A robust biocatalyst based on laccase immobilized superparamagnetic Fe3O4@SiO2–NH2 nanoparticles and its application for degradation of chlorophenols

Chen, Zhihui; Yao, Jun; Ma, Bo; Liu, Bang; Kim, Jonghyok; Li, Hao; Zhu, Xueyan; Zhao, Chenchen; Amde, Meseret

doi:10.1016/j.chemosphere.2021.132727

Cited by 42 publications

(17 citation statements)

References 39 publications

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“…The higher biodegradation efficiency of 2,4-DCP in wastewater samples (Tables 3 and 4) was detected using immobilized enzymes than that of free enzymes and cells. These results are in line with Zhang et al [47] and Chen et al [48], who applied laccases immobilized in nanomaterials for the biodegradation of chlorophenol. Another study found that laccases (free or immobilized) demonstrated high biotransformation of 2,4-dinitrophenol in soil [8].…”

Section: Discussionsupporting

confidence: 91%

2,4-Dichlorophenol biotransformation using immobilized marine halophilic Bacillus subtilis culture and laccase enzyme: application in wastewater treatment

Farag

El-Naggar

Ghanem

2022

Journal of Genetic Engineering and Biotechnology

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Background 2,4-Dichlorophenol (2,4-DCP) is a very toxic aromatic compound for humans and the environment and is highly resistant to degradation. Therefore, it is necessary to develop efficient remediation and cost-effective approaches to this pollutant. Microbial enzymes such as laccases can degrade phenols, but limited information is known about immobilized bacterial laccase and their reuse. Methods Immobilization of marine halophilic Bacillus subtilis AAK cultures via entrapment and adsorption techniques and degradation of different phenolic compounds by immobilized cells were estimated. Partial purification and immobilization of laccase enzymes were carried out. In addition, the biodegradation of 2,4-DCP and others contaminated by wastewater was investigated. Results Immobilization of cells and partially purified laccase enzymes by adsorption into 3% alginate increased 2,4-DCP biotransformation compared with free cells and free enzymes. In addition, the reuse of both the immobilized culture and laccase enzymes was evaluated. The highest removal of 2,4-DCP from pulp and paper wastewater samples inoculated by immobilized cells and the immobilized enzyme was 90% and 95%, respectively, at 50 h and 52 h of incubation, compared to free cells and free enzyme. Conclusion The results of this study have revealed the immobilization of a biocatalyst and its laccase enzyme as a promising technique for enhancing the degradation of 2,4-DCP and other toxic phenolic and aromatic compounds. The reuse of the biocatalyst and its laccase enzyme enabled the application of this cost-effective bioremediation strategy.

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Section: Discussionsupporting

confidence: 91%

2,4-Dichlorophenol biotransformation using immobilized marine halophilic Bacillus subtilis culture and laccase enzyme: application in wastewater treatment

Farag

El-Naggar

Ghanem

2022

Journal of Genetic Engineering and Biotechnology

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“…Stability is an important indicator to evaluate the industrial application of laccase [ 50 ]. During the determination of thermal stability, the free and immobilized laccases were placed at 60 °C for some time, and the laccase activities were measured every hour, defining the initial laccase activity to 100%.…”

Section: Methodsmentioning

confidence: 99%

Magnetic Polyethyleneimine Nanoparticles Fabricated via Ionic Liquid as Bridging Agents for Laccase Immobilization and Its Application in Phenolic Pollutants Removal

et al. 2022

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In this study, polyethyleneimine was combined with magnetic Fe3O4 nanoparticles through the bridging of carboxyl-functionalized ionic liquid, and laccase was loaded onto the carrier by Cu2+ chelation to achieve laccase immobilization (MCIL–PEI–Cu–lac). The carrier was characterized by Fourier transform infrared spectroscopy, scanning electron microscope, thermogravimetric analysis, X-ray diffraction analysis, magnetic hysteresis loop and so on. MCIL–PEI–Cu–lac has good immobilization ability; its loading and activity retention could reach 52.19 mg/g and 91.65%, respectively. Compared with free laccase, its thermal stability and storage stability have been significantly improved, as well. After 6 h of storage at 60 °C, 51.45% of the laccase activity could still be retained, and 81.13% of the laccase activity remained after 1 month of storage at 3 °C. In the pollutants removal test, the removal rate of 2,4-dichlorophenol (10 mg/L) by MCIL–PEI–Cu–lac could reach 100% within 10 h, and the removal efficiency could still be maintained 60.21% after repeated use for 8 times. In addition, MCIL–PEI–Cu–lac also has a good removal effect on other phenolic pollutants (such as bisphenol A, phenol, 4-chlorophenol, etc.). Research results indicated that an efficient strategy for laccase immobilization to biodegrade phenolic pollutants was developed.

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“…The removal efficiency of BPA by Fe-Cu-MPC, Fe-Cu-MPC@Lac and free laccase was investigated. First, 25 mg of different forms of laccase were respectively added to the 50 mL of 40 mg L −1 BPA solution, namely pure carrier material without laccase (0 U mL −1 ), immobilized enzyme (0.3 U mL −1 ) and free enzyme (0.5 U mL −1 ), and shaken in the constant temperature oscillator (200 rpm, 45 °C) for 5 h. 12,48 At the reaction time points of 0.5, 1.0, 1.5, 2.0, 2.5, 3.0, 4.0 and 5.0 h, 2 mL BPA solution was taken and filtered into the sample bottle with disposable 0.45-μm microporous membrane. The BPA concentration was measured by high performance liquid chromatography (HPLC) with a C18 column (4.6 × 250 mm, 5 μm).…”

Section: Bpa Removal Experimentsmentioning

confidence: 99%

“…9 Studies have shown that laccase has a good catalytic capacity to oxidize a variety of substrates, including a range of phenols, aromatic compounds and other persistent organic pollutants, such as phenol, chlorophenol, phenanthrene and anthracene. [10][11][12][13] 13 Because laccase only requires the presence of molecular oxygen (O 2 ) to react with the substrate, and the only product after the reaction is water, laccase also is known as a "green catalyst", offering a sustainable bioremediation technology for solving environmental problems such as industrial wastewater treatment and soil remediation. 14,15 Nevertheless, there are many problems with practical applications for free laccase, such as poor stability, and its activity is easily affected by unfavorable external environmental factors, leading to degeneration and inactivation.…”

Section: Introductionmentioning

confidence: 99%

Laccase immobilization on bimetallic MOF‐derived porous carbon materials for the removal of bisphenol A

Song

Ren

Wang

et al. 2022

J of Chemical Tech & Biotech

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As a result of the poor mechanical properties of most metal-organic frameworks (MOFs), they are liable to dissociate in water and thus cannot maintain immobilized enzyme activity. In this paper, a magnetic porous carbon material (Fe-Cu-MPC) with good stability was prepared by high temperature carbonization using a bimetallic Fe-Cu-MOF precursor, and used to immobilize laccase by a simple and rapid adsorption-crosslinking method. Optimized by the response surface method, optimal conditions for the immobilization of laccase on Fe-Cu-MPC were obtained as follows: enzyme concentration 1.275 mg mL −1 , immobilization time 32 min, and pH 4.7. Under the optimal preparation conditions, the activity of the immobilized laccase obtained was 0.63 U mg −1 , with activity recovery of 63.13%. The enzyme loading was 189.03 mg g −1 and the immobilization yield was 74.13%. Compared with free laccase, Fe-Cu-MPC@Lac showed stronger tolerance to temperature and pH, and had better thermal stability and storage stability. The removal of BPA by immobilized laccase was studied, showing that the removal effect of Fe-Cu-MPC@Lac on BPA was much higher than that of free laccase. Within 5 h, the BPA removal amount of Fe-Cu-MPC@Lac (0.34 mmol g −1 ) was two-fold that of free laccase (0.14 mmol g −1 ), and the BPA removal rate reached 41.35% after ten cycles. Finally, based on the intermediates identified by gas chromatography-mass spectrometry, two possible degradation pathways of BPA were proposed. Studies have shown that Fe-Cu-MPC is an excellent carrier and Fe-Cu-MPC@Lac has great potential in the treatment of BPA containing wastewater.

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A robust biocatalyst based on laccase immobilized superparamagnetic Fe3O4@SiO2–NH2 nanoparticles and its application for degradation of chlorophenols

Cited by 42 publications

References 39 publications

2,4-Dichlorophenol biotransformation using immobilized marine halophilic Bacillus subtilis culture and laccase enzyme: application in wastewater treatment

2,4-Dichlorophenol biotransformation using immobilized marine halophilic Bacillus subtilis culture and laccase enzyme: application in wastewater treatment

Magnetic Polyethyleneimine Nanoparticles Fabricated via Ionic Liquid as Bridging Agents for Laccase Immobilization and Its Application in Phenolic Pollutants Removal

Laccase immobilization on bimetallic MOF‐derived porous carbon materials for the removal of bisphenol A

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