Health related and environmental side effects associated with conventional chemical coagulants used in water treatment has prompted the search for natural alternatives, especially of plant origin. This study investigated the water coagulation activities of a purified protein from Moringa oleifera seeds on the water from Opa reservoir of Obafemi Awolowo University, Ile-Ife. M. oleifera coagulant protein (MoCP) was purified via ion exchange and gel filtration chromatography respectively. Subunit and native molecular weight as determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration was 14.2 kDa and 30.3 kDa respectively. Modified jar test was used to investigate the coagulation activity of the purified protein in comparison to that of conventional chemical coagulant (aluminium sulphate). MoCP significantly reduced turbidity (p < 0.05) and organic load which contributed to about 58.18% reduction in total coliform of treated water. MoCP also elicited promising antimicrobial activity against bacterial isolates in the water from Opa reservoir.
Highlights Purification of Moringa oleifera seed lectin (MoL) was achieved by ammonium sulfate precipitation and size exclusion chromatography MoL hemagglutinating activity was thermostable up to 90°C, within pH 2-4 and moderately inhibited by sucrose and fructose Traces of Ca2+, Mg2+, and Na+ was detected in MoL, and modification of arginine and tryptophan residues affected the hemagglutinating activity Hemolytic (membrane-perturbing) activity of MoL was potentiated in mildly acidic pH, and dependent on concentration, temperature, pH, and time of incubation.
This study investigated the larvicidal activity on Culex quinquefasciatus of lectin purified from fresh fruiting bodies of woodland mushroom, Agaricus semotus. A. semotus lectin (ASL) was purified via ion-exchange chromatography on DEAE-cellulose A-25 and size exclusion chromatography on Sephadex G-100 matrix. Molecular weight (16.6 kDa) was estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The effects of temperature, pH, metal chelation- and larvicidal activity of ASL were also investigated. The ASL indifferently agglutinated the erythrocytes of the human ABO blood system and was stable at acidic pH and below 50 °C whereas 66% of its activity was lost at 60 °C with complete inactivation at 70 °C. ASL is a metalloprotein requiring barium ion as chelation of metals by 50 mM EDTA rendered the lectin inactive, while the addition of BaCl2, among other metal salts, restored the activity. ASL showed larvicidal activity against C. quinquefasciatus larvae after 24 h with a mortality of 5 and 95% at 5 and 25 mg/mL respectively, and LC50 of 13.80 mg/mL. This study concluded that purified A. semotus lectin showed impressive larvicidal activity, which could be exploited in its development as an insecticidal agent.
Microbial infections and antibiotic resistance are two of the most serious threats to society's health today. Millions of people die each year as a result of microbial infections. In 2020, the COVID-19 pandemic caused by viral infections was responsible for the highest amount of all deaths that year. Existing antimicrobial drugs have become less effective, if not ineffective, as a result of the emergence of resistance. Several antibiotic resistance-fighting strategies have been proposed in recent years. One strategy proposed to achieve this objective has been to use combination therapy which appears to restore the desired antimicrobial activity. Several medicinal plants have demonstrated therapeutic effects against pathogens that cause human infections due to their phytochemicals constituents which have been elucidated to act as antimicrobial agents. This chapter focuses on phytochemicals as antimicrobial agents, giving information about infectious diseases and the pathobiology of these diseases. Also, the mechanisms of antimicrobial activity of phytochemical were discussed.
The whole world is still challenged with COVID-19 pandemic caused by Coronavirus-2 (SARS-CoV-2) which has affected millions of individuals around the globe. Although there are prophylactic vaccines being used, till now, there is ongoing research into discovery of drug candidates for total eradication of all types of coronaviruses. In this context, this study sought to investigate the inhibitory effects of six selected tropical plants against four pathogenic proteins of Coronavirus-2. The medicinal plants used in this study were selected based on their traditional applications in herbal medicine to treat COVID-19 and related symptoms. The biological activities (antioxidant, free radical scavenging, and anti-inflammatory activities) of the extracts of the plants were assessed using different standard procedures. The phytochemicals present in the extracts were identified using GCMS and further screened via in silico molecular docking. The data from this study demonstrated that the phytochemicals of the selected tropical medicinal plants displayed substantial binding affinity to the binding pockets of the four main pathogenic proteins of Coronavirus-2 indicating them as putative inhibitors of Coronavirus-2 and as potential anti-coronavirus drug candidates. The reaction between these phytocompounds and proteins of Coronavirus-2 could alter the pathophysiology of COVID-19, thus mitigating its pathogenic reactions/activities. In conclusion, phytocompounds of these plants exhibited promising binding efficiency with target proteins of SARS-COV-2. Nevertheless, in vitro and in vivo studies are important to potentiate these findings. Other drug techniques or models are vital to elucidate their compatibility and usage as adjuvants in vaccine development against the highly contagious COVID-19 infection.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.