Evaluation of the Binding Relationship of the RdRp Enzyme to Novel Thiazole/Acid Hydrazone Hybrids Obtainable through Green Synthetic Procedure

The viral RNA-dependent RNA polymerase (RdRp) complex is used by SARS-CoV-2 for genome replication and transcription, making RdRp an interesting target for developing the antiviral treatment. Hence the current work is concerned with the green synthesis, characterization and docking study with the RdRp enzyme of the series of novel and diverse hydrazones and pyrazoles. 4-Methyl-2-(2-(1-phenylethylidene)hydrazineyl)thiazole-5-carbohydrazide was prepared and then condensed with different carbonyl compounds (aldehydes and ketones either carbocyclic aromatic or heterocyclic) afforded the corresponding hydrazide-hydrazones. The combination of the acid hydrazide with bifunctional reagents such as acetylacetone, β-ketoesters (ethyl acetoacetate and ethyl benzoylacetate) resulted in the formation of pyrazole derivatives. The synthesized compounds were all obtained through grinding method using drops of AcOH. Various analytical and spectral analyses were used to determine the structures of the prepared compounds. Molecular Operating Environment (MOE®) version 2014.09 was used to estimate interactions between the prepared thiazole/hydrazone hybrids and RdRp obtained from the protein data bank (PDB: 7bv2) using enzyme-ligand docking for all synthesized derivatives and Remdesivir as a reference. Docking results with the RdRp enzyme revealed that the majority of the investigated drugs bind well to the enzyme via various types of interactions in comparison with the reference drug

Biologically Reduced Zinc Oxide Nanosheets Using Phyllanthus emblica Plant Extract for Antibacterial and Dye Degradation Studies

The nanostructures synthesized using the green chemistry method have recently attracted the attention of scientists due to their significance in many scientific domains. This work provides an overview of the biosynthesis of zinc oxide (ZnO) nanosheets (NSs) using Phyllanthus emblica plant (PEP) extract. X-ray diffraction analysis (XRD), X-ray photoelectron spectroscopy (XPS), scanning electron microscopy (SEM), and Fourier transform infrared (FTIR) were used to analyze the synthesized ZnO-NSs. Evaluation of the antibacterial activity of biosynthesized ZnO-NSs was performed. ZnO-NSs exhibit effective antibacterial activity against Gram-positive (S. pyogenes and S. aureus) and Gram-negative (S. typhi and E. coli) bacterial strains. S. typhi is the most sensitive microbe towards ZnO-NSs and formed a 21 mm zone of inhibition (ZOI). ZnO-NSs are also tested as a photocatalyst in the degradation of methyl orange (MO) and rhodamine B (RB). The degradation rate of MO was 90%, and RB was 96% after being exposed to UV light for 120 min. The as-synthesized ZnO-NSs exhibited selective dye degradation and showed relatively better photocatalytic activity for positively charged (cationic) dyes. This work could lead to the fabrication of high-yield photocatalysts, which have the potential to degrade textile dyes from aqueous solution

Bioremediation of Neonicotinoid Pesticide, Imidacloprid, Mediated by <i>Bacillus cereus</i>

Imidacloprid, a toxic pesticide of the chloronicotinyl category, is employed extensively in agricultural fields, and its exposure causes serious health issues. Biodegradation is considered to be a green and economical approach to remediate pesticides. Herein, imidacloprid degradation efficiency of Bacillus sp. is highlighted, among which Bacillus cereus exhibited the greatest degradation; optimization of experimental variables (pH, imidacloprid and agitation time) via Box–Behnken factorial design and analysis of variance (ANOVA) revealed 92% biodegradation at the initial substrate concentration of 0.03 mM, aerobically in 11 days under favorable pH 7. The subsequent metabolites, identified through liquid chromatography–mass spectrometry, were 5-hydroxy imidacloprid, imidacloprid-guanidine and 6-chloronicotinic acid

Production of Extracellular Lipase by Bacillus halotolerans from Oil-Contaminated Soil in a Pilot-Scale Submerged Bioreactor

Microbial lipases are the biocatalyst of choice for the present and future because of their characteristics, including their ability to remain active as an enzyme throughout a broad pH, temperature, and substrate range. The goal of the current investigation was to find novel sources of substrates and isolates from soil contaminated by oil for the synthesis of lipase. On tributyrin media, 10 lipolytic bacterial strains that were isolated from oil-contaminated soil were grown. Using the zone of clearance, it was possible to identify the isolates with the highest activity. Following phylogenetic tree analysis, molecular characterization of the 16S rRNA sequence of the bacterial isolates revealed that it was Bacillus halotolerans (VSH 09). The enzyme was purified to near homogeneity. The enzyme activity was found to be optimum at a pH of 7.0 and a temperature of 35 &deg;C. While Ni2+ and Cu2+ had no effect, the presence of Mg2+ and Ca2+ exhibited the highest levels of enzyme activity. At 1%, tributyrin as a substrate exhibited its highest level of activity. The molecular weight, as determined by SDS-PAGE, was found to be 38 kDa. The kinetics of the enzyme were found to be 41.66 and 9.37 mg/mL for Vmax and Km, respectively. The high yield of lipase produced by this method suggests that it holds potential for production on a large scale and could be used for various biotechnological applications