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1.
Mikrochim Acta ; 191(3): 152, 2024 Feb 22.
Article in English | MEDLINE | ID: mdl-38388755

ABSTRACT

The successful synthesis of La-doped CoFe LDH@rGO nanocomposite is reported combining the advantages of LDH and rGO and shows promising performances in electrochemical sensors. The structure of the obtained nanocomposite was investigated using Fourier transform infrared spectroscopy (FTIR), X-ray diffraction pattern (XRD), and field emission scanning electron microscope images (FE-SEM). Then, it was directly utilized to construct a carbon paste electrode (CPE) for urea detection. The electrochemical performance of the sensor was evaluated by various electrochemical methods. The La-CoFe LDH@rGO electrode exhibited excellent electrocatalytic properties, including a wide linear working range of 0.001-23.5 mM, very high sensitivity of 1.07 ± 0.023 µA µM-1 cm-2, a low detection limit of 0.33 ± 0.11 µM, and rapid response time of 5 s towards urea detection at the working potential of 0.4 V. Furthermore, the sensor displayed a high selectivity in different matrices, appropriate reproducibility, and long shelf life without activity loss during 3 months of storage under ambient conditions. Further tests were performed on serum and milk samples to confirm the capability of the proposed sensor for practical applications, demonstrating a reasonable recovery of 94.8 to 102% with an RSD value below 3%. Consequently, the synergistic effect of each component led to the good electrocatalytic activity of the modified electrode towards urea.

2.
Ultrason Sonochem ; 102: 106740, 2024 Jan.
Article in English | MEDLINE | ID: mdl-38171194

ABSTRACT

The health of all living organisms is greatly influenced by the quality of the water. Therefore, developing cost-effective, eco-friendly, and easily accessible methods is desperately needed to meet the high global demand for clean water. Recently, nanozyme-based dye degradation methods have been promising for the remediation of water pollution. In this work, peroxidase-mimic Co3O4/TiO2 nanocomposite was synthesized and characterized for its size, morphology, and crystalline structure. Colorimetric assay results showed that the peroxidase-like activity of the Co3O4/TiO2 nanocomposite was considerably enhanced compared to the pure Co3O4 NPs and TiO2 NPs. Besides excellent enzyme-mimic activity, the higher sonophotocatalytic dye degradation capability of the nanocomposite after immobilization on zeolite (Co3O4/TiO2@Ze) was also demonstrated. Under optimal conditions (pH = 5.0, 25 °C), 0.1 g/L of catalyst was able to degrade 100 % of methylene blue (MB) with 600 µM in the presence of 30 µM H2O2 within 12 min. GC/MS analysis and toxicity studies revealed less toxic metabolite production after treatment of MB with sonophotocatalytic Co3O4/TiO2@Ze. Modeling of MB degradation using artificial neural networks (ANN) with a 5:6:1 topology was successfully performed, and the results confirmed the fitness of theoretical and experimental outputs according to the calculated correlation coefficient values. The prepared nanocomposite could thus be used as a promising and highly effective catalyst for the removal of organic dyes from polluted water.


Subject(s)
Cobalt , Environmental Pollutants , Nanocomposites , Oxides , Zeolites , Zeolites/chemistry , Environmental Pollutants/analysis , Hydrogen Peroxide/analysis , Peroxidases , Nanocomposites/chemistry , Water , Neural Networks, Computer
3.
Food Chem Toxicol ; 160: 112801, 2022 Feb.
Article in English | MEDLINE | ID: mdl-34974130

ABSTRACT

In this research retrieval effects of natural yellow (NY) on the performance of carmoisine (CAR) inhibited bovine liver catalase (BLC) was studied using multispectral and theoretical methods. Kinetic studies showed that CAR inhibited BLC through competitive inhibition (IC50 value of 2.24 × 10-6 M) while the addition of NY recover the activity of CAR-BLC up to 82% in comparison with the control enzyme. Circular dichroism data revealed that NY can repair the structural changes of BLC, affected by CAR. Furthermore, an equilibrium dialysis study indicated that NY could reduce the stability of the CAR-catalase complex. The surface plasmon resonance (SPR) data analysis indicated a high affinity of NY to BLC compared to CAR and the binding of NY led to a decrease in the affinity of the enzyme to the inhibitor. On the other hand, fluorescence and molecular docking studies showed that the quenching mechanism of BLC by CAR occurs through a static quenching process, and van der Waals forces and hydrogen bonding play a crucial role in the binding of CAR to BLC. MLSD data demonstrated that NY could increase the binding energy of CAR-BLC complex from -7.72 kJ mol-1 to -5.9 kJ mol-1, leading to complex instability and catalase activity salvage.


Subject(s)
Catalase/antagonists & inhibitors , Catalase/chemistry , Curcumin/chemistry , Food Coloring Agents/chemistry , Naphthalenesulfonates/chemistry , Animals , Cattle , Circular Dichroism , Competitive Bidding , Hydrogen Bonding , Kinetics , Molecular Docking Simulation , Surface Plasmon Resonance
4.
Chemosphere ; 291(Pt 1): 133063, 2022 Mar.
Article in English | MEDLINE | ID: mdl-34848228

ABSTRACT

There are different analytical methods available for the determination of metformin, as an oral hypoglycemic and antidiabetic drug, in biological samples. However, most of these methods suffer from some drawbacks, including high-priced materials and equipment, damaging chemical reagents, time-consuming nature, and tedious operation procedures. So, in this work a new, sensitive and simple method was reported for the detection of metformine. In this regard, nanolayered manganese-calcium oxide (NL-MnCaO2) were synthesized and characterized using scanning electron microscopy (SEM), fourier transform infrared (FTIR) spectroscopy, and X-ray powder diffraction (XRD) techniques. Also, we studied the enzyme-like activity of synthesized particles and reported a bifunctional nanozyme, which performs the dual roles for peroxidase and catalase-mimicking. The results demonstrated the hindering effect of metformin on the peroxidase-mimic activity of NL-MnCaO2 and this effect was increased by raising metformin concentration. So, a sensitive fluorometric detection system was designed for the analytical assay of metformin, based on the terephthalic acid (TA)-H2O2 reaction with NL-MnCaO2. An acceptable linearity was observed between the metformin concentration and fluorescence quenching of the system in the range of 0.07-0.77 mM. Limit of detection (LOD) and limit of quantification (LOQ) were 0.17 µM and 0.96 µM, respectively. The proposed system was applied for the estimation of metformin concentration in serum samples by recoveries of 86.68-106%. So, the proposed fluorometric method provides some main advantages such as wide linear range, low detection limit, rapid detections, high sensitivity, and good practicability for the determination of metformin in biological samples.


Subject(s)
Manganese , Metformin , Calcium , Calcium Compounds , Hydrogen Peroxide , Limit of Detection , Oxides
5.
Iran J Pharm Res ; 19(1): 383-397, 2020.
Article in English | MEDLINE | ID: mdl-32922495

ABSTRACT

Lawsone (2-hydroxy-1,4-naphtoquinone; LAW), as a naphthoquinone derivative, is the biologically active component of Henna leaves. In this study, the structural and functional effects of LAW on bovine liver catalase (BLC), has been studied utilizing ultraviolet-visible (UV-vis) absorption, fluorescence, and ATR-FTIR spectroscopic techniques, and molecular docking approach. In-vitro kinetic study showed that by adding gradual concentrations of LAW, catalase activity was significantly decreased through noncompetitive inhibition mechanism. UV-vis and ATR-FTIR spectroscopic results illustrated that additional concentration of LAW lead to significant change in secondary structure of the enzyme.The fluorescence spectroscopic results at different temperatures indicated that LAW quenches the intrinsic fluorescence of BLC by dynamic mechanismand there is just one binding site for LAW on BCL. Changing the micro-environment nearby two aromatic residues (tryptophan (Trp) and tyrosine (Tyr)) were resulted from synchronous fluorescence. The thermodynamic parameters were implied that the hydrophobic bindings have a significant impress in the organization of the LAW-catalase complex. Molecular docking data in agreement with experimental results, confirmed that hydrophobic interactions are dominant. Inhibition of enzyme activity by LAW, showed that along withits helpful effects as ananti-oxidant compounds, the side effects of LAW should not be overlooked.

6.
Int J Biol Macromol ; 143: 850-861, 2020 Jan 15.
Article in English | MEDLINE | ID: mdl-31739034

ABSTRACT

Ellagic acid (ELA), as a polyphenolic natural compound and food additive, which has reported to possess anti-carcinogenic, antioxidant, antidepressant, ameliorative and anti-mutagenic effects. In the current work, the effects of ELA on the conformation and catalytic activity of catalase were investigated by using spectroscopic techniques including ultraviolet visible (UV-vis), fluorescence, synchronous fluorescence and attenuated total reflectance-Fourier transform infrared (ATR-FTIR) spectroscopy as well as molecular dynamics (MD) simulation. Kinetic studies showed that the enzymatic activity of catalase increases in the presence of ELA (almost 2-fold higher than free enzyme activity). Moreover, analysis of fluorescence data revealed two binding sites for ELA on the catalase and static type of quenching mechanism. The binding constants between ELA and catalase were obtained to be 47.35 × 107 M-1 (at 298 K) and 17.60 × 107 M-1 (at 310 K) and the binding distance was calculated to be 2.83 nm. Thermodynamic data showed that hydrogen bonds have a main role in the ELA-catalase complex formation. The best binding sites for ELA were, in the middle of ß-barrel and wrapping domain and in the middle of ß-barrel and helical domain, according to molecular docking data. MD simulation results were confirmed that ELA can increase catalase activity through increasing the distance between an upper side α-helix structure and a down side random coil structure.


Subject(s)
Catalase/chemistry , Ellagic Acid/chemistry , Molecular Docking Simulation , Molecular Dynamics Simulation , Animals , Binding Sites , Catalase/metabolism , Cattle , Ellagic Acid/metabolism , Enzyme Activation , Erythrocytes/enzymology , Hydrogen Bonding , Liver/enzymology , Molecular Structure , Protein Binding , Spectrum Analysis , Thermodynamics
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