This paper concerns is the preparation and characterization of a bidentate ligand [4-(5,5- dimethyl-3-oxocyclohex-1-enylamino)-N-(5-methylisoxazol-3-yl) benzene sulfonamide]. The ligand was prepared from fusing of sulfamethoxazole and dimedone at (140) ºC for half hour. The complex was prepared by refluxing the ligand with a bivalent cobalt ion using ethanol as a solvent. The prepared ligand and complex were identified using Spectroscopic methods. The proposed tetrahedral geometry around the metal ions studied were concluded from these measurements. Both molar ratio and continuous variation method were studied to determine metal to ligand ratio (M:L). The M to L ratio was found to be (1:1). The adsorption of cobalt complex was carried out

Wastewater recycling for non-potable uses has gained significant attention to mitigate the high pressure on freshwater resources. This requires using a sustainable technique to treat natural municipal wastewater as an alternative to conventional methods, especially in arid and semi-arid rural areas. One of the promising techniques applied to satisfy the objective of wastewater reuse is the constructed wetlands (CWs) which have been used extensively in most countries worldwide through the last decades. The present study introduces a significant review of the definition, classification, and components of CWs, identifying the mechanisms controlling the removal process within such units. Vertical, horizontal, and hybrid CWs

Leucine amino peptidases (LAP; EC 3.4.11.1) constitute a diverse set of exopeptidases that catalyze the hydrolysis of leucine residues from the amino-terminal of protein or peptide substrates, (LAP) are present in animals, plants, and microbes. In this study, leucine amino peptidase was purified partial from Arachis hypogaea seeds by using gel filtration chromatography Sephadex G-100. The enzyme was purified 3.965 fold with a recovery of 29.4%. Its pH and temperature optimum were(8.7) and (37oC), respectively. The results show novel properties of LAP from Arachis hypogaea L. or peanut. The Km value for LAP (77 mM), with V max (1538 m mole min-1). We recommend a separate isoenzymeof the enzyme (LAP) from Arachis hypogaea on L. peanut seeds a

In this study, the ability of pistachio shells, as an unconventional adsorbent, to recover thallium cations from contaminated aqueous solutions was investigated. To achieve the objective of the study, practical experiments were conducted using a batch-mode adsorption unit under various operating conditions. The results obtained showed that the pistachio shells have the ability to remove thallium cations with a high efficiency exceeding 86% at room temperature. The results indicated that the maximum treatment efficiency was achieved at values of 7, 350 rpm, 86 ppm, 5 g, 150 min of pH, agitation speed, initial concentration of thallium, dosage of pistachio shell used, and contact time, respectively. Morphological results confirmed tha

Beta-lactamase was purified from local isolate Klebsiella pneumonia by several steps included precipitation with ammonium sulphate at 20-40% saturation, DEAE- ion exchange chromatography and gel filtration on Sephacryl S-200 column. The obtained purification fold and recovery were 32.66; 47.04% respectively. The characterization of the purified beta-lactamase showed that the molecular weight was about 4000 daltons as determined by gel filtration.Purified enzyme had an optimal pH of 7 for activity and an optimal stability between pH 6.5-7.5, results shows that the optimal temperature appear to be 35 ? C .During storage the enzyme retained 72% at -20 ? C and retained 25% of the activity at the same period at 4 ? C.

Endoglucanase produced from Aspergillus flavus was purified by several steps including precipitation with 25 % ammonium sulphate followed by Ion –exchange chromatography, the obtained specific activity was 377.35 U/ mg protein, with a yield of 51.32 % .This step was followed by gel filtration chromatography (Sepharose -6B), when a value of specific activity was 400 U/ mg protein, with a yield of 48 %. Certain properties of this purified enzyme were investigated, the optimum pH of activity was 7 and the pH of its stability was 4.5, while the temperature stability was 40 °C for 60 min. The enzyme retained 100% of its original activity after incubation at 40 °C for 60 min; the optimum temperature for enzyme activity was 40 °C.

The present investigation is concerned for the purification of impure zinc oxide (80-85 wt %) by using petroleum coke
(carbon content is 76 wt %) as reducing agent for the impure zinc oxide to provide pure zinc vapor, which will be
oxidized later by air to the pure zinc oxide.
The operating conditions of the reaction were studied in detail which are, reaction time within the range (10 to 30 min),
reaction temperature (900 to 1100 oC), air flow rate (0.2 to 1 l/min) and weight percentage of the reducing agent
(petroleum coke) in the feed (14 to 30 wt %).
The best operating conditions were (30 min) for the reaction time, (1100 oC) for the reaction temperature, (1 l/min) for
the air flow rate, and (30 wt %) of reducing

Twenty isolates of Serratia marcescens were isolated from inflammation of the urinary tract (UTI)., These isolates were found to produce hemolysin as indicated by blood agar plates in which the hemolysis of red blood cell indicate a positive result. Isolates were selected according to their hemolysis activity by measuring absorbance of hemoglobin at 405 nm that released from red blood cell. Hemolysin was completely purified using 50-75% saturation of ammonium sulphate followed by ion exchange chromatography with DEAE-cellulose then gel filtration chromatography by sepharose 4B. Accordingly molecular weight for the purified toxin was estimated as 45 KD.