Negative Impact of Adjacent Coordination on Direct Electrochemistry and Enzymatic Catalysis of Laccase Immobilization onto Multi-wall Carbon Nanotubes Functionalized by Perylene Derivative

Zeng, Han; Huo, Wen Shan; Wang, Fang; Mei, Ting

doi:10.1007/s13233-019-7131-3

Cited by 6 publications

(2 citation statements)

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“…28,29 Therefore, inspired by the reported works, mesoporous silica coated magnetic multiwalled carbon nanotubes were developed and used in the enzyme immobilization process. 30 Laccase enzyme was selected as a model enzyme due to its wide range of substrates, ability to oxidize organic and some inorganic substrates, and ability to remove xenobiotics from industrial effluents as well as discoloration of dyes. In addition, compared to the peroxidase enzyme, the laccase enzyme does not need hydrogen peroxide (H 2 O 2 ) but can oxidize organic compounds with oxygen (O 2 ) as a co-substrate.…”

Section: ■ Introductionmentioning

confidence: 99%

“…Nonetheless, a major challenge is its separation from reaction mixtures and the low adsorption capacity. The magnetic functionalization is the best way for its fast, suitable, and efficient removal from reaction mixtures. , Therefore, inspired by the reported works, mesoporous silica coated magnetic multiwalled carbon nanotubes were developed and used in the enzyme immobilization process . Laccase enzyme was selected as a model enzyme due to its wide range of substrates, ability to oxidize organic and some inorganic substrates, and ability to remove xenobiotics from industrial effluents as well as discoloration of dyes.…”

Section: Introductionmentioning

confidence: 99%

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Improvement of Laccase Activity Via Covalent Immobilization over Mesoporous Silica Coated Magnetic Multiwalled Carbon Nanotubes for the Discoloration of Synthetic Dyes

et al. 2021

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Due to its environmental friendliness and biodegradable ability, the enzymatic decolorization of azo dyes is the best option. However, the free enzyme suffers from various limitations, including poor stability, no repeatable use, and a high expense, which is the key drawback for its practical use. In this analysis, the laccase enzyme was immobilized in mesoporous silica coated magnetic multiwalled carbon nanotubes (Fe 3 O 4 -MWCNTs@SiO 2 ) by a glutaraldehyde cross-linker to create an easily separable and stable enzyme. Fourier transform infrared (FTIR) spectroscopy, scanning electron microscopy (SEM), and energy-dispersive Xray spectroscopy (EDX) were used to characterize the as-synthesized Fe 3 O 4 -MWCNTs@SiO 2 . Laccase immobilized in Fe 3 O 4 -MWCNTs@SiO 2 showed a good improvement in temperature, pH, and storage stability. Moreover, the operational stability of the biocatalyst was improved, retaining 87% of its original activity even after 10 cycles of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) oxidation. The biocatalysts were applied for the decolorization of selected azo dyes without a mediator, and up to 99% of Eriochrome Black T (EBT), 98% of Acid Red 88 (AR 88), and 66% of Reactive Black 5 (RB5) were decolorized. Based on these properties, the biocatalysts can be potentially utilized in various environmental and industrial applications.

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Section: ■ Introductionmentioning

confidence: 99%