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1.
Ultrason Sonochem ; 93: 106289, 2023 Feb.
Article in English | MEDLINE | ID: mdl-36638651

ABSTRACT

Currently, the polluted wastewater discharged by industry accounts for the major part of polluted bodies of water. As one of the industrial wastewaters, dye wastewater is characterized by high toxicity, wide pollution, and difficulty in decolorization degradation. In this paper, a novel composite nanomaterial catalyst of silver was prepared by using Angelica sinensis polysaccharide (ASP) as a reducing and stabilizing agent. And the optimum reaction conditions explored are VAgNO3 = 5 mL (300 mM) and vASP = 7% (w/v) for 6 h at 90 °C. In addition, the ASP-Ag nanocatalyst was characterized by several techniques. The results demonstrated that ASP-Ag nanoparticles were successfully synthesized. Degradation rate, which provides a numerical visualization of the percentage reduction in pollutant concentration. With the wrapping of ASP, the ultrasonic catalytic degradation rates of different organic dyes including rhodamine B (RB), methylene blue (MB), and methyl orange (MO) were from 88.2%, 88.7%, and 85.2% to 96.1%, 95.2% and 93.5% at room temperature, respectively. After the experiments, when cdyes = 10 mg/L, the highest degradation rate can be observed under cAPS-AgNPs = 10 mg/L with the most powerful cavitation frequency f = 59 kHz. The effect of ultrasonic frequency on the acoustic pressure distribution in the reactor was investigated by using COMSOL Multiphysis@ software to propose the mechanism of ultrasonic degradation and the mechanism was confirmed by OH radical trapping experiments. It indicates that OH produced by the ultrasonic cavitation effect plays a determinant role in the degradation. And then, the intermediate products of the dye degradation process were analyzed by gas chromatography and mass spectrometry (GC-MS), and the possible degradation processes of dyes were proposed. The resulting products of degradation are SO42-, NH4+, NO3-, N2, CO2 and H2O. Finally, the recycling degradation experiments showed that catalyst maintains a high degradation rate within reusing 5 cycles. Thus, this catalyst is highly efficient and recyclable.

2.
Spectrochim Acta A Mol Biomol Spectrosc ; 278: 121383, 2022 Oct 05.
Article in English | MEDLINE | ID: mdl-35597157

ABSTRACT

In this article, the interaction between six fluoroquinolones (FQs) and bovine serum albumin (BSA) was initially studied at 298 K, 303 K and 310 K respectively under simulated physiological conditions by fluorescence spectroscopy. At the same time, the sub-structural domains on BSA that may bind to FQs were investigated by molecular docking simulation technique. A combination of quantitative and qualitative approaches was used in the analysis of the binding constants, binding sites and corresponding thermodynamic parameters in the interaction system, it was found that FQs forms a complex with BSA and undergoes static quenching, which is the main cause of fluorescence quenching. The results indicated that hydrogen bonds, Van der Waals force and electrostatic interaction were the main binding forces between the complexes, it also showed that these six fluoroquinolones mainly bound to the IIA and IIIA structural domains of BSA, while DANO and SARA may be more toxic than other antibiotics. Based on Foster's non-radiative energy transfer theory, the binding distance between FQs and BSA was calculated to be less than 7 nm, indicating the existence of energy transfer between small molecule drugs and proteins. Synchronous fluorescence and UV-Vis absorption spectroscopy further confirmed that FQs can alter the secondary conformational change of BSA. Lomefloxacin has a different effect from the other five fluoroquinolone antibiotics because it causes a decrease in polarity and an increase in hydrophobicity around tryptophan residues, while the other five FQs have the opposite effect. Together, the study of FQs-BSA is of great significance to elucidate the pharmacokinetics and pharmacodynamics of FQs.


Subject(s)
Fluoroquinolones , Serum Albumin, Bovine , Anti-Bacterial Agents/pharmacology , Binding Sites , Fluoroquinolones/chemistry , Molecular Docking Simulation , Protein Binding , Serum Albumin, Bovine/chemistry , Spectrometry, Fluorescence , Thermodynamics
3.
Biotechnol Appl Biochem ; 69(2): 629-641, 2022 Apr.
Article in English | MEDLINE | ID: mdl-33650711

ABSTRACT

In this work, Fe3 O4 nanoparticles (NPs) were coated with polydopamine (PDA) to structure Fe3 O4 @PDA NPs by the spontaneous oxygen-mediated self-polymerization of dopamine (DA) in an aqueous solution of pH = 8.5. The fabricated Fe3 O4 @PDA NPs were grafted by glutaraldehyde to realize the immobilization of penicillin G acylase (PGA) under mild conditions. The carriers of each stage were characterized and investigated by transmission electron microscopy, X-ray diffraction, Fourier transform infrared, and vibrating sample magnetometry. To improve the catalytic activity and stability of immobilized PGA, the immobilization conditions were investigated and optimized. Under the optimal immobilization conditions, the enzyme loading capacity, enzyme activity, and enzyme activity recovery of immobilized PGA were 114 mg/g, 26,308 U/g, and 78.5%, respectively. In addition, the immobilized PGA presented better temperature and pH stability compared with free PGA. The reusability study ensured that the immobilized PGA showed an excellent repeating application performance. In particular, the recovery rate of immobilized PGA could reach 94.8% and immobilized PGA could retain 73.0% of its original activity after 12 cycles, indicating that the immobilized PGA exhibited a high operation stability and broad application potential in the biocatalysis field.


Subject(s)
Magnetite Nanoparticles , Nanoparticles , Penicillin Amidase , Enzyme Stability , Enzymes, Immobilized/chemistry , Glutaral/chemistry , Hydrogen-Ion Concentration , Indoles , Magnetite Nanoparticles/chemistry , Nanoparticles/chemistry , Penicillin Amidase/chemistry , Polymers , Temperature
4.
Biotechnol Appl Biochem ; 66(6): 990-998, 2019 Nov.
Article in English | MEDLINE | ID: mdl-31502318

ABSTRACT

In this work, TiO2 , which was modified by glutaraldehyde, was adopted as the carrier; the penicillin G acylase (PGA) was immobilized and the influence of immobilized conditions, such as pH of solution, the concentration of PGA, the immobilization temperature, and the reaction time, on the catalytic performance of the immobilized PGA was investigated and optimized. During this process, potassium penicillin G (PG) was chosen as substrate, and the quantity of 6-aminopenicillanic acid (6-APA) produced by PG at the temperature of 25 °C for 3 Min in neutral solution was conscripted as the evaluation foundation, indexes, containing the loading capacity (ELC), the activity (EA), and activity retention rate (EAR), were calculated based on quantities of produced 6-APA and compared with finding out the suitable conditions. Results showed that when the solution pH, PGA concentration, immobilization temperature, and reaction time were 8.0, 2.5% (v/v), 35 °C, and 24 H, respectively, ELC, EA, and EAR presented optimal values of 9,190 U, 14,969 U/g, and 88.5% relatedly. After that, the stability and reusability of immobilized PGA were studied, and the results documented that the pH resistance, thermal stability, and storage stability of immobilized PGA were significantly improved. This work provided technique support for the practical application of immobilized PGA carrier.


Subject(s)
Glutaral/metabolism , Penicillin Amidase/metabolism , Titanium/metabolism , Enzymes, Immobilized/metabolism , Glutaral/chemistry , Hydrogen-Ion Concentration , Solutions , Temperature
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