Ozonation of an extremely polluted petrochemical wastewater from styrene and propylene oxide production and the influence of different factors on the treatment efficiency were investigated. The treatment efficiency was the highest under... more
Ozonation of an extremely polluted petrochemical wastewater from styrene and propylene oxide production and the influence of different factors on the treatment efficiency were investigated. The treatment efficiency was the highest under alkaline conditions and with the use of catalysts. Optimal values of ozone concentration and volumetric flow rate of the ozone-oxygen mixture were 20 mg L –1 and 400 L (L × h) –1 , respectively. The use of H2O2 (0.075 wt%) as a catalyst allowed the maximum COD conversion (93%) and acetophenone removal (98%) to be achieved after 60 min. In the meantime, at an optimal concentration of MnSO4.5H2O (0.1 wt%), the treatment efficiency in terms of COD and acetophenone removal increased up to 85% and 84%, respectively. Acetophenone was completely removed from the wastewater when the ozonation time was increased to 90 min, using H2O2 or MnSO4.5H2O as a catalyst, while phenol, styrene, and ethylbenzene were entirely removed after 60 min. During the ozonation p...
Ribonucleases are considered as promising tools for anticancer treatment due to their selective cytotoxicity against tumor cells. We investigated a new RNase from Bacillus altitudinis termed BALNASE (B. altitudinis RNase). Balnase is a... more
Ribonucleases are considered as promising tools for anticancer treatment due to their selective cytotoxicity against tumor cells. We investigated a new RNase from Bacillus altitudinis termed BALNASE (B. altitudinis RNase). Balnase is a close homolog of the well-known cytotoxic binase, differing by only one amino acid residue: nonpolar hydrophobic alanine at position 106 in the balnase molecule is replaced by a polar uncharged threonine in binase. The most exciting question is how the physico-chemical properties and biological effects of RNase might be changed by A106T substitution. Here, we have developed a chromatography-based rapid and modern technique for the purification of this new RNase which allowed us to get a protein sample of high quality with specific activity of 1.2 × 10(6) units in preparative amounts, suitable for further investigation of its biological properties.
