Preparation of a novel multi-walled-carbon-nanotube/cordierite composite support and its immobilization effect on horseradish peroxidase

Li, Z.L.; Cheng, Li; Zhang, L.W.; Liu, W.; Ma, Weiqian; Liu, L.

doi:10.1016/j.psep.2017.02.021

Cited by 27 publications

(8 citation statements)

References 15 publications

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“…Results showed that the immobilized JP retained 45% of its relative activities at 90 min, while free enzyme experienced a huge loss of its activity under similar operating parameters. Besides, previous studies also confirmed the enhancement of thermal stability of enzymes after immobilization 43 . The strong covalent interaction between the enzyme molecules to the BP/PVA membrane support improved the thermal stability of immobilized enzymes.…”

Section: Resultsmentioning

confidence: 55%

Immobilization of Peroxidase on Functionalized MWCNTs-Buckypaper/Polyvinyl alcohol Nanocomposite Membrane

Jun

Mubarak

Yon

et al. 2019

Sci Rep

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Surface modified Multi-walled carbon nanotubes (MWCNTs) Buckypaper/Polyvinyl Alcohol (BP/PVA) composite membrane was synthesized and utilized as support material for immobilization of Jicama peroxidase (JP). JP was successfully immobilized on the BP/PVA membrane via covalent bonding by using glutaraldehyde. The immobilization efficiency was optimized using response surface methodology (RSM) with the face-centered central composite design (FCCCD) model. The optimum enzyme immobilization efficiency was achieved at pH 6, with initial enzyme loading of 0.13 U/mL and immobilization time of 130 min. The results of BP/PVA membrane showed excellent performance in immobilization of JP with high enzyme loading of 217 mg/g and immobilization efficiency of 81.74%. The immobilized system exhibited significantly improved operational stability under various parameters, such as pH, temperature, thermal and storage stabilities when compared with free enzyme. The effective binding of peroxidase on the surface of the BP/PVA membrane was evaluated and confirmed by Field emission scanning electron microscopy (FESEM) coupled with Energy Dispersive X-Ray Spectroscopy (EDX), Fourier transform infrared spectroscopy (FTIR) and Thermogravimetric Analysis (TGA). This work reports the characterization results and performances of the surface modified BP/PVA membrane for peroxidase immobilization. The superior properties of JP-immobilized BP/PVA membrane make it promising new-generation nanomaterials for industrial applications.

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Section: Resultsmentioning

confidence: 55%

Immobilization of Peroxidase on Functionalized MWCNTs-Buckypaper/Polyvinyl alcohol Nanocomposite Membrane

Jun

Mubarak

Yon

et al. 2019

Sci Rep

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“…The improved immobilization yield and reusability of the SnO 2 nanotube-bound enzymes indicate that these hollow nanotubes are promising supports for enzyme immobilization. In addition, enzymes immobilized on SnO 2 hollow nanotubes exhibited higher loadings and improved properties compared to enzymes immobilized on carbon nanotubes 35 , 38 , 39 . Given the improved biochemical properties and stability of the immobilized enzymes, it is reasonable to expect that the SnO 2 hollow nanotubes would also be a promising candidate for the immobilization of various important enzymes for industrial applications.…”

Section: Introductionmentioning

confidence: 97%

SnO2 hollow nanotubes: a novel and efficient support matrix for enzyme immobilization

Anwar

Kim

Kumar

et al. 2017

Sci Rep

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A major challenge in the industrial use of enzymes is maintaining their stability at elevated temperatures and in harsh organic solvents. In order to address this issue, we investigated the use of nanotubes as a support material for the immobilization and stabilization of enzymes in this work. SnO2 hollow nanotubes with a high surface area were synthesized by electrospinning the SnCl2 precursor and polyvinylpyrrolidone (dissolved in dimethyl formamide and ethanol). The electrospun product was used for the covalent immobilization of enzymes such as lipase, horseradish peroxidase, and glucose oxidase. The use of SnO2 hollow nanotubes as a support was promising for all immobilized enzymes, with lipase having the highest protein loading value of 217 mg/g, immobilization yield of 93%, and immobilization efficiency of 89%. The immobilized enzymes were fully characterized by various analytical methods. The covalently bonded lipase showed a half-life value of 4.5 h at 70 °C and retained ~91% of its original activity even after 10 repetitive cycles of use. Thus, the SnO2 hollow nanotubes with their high surface area are promising as a support material for the immobilization of enzymes, leading to improved thermal stability and a higher residual activity of the immobilized enzyme under harsh solvent conditions, as compared to the free enzyme.

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“…Many procedures in the literature enable modification of MWCNT aimed at improvement of its bio-capability with biological species [33]. Thus, MWCNT is very often used in the deposition of biorecognition layers, especially laccase [34,35], lipase [36][37][38][39], hemoglobin [33,40], glucose oxidase [41] and horseradish peroxidase [42][43][44].…”

Section: Introductionmentioning

confidence: 99%

Theoretical insight into plasma deposition of laccase bio-coating formation

Malinowski

Jaroszyńska-Wolińska

Herbert³

2019

J Mater Sci

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Development of new techniques for deposition of biologically active coatings in the form of bio-recognition layers in biosensor construction is a current technological challenge. Biosensors are widely applied in environmental protection in determination of hazardous materials, e.g., catechol, hydrochinon or resorcinol. Application of a soft plasma polymerization (SPP) technique by lowenergy-density corona discharge has allowed significant simplification of the deposition process of bio-recognition layers. However, the mechanism of the SPP process is by no means fully understood. This paper presents insights into the mechanism of binding laccase enzyme onto graphene oxide (GO) and multiwalled carbon nanotubes (MWCNT) through analysis carried out by density functional theory (DFT) methods and Fourier transform infrared spectroscopy (FTIR). The objective was to examine the mechanism on the basis of binding energies and electrostatic interactions between laccase and carbon nanomaterials as well as enzyme structure after cold plasma deposition. The lowest binding energies have been calculated for the ON bond between the arginine amino acid of laccase and the hydroxyl group of GO and the CO bond between the serine molecule of laccase and the carboxyl groups of GO and MWCNT. FTIR and DFT studies showed that the chemical structures of the laccase enzyme and carbon nanomaterials after corona jet plasma treatment are not substantially changed. Preliminary recognition of the mechanism of biosensing layer deposition by the SPP technique opens the way to application of this innovative technique to the construction of other biosensors such as for determination of pollutants in water samples.

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Preparation of a novel multi-walled-carbon-nanotube/cordierite composite support and its immobilization effect on horseradish peroxidase

Cited by 27 publications

References 15 publications

Immobilization of Peroxidase on Functionalized MWCNTs-Buckypaper/Polyvinyl alcohol Nanocomposite Membrane

Immobilization of Peroxidase on Functionalized MWCNTs-Buckypaper/Polyvinyl alcohol Nanocomposite Membrane

SnO2 hollow nanotubes: a novel and efficient support matrix for enzyme immobilization

Theoretical insight into plasma deposition of laccase bio-coating formation

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