Open Access Original Research Article

Mineralization of Wastewater from the Teaching Hospital of Treichville by a Combination of Biological Treatment and Advanced Oxidation Processes

Sadia Sahi Placide, Kambiré Ollo, Gnamba Corneil Quand-même, Pohan Lemeyonouin Aliou Guillaume, Berté Mohamed, Ouattara Lassiné

Asian Journal of Chemical Sciences, Page 1-10
DOI: 10.9734/ajocs/2021/v10i219086

Biological treatment, due to its low installation cost, is widely used for wastewater treatment. However, this treatment remains ineffective for the oxidation of so-called emerging molecules. To solve this environmental problem, advanced oxidation processes (AOPs) combine with Biological treatment for rapid, efficient and cost-effective purification of wastewater. This combination used in this work, allowed a total mineralization of a real wastewater solution from the teaching hospital of Treichville named CHU of Treichville in Abidjan (CHUT), both in terms of organic and microbiological pollutants. Real wastewater from the CHUT underwent a Biological treatment for 28 days via the Zahn-Wellens methods which made it possible to have a reduction rate of the chemical oxygen demand of more than 90% of biologically active organic pollutants. The biologically treated wastewater was doped with ceftriaxone (CTX) to simulate a situation of wastewater containing a recalcitrant compound after Biological treatment. Subsequently, the doped solution underwent treatment with different AOPs (UV / H2O2, Fe2+ / H2O2 and UV / Fe2+ / H2O2). This combination resulted in a COD reduction rate of over to be higher 98% and total inactivation of microbiological germs.

Open Access Original Research Article

Physicochemical Evaluation of Eichhornia crassipes and Pennisetum purpureum used for Production of Drilling Mud Additives

I. U. Emenike, Leo C. Osuji, M. C. Onojake

Asian Journal of Chemical Sciences, Page 23-31
DOI: 10.9734/ajocs/2021/v10i219088

Cellulose isolated from Eichhornia crassipe (Water hyacinth) and Pennisetum purpureum (elephant grass) were evaluated using Fourier Transform Infra-Red spectroscopy and standard analytical methods for production of drilling mud. The physico-chemical analyses were carried out after chlorination and alkaline process using sodium chlorite and sodium hydroxide for the extraction of cellulose from the two biomass samples under same experimental conditions. Results of physico-chemical analysis of Eichhornia crassipes showed pH: 7.30; conductivity 0.028; bulk density 0.1097g/ml. Pennisetum purpureum showed pH: 7.50; conductivity 0.192; bulk density 0.1378g/ml. Pennisetum purpureum has a higher cellulose yield of 31.39% compared with Eichhornia crassipes with a percentage cellulose yield of 21.88%. Both biomass samples have Herzberg strain of Violet-blue. The results of the Fourier Transform Infra-Red spectroscopy showed prominent peaks at 3353-3164, 1655, 1629, 1320, 1033 and 1019 cm-1. The broad absorption bands around 3353-3164 cm-1 indicated stretching of –OH groups due to inter-molecular and intra-molecular hydrogen bonds of polymeric compounds. The sharp bands at 1655 cm-1  and 1629 cm-1 showed C=C stretch of aromatics. The sharp absorption bands observed at 1320, 1019 and 1033 cm-1 were characteristic of C—O stretch and C—O—C asymmetric stretch of cellulose. The FTIR results proved that the products extracted from the two samples were aromatic hydroxyl compounds. The results of the physicochemical analyses showed that cellulose isolated from the biomass samples which are persistent noxious weeds that invade the aquatic and terrestrial environment can be utilized in industrial applications for drilling fluid production.

Open Access Original Research Article

Antimicrobial Activities of Co (III), Mono and Tri-nuclear Ni Complexes Containing Schiff base Functionalized Imidazolium based Ligands

Samaila Abubakar, Musa Muktari, Rifkatu Kambel Dogara

Asian Journal of Chemical Sciences, Page 32-40
DOI: 10.9734/ajocs/2021/v10i219089

We reported the antimicrobial activities of cobalt and nickel complexes containing imino-NHC ligands. Complex 2 was synthesized by direct reaction of the insitu generated free carbene from 2-[2-(3-benzylimidazol-1-yl)ethyliminomethyl]phenol ligand with NiCl2 diglyme while complexes 3-5 were previously reported as catalysts in the transfer hydrogenation reaction of ketones. The compounds 1-5 were screened for antimicrobial sensitivity test against four gram-negative bacteria Escherichia Coli (E-coli), Shigella, Klebsiella Pneumoniae (K. Pneumoniae) and Salmonella Typhi (S.Typhi) and a gram positive bacteria Staphylocossus aureus (S.aureus). At a varying concentrations of 100, 200, 300, 400 and 500 µg/mL, significant activities were recorded using disc diffusion methods. The cobalt complex 3 was found to have higher activities compared with the corresponding nickel complexes and among the three nickel complexes, nickel complex with pyridine as wingtip was found to be more active than the one with a benzyl group. Similarly, the nickel centre with mononuclear was found to be more active than the tri-nuclear nickel complex.  Except for the cobalt complex 3 no activity was recorded against S. typhi for all the nickel compounds. 

Open Access Original Research Article

Removal of Malachite Green Dye from Aqueous Solutions by an Efficient Nanosized NiO Fabricated by a Facile Sol-Gel Autocombustion

Hesham H. El-Feky, Reham N. Nassar, Alaa S. Amin, Mostafa Y. Nassar

Asian Journal of Chemical Sciences, Page 41-51
DOI: 10.9734/ajocs/2021/v10i219090

Nickel oxide nanostructures were synthesized via a sol-gel combustion method using glucose, glycine and tartaric acid fuels. The effect of the fuel type on the formed nanostructures was studied. The as-prepared products were characterized by means of FE-SEM, HR-TEM, XRD, and FT-IR analyses. The results exhibited that the used fuels gave NiO products with different morphologies, and the glucose fuel produced pure NiO nanoparticles with the smallest crystallite size (ca. 8.2 nm). The adsorption properties of the NiO products for the removal of malachite green dye (MG) was examined. Using a batch method, various parameters affecting the adsorption properties were studied. The results revealed that NiO nanostructure generated from the glucose fuel had the highest adsorption capacity

Open Access Review Article

Peroxidase, an Example of Enzymes with Numerous Applications

I. Nnamchi, Chukwudi, C. Amadi Onyetugo, I. Nnaji Amarachi

Asian Journal of Chemical Sciences, Page 11-22
DOI: 10.9734/ajocs/2021/v10i219087

The enzyme peroxidase is a heme or iron-porphyrin protein that belongs to a large family of enzymes called the oxidoreductases. Their function mainly is to oxidize molecules at the expense of hydrogen peroxide. They are widely distributed in living organisms, and usually show dramatic colour-product formation as a result of their catalytic effect. They generally catalyse many oxygen transfer reactions involving hydrogen peroxide or anyone of the many other peroxides as electron acceptors and substrates. This ability of reducing peroxides at the expense of electron donating substrates is what marks peroxidases as ubiquitous and very important enzymes with many biotechnological applications. Not surprisingly therefore peroxidases play many important roles in different areas of biotechnology. Among others, these include such diverse areas as bioenergy, bioremediation, dye decolorization, humic acid degradation, paper and pulp and textile industries among many others. An important reason for this ability is the different areas from which peroxidases could be sourced as the function of many peroxidases show variations according to its source. This is a character that differentiates peroxidases from many other biological catalysts. Among the many different types of peroxidases are the heme peroxidases which mainly come from plants and fungi and include among others lignin peroxidases, manganese peroxidases and versatile peroxidases.  Some important types of peroxidases from humans and animals are glutathione peroxidase, thyroid peroxidase, lactoperoxidase, salivary peroxidase and thyroid peroxidase.