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In Ramanathapuram area, the fundamental hotspot for drinking and different purposes, for the most part, relies upon groundwater since the surface water is least and the stream water additionally not accessible during the storm season. The primary point of the work is to find the water quality index (WQI) in Ramanathapuram area by utilizing Geographical Information System (GIS). Around forty-six water specimens were gathered from the wells and examined to evaluate the groundwater quality in the investigation region. Water quality examinations of similar specimens were done for pH, total dissolved solids (TDS), fluoride (F−), Fe, ammonia (NH3), phosphate (PO), nitrate (NO3-), nitrite (NO2), alkalinity and chloride (Cl−). The water quality map for the study area was generated based on the results of forty-six observation wells. Based on the results, the study area is classified into five different categories as excellent, good, poor, very poor and water unsuitable for consumption. In this manner, continual checking of groundwater is important to save the groundwater in the future.

The P. falciparumserine repeat antigen (PfSERA5) is the most abundantly expressed protein in the parasitophorous vacuole during the asexual blood stage and serves as both drug and vaccine target. The processed central fragment (56 KDa) of PfSERA5 is implicated to play an important role in parasite exit (egress) during schizont rupture from erythrocytes. Structural characterization of its enzymatic domain supports protease-like function for this central domain. The understanding of exact functional role of PfSERA5 in parasite egress remains unconfirmed as recent studies also indicate an indispensable non-catalytic role for PfSERA5 putative enzyme domain in the blood stage. No structural insight into PfSERA5 prodomain is available. Structure prediction of PfSERA5 prodomain using in silicoapproach in our study, showed it to have structural similarity with calcium-binding proteins. An earlier observation of steep rise in intracellular calcium concentration as an important factor in egress makes the prodomain calcium-binding role significant. The implication of calcium on structure and activity of PfSERA5 putative enzyme domain is also unknown, and such information would aid to substantiating any calcium-dependent effects on PfSERA5. To understand this, we performed molecular dynamic (MD) simulation both in the presence and absence of calcium. MD results show secondary structure conformational differences in local regions of protein structure. Our results support calcium to be an important parameter for stability and function of PfSERA5. This computational assessment suggest a need to design future experiments like calcium-dependent inhibition studies to reveal exact functional role of PfSERA5 in parasite egress.

Plasmodium vivaxmalaria is geographically the most widely distributed and prevalent form of human malaria. The development of drug resistance by the parasite to existing drugs necessitates higher focus to explore and identify new drug targets. Plasmodialproteases have key roles in parasite biology and are involved in nutritional uptake, egress from infected reticulocytes, and invasion of the new target erythrocytes. Serine repeat antigens (SERA) of Plasmodiumare parasite proteases that remain attractive drug targets and are important vaccine candidates due to their high expression profiles in the blood stages. SERA proteins have a unique putative papain-like cysteine protease motif that has either serine or cysteine in its active site. In P. vivax, PvSERA4 is the highest transcribed member of this multigene family. In this study, we have investigated the genetic polymorphism of PvSERA4 central protease domain and deduced its 3D model by homology modeling and also performed MD simulations to acquire refinedprotein structure. Sequence analysis of protease domain of PvSERA4 from Indian field isolates reveals that the central domain is highly conserved. The high sequence conservation of the PvSERA4 enzyme domain coupled with its high expression raises the possibility of it having a critical role in parasite biology and hence, being a reliable target for new selective inhibitor-based antimalarial chemotherapeutics. The 3D model showed the presence of an unusual antiparallel Beta hairpin motif between catalytic residues similar to hemoglobin binding motif of Plasmodialhemoglobinases. Our PvSERA4 model will aid in designing structure-based inhibitors against this enzyme.

The recovery of rare earth elements (REEs) is a global challenge and the mining of rare earths has serious environmental implications due to the toxic waste released post mining. Hence, the rising demand for rare earths and their far reaching electronic applications necessitates an effective strategy to recover the REEs from more viable sources. In this work, the graphene oxide–Aspergillus nigerspores (GO–A. nigerspores) blend was utilized for adsorptive recovery of a precious rare earth Eu(III) and the adsorption variables like pH of the medium, adsorbent dosage, sorption kinetics, thermodynamics, and isotherm were optimized for the developed biosorbent. The adsorption process suited the Langmuir isotherm model with a maximum adsorption capacity of 147.3 mg/g. The pseudo–second–order kinetics was a perfect fit to describe the adsorption process. The results obtained through the Van’t Hoff plot show negative free energy change (ΔGº) which implies the spontaneity and the negative standard enthalpy change (ΔHº) values show that the nature of the adsorption process is exothermic. The analytical characterizations including FTIR, Raman, X-ray diffraction (XRD), X-ray photoelectron spectroscopy (XPS), Brunauer–Emmett–Teller (BET), thermal gravimetric analysis (TGA), and scanning electron microscopy–energy dispersive X-ray spectroscopy (SEM–EDX) were employed to study the biosorbent. The features of GO–A. nigerspores biosorbent was applied to recover Eu(III) from real samples such as fluorescent lamp phosphor, red phosphor powder, and a simulated radioactive waste solution.