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Hydroxychloroquine in addition azithromycin earlier treating gentle COVID-19 inside outpatient environment: the randomized, double-blinded, placebo-controlled clinical trial analyzing popular settlement.
According to these results of the immobilized phytase, it could be used in some industrial applications such as animal feed, agriculture, pharmaceutical area, and food industry.Lipase is a versatile enzyme found in microorganisms, animals and plants. It has applications in a wide variety of fields ranging from the food industry to the pharmaceutical. For these applications, mainly microbial lipases are exploited in great detail. On the other hand lipases from the plant source have been characterized to a much lesser extent. Although many plant lipase sequences have been reported in UniProtKB, till date there is no report on the crystal structure of any plant lipase. In view of very limited availability of structural information on plant lipases, in this study, we modeled the three-dimensional structure of seven plant lipases and studied the conformational changes under four different solvents at two different temperatures. Most lipases have a lid domain and its movement is implicated in the interfacial activation of lipases. Among the 56 conditions tested in this study, some lipases at certain condition exhibit the lid domain movement thus implying the functional importance. Laborious purification and minimal yield are the likely reasons for poor characterization of plant lipases. In this scenario, the results of computational studies on plant lipases under different environmental conditions will provide useful data for subsequent in vitro functional studies.Treatment of non-healing skin wounds infected with extensively drug-resistant (XDR) bacteria remains as a big challenge. To date, different biomaterials have been applied for treatment of post-wound infections, nevertheless their efficacy for treatment of the wounds infected with XDR isolates has not been determined yet. In this study, the potential of the thermo-responsive chitosan (TCTS) hydrogel for protection of full-thickness wounds XDR bacteria isolated from burn patients was evaluated both in vitro and in vivo in a rat model. Antibacterial activity of the TCTS hydrogel against standard strain and clinical isolates of Acinetobacter baumannii, cytobiocompatibility for Hu02 fibroblast cells, degradation rate and swelling ratio were determined in vitro. Selleckchem LY450139 MTT assay and disk diffusion test indicated no detectable cytotoxicity and antibacterial activity in vitro, respectively. In vivo study showed significant acceleration of wound healing, re-epithelialization, wound closure, and decreased colony count in the TCTS hydrogel group compared with control. This study suggests TCTS hydrogel as an excellent wound dressing for management of the wounds infected with XDR bacteria, and now promises to proceed with clinical investigations.Carboxymethylation of Cassia obtusifolia galactomannan was carried out by Williamsons synthesis. Modification of galactomannan was confirmed by Fourier-transform infrared and 1H-Nuclear magnetic resonance spectroscopy. The degree of carboxymethyl substitution was found to be 1.69. Carboxymethylation was observed to increase the powder flow, solubility and swelling, while decrease the viscosity and alter the compression characteristics from elastic to plastic. The results of X-ray diffraction and scanning electron microscopy studies indicated increase in degree of crystallinity. The modified gum was used for preparing diclofenac sodium-loaded, Ca2+-gelled beads which were coated with gastroresistant Eudragit-L100. The formulation of beads was optimized using central composite experimental design. The optimal formulation of beads contained carboxymethylated Cassia galactomannan-2.85%,w/v and calcium chloride -15%,w/v, which showed yield -185.4%, entrapment-95.41% and release of 93.32% of diclofenac over 24 h. The release of diclofenac followed first-order kinetics by Super case-II transport. Thus, carboxymethyl Cassia galactomannan appears suitable for sustained drug delivery.Rv2966c is a highly specific methyltransferase that methylates G966 at the N2 position in 16S rRNA of mycobacterial ribosome and can be secreted inside the host cell to methylate host DNA. However, how the secreted protein retains its structure and function in the harsh environment of host cell, remains unclear. In this work, we investigate structural features of Rv2966c at pH 4.0 and pH 7.5 by far-UV- and near-UV-circular dichroism (CD) and fluorescence spectroscopy, to gain insights into its folding and stability at the acidic pH, that it is likely to encounter inside the macrophage. We show that Rv2966c exists in a compact, folded state at both pH 7.5 and pH 4.0, a result corroborated by molecular dynamics simulations as a function of pH. In fact, Rv2966c was found to be more stable at pH 4.0 than pH 7.5, as evidenced by thermal-induced CD and nanodifferential scanning fluorimetry, and urea-induced denaturation measurements. Interestingly, unlike pH 7.5 (two-state unfolding), denaturation of Rv2966c at pH 4.0 occurs in a biphasic (N ↔ X ↔ U) manner. Further spectroscopic characterization of 'X' state, identifies characteristics of a molten globule-like intermediate. We finally conclude that Rv2966c maintains a compact folded state at pH 4.0 akin to that at pH 7.5 but with higher stability.β-Aminobutyric acid (BABA) can be widely used in the preparation of anti-tumor drugs, AIDS drugs, penicillin antibiotics, and plant initiators. However, the efficient, economical, and environmentally friendly production of BABA still faces challenges. Its important production enzyme, aspartase, catalyzes the substrate crotonic acid, and depends on harsh conditions, such as high temperatures and the presence of strong alkali. Here, we modified the surface charge of the enzyme to enable it to become more negatively charged (K19E, N87E, N125D, S133D, Q262E, and N451E; from -60 to -80), reducing its optimal pH from 9.0 to 8.0. The M20 enzyme showed improved specific activity (400.21 mU/mg at pH 8.0; 2.47-fold that of aspartase), and at pH 7.0, its activity increased 3-fold. The thermal stability of the enzyme was also improved. For the production of BABA, a 500 g/L whole-cell transformation was obtained with a 1.41-fold increase in yield, and the final production of BABA reached 556.1 g/L within 12 h. Our method provides a new strategy for modifying the characteristics of the enzyme through the modification of its surface charge, which also represents the first modification of the optimal pH for aspartase.The radiological toxicity of uranium in nuclear industrial wastewater poses a long-term threat to environment, thus the effective separation of radionuclide from wastewater is very important for environmental safety. Herein, the macroporous ion-imprinted chitosan foams (ICFs) were synthesized by the combination of the facile freezing-drying and ion-imprinting techniques. Compared with non-imprinted chitosan foam, the ICFs showed much higher adsorption capacities (qm = 248.9-253.6 mg/g) and better adsorption selectivity for U(VI) owing to their smart recognition of the target ions for matching the cavities formed during U(VI)-imprinting process. The adsorption kinetics could be fitted by pseudo-second-order model; whereas the adsorption isotherms could be described by Langmuir model, indicating chemisorption or complexation mechanism. The FT-IR and XPS analysis further confirms that the coordination between U(VI) and the active sites (amine and hydroxyl groups) is the main adsorption mechanism. The thermodynamic parameters suggest that the adsorption of U(VI) is endothermic and spontaneous. This work provides new insights for the design of novel macroporous biosorbents with both high adsorption capacity and excellent adsorption selectivity for U(VI) biosorption from wastewater.Endoglucanases provide an attractive avenue for the bioconversion of lignocellulosic materials into fermentable sugars to supply cellulosic feedstock for biofuels and other value-added chemicals. Thermostable endoglucanases with high catalytic activity are preferred in practical processes. link2 To improve the thermostability and activity of the thermostable β-1,4-endoglucanase CTendo45 isolated from the thermophilic fungus Chaetomium thermophilum, structure-based rational design was performed by using site-directed mutagenesis. When inactivated mutation of the unique N-glycosylation sequon (N88-E89-T90) was implemented and the conserved Y173 residue was substituted with phenylalanine, a double mutant T90A/Y173F demonstrated enzymatic activity that dramatically increased 2.12- and 1.82-fold towards CMC-Na and β-D-glucan, respectively. Additionally, T90A/Y173F exhibited extraordinary heat endurance after 300 min of incubation at elevated temperatures. This study provides a valid approach to the improvement of enzyme redesign protocols and the properties of this endoglucanase mutant distinguish it as an excellent candidate enzyme for industrial biomass conversion.A zein-degrading protease (ZDP) from Zea mays was heterologously expressed using Pichia pastoris and its characteristics and effects on enzymatic hydrolysis of corn starch were investigated in the current study. The optimal temperature and pH for ZDP activity was 40 °C and pH 5.0, respectively. The ZDP exhibited a degree of thermal stability and was repressed by some metal ions (5 mM) including Zn2+, Mg2+, Cu2+, Mn2+, Ni2+, K+, and Ca2+, especially Mn2+ and Cu2+, which caused near complete inhibition. Dithiothreitol and β-mercaptoethanol (5 mM) could tremendously increase the ZDP activity by 102.1% and 60.7%, respectively. The ZDP could not tolerate organic solvents such as ethanol, acetone, and dimethyl sulphoxide. The ZDP could efficiently degrade the pure commercial zein and the native zein in the corn, increase the leaching of corn soluble sugars, destroy the cross-linked starch-zein structure, and release the starch granules, consequently increasing the α-amylase hydrolysis of corn starch. The recombinant ZDP might be useful to improve the utilization of corn.A biogenic mesoporous silica nanoparticles (MSNs)-based nanocarrier has been used for improving the stability and recyclability of PersiXyn2 as a recombinant xylanase enzyme. The biogenic MSNs (called RKIT-6 henceforth) were synthesized via a soft templating method using rice husk biomass as a renewable silica source. Then bis-(2-aminoethyl) ether modified RKIT-6 (denoted as bis-AE@RKIT-6) was prepared through the furnishing surface with bis-(2-aminoethyl) ether, as a pendant anchoring agent to immobilize PersiXyn2. The nanomaterials were characterized using nitrogen adsorption-desorption isotherms, atomic force microscopy (AFM), X-ray diffraction (XRD), molecular docking (MD) study, and thermogravimetric analysis (TGA). After immobilizing, PersiXyn2@bis-AE@RKIT-6, the optimal temperature of enzyme performance was improved more than 10 °C in comparison with the free enzyme. Such a way that PersiXyn2@bis-AE@RKIT-6 sample could maintain 90% of its maximum activity at the range of 30-60 °C. PersiXyn2@bis-AE@RKIT-6 also enhanced the degradation of lignocellulosic agro-waste (rice straw) and reducing sugar production up to 35% in comparison to the free enzyme. link3 Moreover, PersiXyn2@bis-AE@RKIT-6 could be recycled for ninth runs with a reasonable decrease in its activity. This study presents an efficient nano-biocatalyst which in a more comprehensive sense can be considered as a promising candidate in the fields of animal feed and lignocellulosic biomasses saccharification.
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