Polyacrylonitrile nanofiber (PANFS), a well-known polymers, has been extensively employed in the manufacturing of carbon nanofibers (CNFS), which have recently gained substantial attention due to their excellent features, such as spinnability, environmental friendliness, and commercial feasibility. Because of their high carbon yield and versatility in tailoring the final CNFS structure, In addition to the simple formation of ladder structures through nitrile polymerization to yield stable products, CNFS and PAN have been the focus of extensive research as potential production precursors. For instance, the development of biomedical and high-performance composites has now become achievable. PAN homopolymer or PAN-based precursor copol

Polyacrylonitrile nanofiber (PANFS), a well-known polymers, has been extensively employed in the manufacturing of carbon nanofibers (CNFS), which have recently gained substantial attention due to their excellent features, such as spinnability, environmental friendliness, and commercial feasibility. Because of their high carbon yield and versatility in tailoring the final CNFS structure, In addition to the simple formation of ladder structures through nitrile polymerization to yield stable products, CNFS and PAN have been the focus of extensive research as potential production precursors. For instance, the development of biomedical and high-performance composites has now become achievable. PAN homopolymer or PAN-based precursor copolymer can

Pharmaceuticals have been widely remaining contaminants in wastewater, and diclofenac is the most common pharmaceutical pollutant. Therefore, the removal of diclofenac from aqueous solutions using activated carbon produced by pyrocarbonic acid and microwaves was investigated in this research. Apricot seed powder and pyrophosphoric acid (45 wt%) were selected as raw material and activator respectively, and microwave irradiation technique was used to prepare the activated carbon. The raw material was impregnated in pyrophosphoric acid at 80◦C with an impregnation ratio of 1: 3 (apricot seeds to phosphoric acid), the impregnation time was 4 h, whereas the power of the microwave was 700 watts with a radiation time of 20 min. A series o

For this research, the utilisation of electrocoagulation (EC) toremove theciprofloxacin (CIP) and levofloxacin (LVX) from aqueous solutions was examined. The effective removal efficiencies are 93.47% for CIP and 88.00% for LVX, under optimum conditions. The adsorption isotherm models with suitable mechanisms were applied to determine the elimination of CIP and LVX utilizingtheEC method. Thefindingsshowed the adsorption of CIP and LVX on iron hydroxide flocs followed the Sips isotherm, with correlation coefficient values (R2) of 0.939 and 0.937. Threekinetic models were reviewed to determine the accurate CIP and LVX elimination methods using the EC method. The results showed that itfittedfor the second-order model, which indicated that the c

For this research, the utilisation of electrocoagulation (EC) toremove theciprofloxacin (CIP) and levofloxacin (LVX) from aqueous solutions was examined. The effective removal efficiencies are 93.47% for CIP and 88.00% for LVX, under optimum conditions. The adsorption isotherm models with suitable mechanisms were applied to determine the elimination of CIP and LVX utilizingtheEC method. Thefindingsshowed the adsorption of CIP and LVX on iron hydroxide flocs followed the Sips isotherm, with correlation coefficient values (R2) of 0.939 and 0.937. Threekinetic models were reviewed to determine the accurate CIP and LVX elimination methods using the EC method. The results showed that itfittedfor the second-order model, which indicated that the 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.