No abstract

Zinc oxide nanoparticles (ZnO NPs) were confirmed in this work as a good antioxidant source. They were biosynthesised by the preformed biomass of Aspergillus carneus when contacted with 1 mM zinc nitrate solution of pH 9 after 24 h at 150 rpm and 30°C. The biosynthesised NPs were moderately distributed, quasi-spherical in shape with clear edges and the average size of 8-12 nm. The NPs retained full stability at 4°C for at least six months. Their zeta potential was found to be 18.3 mV. Crystalline nature of the ZnO NPs was suggested from diffraction rings appeared as lighted spots on the selected area electron diffraction pattern and confirmed by the X-ray diffraction analysis. High radical scavenging activities (RSA) were found against peroxide (O 2− 2) and 2,2-diphenyl-1-picrylhydrazyl (DPPH). Good activities were also recorded against hydroxyl (OH −) and superoxide (O − 2) radicals. This potential RSA can be rendered to the adsorbed biomolecules on the NPs surface especially the phenolic compounds detected by Fourier transform infrared analysis.

Cochliobolus hawaiiensis Alcorn AUMC 8606 was chosen from the screened twenty fungal species as the potent producer of fibrinolytic enzyme on skimmed-milk agar plates. The greatest enzyme yield was attained when the submerged fermentation (SmF) conditions were optimized, and it was around (39.7 U/mg protein). Moreover, Upon optimization of fibrinolytic enzyme production under solid state fermentation (SSF), the maximum productivity of fibrinolytic enzyme was greatly increased recorded a bout (405 U/mg protein) on sugar cane bagasse. The yield of fibrinolytic enzyme by C. hawaiiensis under SSF was higher than that of SmF with about 10.20 fold. The purification procedures of fibrinolytic enzyme caused a great increase in its specific activity to 2581.6 U/mg protein with an overall yield of 55.89%, 6.37 purification fold and molecular weight of 35kDa. Maximal activity was recorded at pH 7 and 37oC. The enzyme showed the highest affinity towards Fibrin, with Vmax of 240 U/ml and an apparent Km value of 47.61 mmol. Mg2+ and Ca2+ moderately induced fibrinolytic activity, while Cu2+ and Zn2+ greatly suppressed the enzyme activity. The produced enzyme is categorized as serine protease and non metalloprotease due to the great suppression in its activity by using phenylmethylsulfonyl fluoride and thylenediamine-tetraacetat, respectively. The purified fibrinolytic enzyme showed efficient thrombolytic and antiplaetlet aggregation activities by completely prevention and dissolution of the blood clot which confirmed by microscopic examination and amelioration of blood coagulation assays. These findings suggested that the produced fibrinolytic enzyme is a promising agent in management of blood coagulation disorders