One-Step Room-Temperature Synthesis of Bimetallic Nanoscale Zero-Valent FeCo by Hydrazine Reduction: Effect of Metal Salts and Application in Contaminated Water Treatment.

The effect of initial salt composition on the formation of zero-valent bimetallic FeCo was investigated in this work. Pure crystalline zero-valent FeCo nanoparticles (NPs) were obtained using either chloride or nitrate salts of both metals. Smaller NPs can be obtained using nitrate salts. Comparing the features of the FeCo prepared at room temperature and the solvothermal method revealed that both materials are almost identical. However, the room-temperature method is simpler, quicker, and saves energy. Energy-dispersive X-ray (EDX) analysis of the FeCo NPs prepared using nitrate salts at room temperature demonstrated the absence of oxygen and the presence and uniform distribution of Fe and Co within the structure with the atomic ratio very close to the initially planned one. The particles were sphere-like with a mean particle size of 7 nm, saturation magnetization of 173.32 emu/g, and surface area of 30 m2/g. The removal of Cu2+ and reactive blue 5 (RB5) by FeCo in a single-component system was conformed to the pseudo-first-order and pseudo-second-order models, respectively. The isotherm study confirmed the ability of FeCo for the simultaneous removal of Cu2+ and RB5 with more selectivity toward Cu2+. The RB5 has a synergistic effect on Cu2+ removal, while Cu2+ has an antagonistic effect on RB5 removal.

Biodegradation of feather waste by keratinase produced from newly isolated Bacillus licheniformis ALW1.

Keratinase are proteolytic enzymes which have gained much attention to convert keratinous wastes that cause huge environmental pollution problems. Ten microbial isolates were screened for their keratinase production. The most potent isolate produce 25.2 U/ml under static condition and was primarily identified by partial 16s rRNA gene sequence as Bacillus licheniformis ALW1. Optimization studies for the fermentation conditions increased the keratinase biosynthesis to 72.2 U/ml (2.9-fold). The crude extracellular keratinase was optimally active at pH 8.0 and temperature 65 °C with 0.7% soluble keratin as substrate. The produced B. licheniformis ALW1 keratinase exhibited a good stability over pH range from 7 to 9 and over a temperature range 50-60 °C for almost 90 min. The crude enzyme solution was able to degrade native feather up to 63% in redox free system.

Levansucrase optimization using solid state fermentation and levan biological activities studies.

Bacillus subtilis NRC1aza produced levansucrase under solid state fermentation using starch as support. A sequential optimization strategy, based on statistical experimental designs is employed to enhance enzyme productivity. First, a 2-level Plackett-Burman design was applied for bioprocess parameters screen that significantly increase levansucrase production. Second optimization step was performed using fractional factorial design in order to optimize the amounts of highest positive variables that had significant effect on levansucrase productivity. Maximal enzyme productivity of 170 U/gds was achieved in presence of glucose, yeast extract, and pH 8. In vitro, experiments confirmed that LevCR and LevQT had an antitumor activity against different animal and human cancer cell lines by demonstrating inhibitory effects on growth of Ehrlich ascites carcinoma cell line, human MCF-7 breast and liver HepG2 cancer cell lines, in particular LevQT was found to be efficacious compared to anticancer drug, cisplatin. Result focused in LevCR as strong fibrinolytic agent.