of peroxidase from strains of ofAspergillus tamarrii sp. and Aspergillusshowed that the highest peroxidase (A and B) activity representing peroxidase from dry and wet conditions were obtained on the day 6th and 5th of the fermentation time figure peroxidase A activity peaked at pH 5 while that of peroxidase B peaked at pH 6.0; proteins with highest peroxidase activity was peak precipitated at 60% and 80% saturation of the salt for peroxidase A and B, respectively. The gel chromatogram showed single almost superimposed peaks of enzyme activity for peroxidase A and B respectively. Peroxidase A and B activity peaked at pH 4.5 and 5.0. Optimum temperature for the enzyme activity was at 50 and 60°C respectively. Km and V max of 3.45mM and 280 μmole/min; 2.44mM and 305μmole/min were extrapolated from the reciprocal curve of Lineweaver-burke at various concentrations of 2,6 DMP for peroxidase A. Fe, Ca, Co and Mn selected as their notable impact in the active site of peroxidase guided the selected were assayed in the presence of the enzymes, respectively. The stability curve obtained for the peroxidases was single biphasic which represents the first order; Peroxidase B maintained greater stability than A at its optimum pH and pH 7. The enzymes maintained greater than 50% of their activity after 30 min of incubation as activity progressively decreased up to 40% after 60 min of incubation. Thermal stability of peroxidase A and B at their respective optimum temperatures (50 and 60°C) and at 70°C showed a biphasic stability curve of peroxidase A but single phase in peroxidase B. Peroxidase B maintained greater stability than A at its optimum temperature and at 70°C. The enzymes maintained greater than 50% of their activity after 60 min of incubation. Stability curve of peroxidase A and B at 70°C showed a maximum activity of the enzymes after 30 min of incubation. However, Peroxidase B maintained greater stability than A after 60 min of incubation. Peroxidase B maintained 57.89% of its activity after 60 min while peroxidase A from fig 19 showed a residual activity of 41.2%.