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Introduction: Zinc oxide nanoparticles (ZnONPs) are one of the most interesting metal oxide nanoparticles due to their easy functionalization, biocompatibility, and anticancer impact. The current study was designated to evaluate the in vitro and in vivo anticancer potency of biologically synthesized ZnONPs. Methods: Fenugreek seeds' extract was used to prepare ZnONPs, and then characterized by scanning electron microscope (SEM), energy dispersive X-ray (EDX), X-ray diffraction (XRD), UV-V spectroscopy and transmission electron microscope (TEM). The in vitro antitumor activity of biogenic ZnONPs against different cancer cells was evaluated by MTT assay. In addition, their anticancer activities alone or in combination with Doxorubicin were investigated against EAC model using intraperitoneal injection day after day. Results: Biologically synthesized ZnONPs showed a cytotoxic potency against different cancer cell lines combined with lower toxicity against normal cells. Further, the in vivo study revealed that the treatment by ZnONPs alone or combined with doxorubicin hampered the proliferation of EAC in mice by lowering the ascetic volume and the number of viable tumor cells. Moreover, ZnONPs alone or combined with doxorubicin induced the cell cycle arrest at G0/G1 phase and apoptosis by up-regulating the expression of caspase-3 and Bax and down-regulating the expression of Bcl-2 proteins. Conclusion: Our study indicated that the biogenic ZnONPs could be instructive to future cancer treatment research.

The efficient, facile and green synthesis of 4-bromo pyrazolone by using N-bromo saccharine as valuable green reagent encouraged us to prepare some new fused heterocycles as furopyrazole, pyranopyrazole, imidazopyrazole, pyrazolothiazole, pyrazol thiazolopyrimidine, pyrazolothiazine, oxathinopyrazole, pyrazolobenzooxazine, and pyrazoloquinoxaline. The synthesis was carried out by a basic condensation of bromo pyrazolone 2 and a suitable reagent in a one-pot reaction using chitosan as a green basic catalyst. The reactions were carried out by microwave irradiation technique as a green source of energy as well as the conventional heating. The antioxidant activity of the prepared compounds was studied using 1,1-phenyl-2-picrylhydrazyl (DPPH) assay and their antibacterial activity against Gram-positive, Gram-negative bacteria and antifungal activity was evaluated.

Eight fungal species were cultivated on the Czapek liquid medium and a good starting extracellular and intracellular exo-inulinase were selected. Extracellular inulinase from Ulocladium atrum was prepared in the presence of 1% inulin source and 0.2% sodium nitrate as the best carbon and nitrogen sources. Incubation for the U. atrum was increased till it reached its maximum (36 U/ ml) at the sixth day of incubation at 30°C which was the best temperature for the production of exo-inulinase. Effect of all metal ions inhibited inulase production by U. atrum. Exo-inulinase was purified by using ammonium sulfate precipitation, ion exchange chromatography on DEAEcellulose. Three active inulinase forms INI, INII and INIII were resolved, each for DEAE cellulose. The specific activity of INI was 1915 U/mg protein which represented 2.65-fold purification over the crude extract with 42.8% recovery pooling of INI placed on CM cellulose chromatography and INI was resolved into INIa, INIb and INIc. The specific activity of INIa was 2479.2 U/mg protein which represented 3.43-fold purification over the crude extract with 24.2% recovery. ª 2014 Production and hosting by Elsevier B.V. on behalf

Ulocladium atrum inulinase was immobilized on different composite membranes composed of chitosan/nonwoven fabrics. Km values of free and immobilized U. atrum inulinase on different composite membranes were calculated. The enzyme had optimum pH at 5.6 for free and immobilized U. atrum inulinase on polyester nonwoven fabric coated with 3 percent chitosan solution (PPNWF3), but optimum pH was 5 for immobilized U. atrum inulinase on polyester and polypropylene nonwoven fabrics coated with 1 percent chitosan solution. The enzyme had optimum temperature at 40 degree C for immobilized enzyme on each of polyester and polypropylene composite membranes coated with 1 percent chitosan, while it was 50 degree C for free and immobilized enzyme on polypropylene nonwoven fabric coated with 3 percent chitosan solution. Free U. atrum inulinase was stable at 40 degree C but thermal stability of the immobilized enzyme was detected up to 60 degree C. Reusability of immobilized enzyme was from 38 to 42 cycles of reuse; after this, the immobilized enzyme lost its activity completely. In conclusion, immobilized U. atrum inulinase was considerably more stable than the free enzyme, and could be stored for extended periods.