Degradation of tetracycline by immobilized laccase and the proposed transformation pathway

Yang, Jie; Lin, Yi-Ting; Yang, Xiaodan; Ng, Tzi Bun; Ye, Xiuyun; Lin, Juan

doi:10.1016/j.jhazmat.2016.10.019

Cited by 200 publications

(67 citation statements)

References 41 publications

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“…This is presumably due to the strong electron donating aromatic amine group in sulfonamides and the phenol group in tetracyclines, which are not found in quinolones (Ding et al, 2016). However, identified tetracycline transformation intermediates suggest that the phenol group is not the primary target for laccase oxidation, and that oxygen addition, demethylation, water elimination reactions occur during laccase treatment (Llorca et al, 2015; Yang et al, 2017). For sulfonamides, increasing electronegativity of the substituents is accompanied by decreased degradation (Yang C. W. et al, 2016).…”

Section: Laccase Applications In Biodegradation Of Ppcpsmentioning

confidence: 99%

“…and Myceliophthora thermophila (recombinantly expressed in Aspergillus oryzae ) and from actinobacteria Streptomyces ipomoeae (expressed in E. coli ; Table 4). Laccases immobilized by different methods have been used for antibiotic degradation, including enzymatic membrane reactors (Nguyen et al, 2014b; Becker et al, 2016), granular activated carbon (Nguyen et al, 2016a), silica beads (Rahmani et al, 2015), oriented immobilization (Shi et al, 2014), magnetic cross-linked enzyme aggregates (Kumar and Cabana, 2016; Yang et al, 2017), and cell surface display (Chen et al, 2016). In particular, enzymatic membrane reactors (gelatin-ceramic membranes grafted with commercial T. versicolor laccase) in tetracycline degradation have been evaluated in depth with respect to membrane preparation, efficiency, kinetics, and economics (de Cazes et al, 2014, 2015; Abejón et al, 2015a,b).…”

Section: Laccase Applications In Biodegradation Of Ppcpsmentioning

confidence: 99%

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Laccases: Production, Expression Regulation, and Applications in Pharmaceutical Biodegradation

et al. 2017

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Laccases are a family of copper-containing oxidases with important applications in bioremediation and other various industrial and biotechnological areas. There have been over two dozen reviews on laccases since 2010 covering various aspects of this group of versatile enzymes, from their occurrence, biochemical properties, and expression to immobilization and applications. This review is not intended to be all-encompassing; instead, we highlighted some of the latest developments in basic and applied laccase research with an emphasis on laccase-mediated bioremediation of pharmaceuticals, especially antibiotics. Pharmaceuticals are a broad class of emerging organic contaminants that are recalcitrant and prevalent. The recent surge in the relevant literature justifies a short review on the topic. Since low laccase yields in natural and genetically modified hosts constitute a bottleneck to industrial-scale applications, we also accentuated a genus of laccase-producing white-rot fungi, Cerrena, and included a discussion with regards to regulation of laccase expression.

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Section: Laccase Applications In Biodegradation Of Ppcpsmentioning

confidence: 99%

Section: Laccase Applications In Biodegradation Of Ppcpsmentioning

confidence: 99%

Laccases: Production, Expression Regulation, and Applications in Pharmaceutical Biodegradation

et al. 2017

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“…Laccase (EC 1.10.3.2) is a copper-containing oxidase widely distributed in plants, insects, and fungi [ 26 ]. Laccase mainly catalyze the polymerization or depolymerization processes of lignin formation in plants.…”

Section: Introductionmentioning

confidence: 99%

Enhanced Performance of Magnetic Graphene Oxide-Immobilized Laccase and Its Application for the Decolorization of Dyes

et al. 2017

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In this study, magnetic graphene oxide (MGO) nanomaterials were synthesized based on covalent binding of amino Fe3O4 nanoparticles onto the graphene oxide (GO), and the prepared MGO was successfully applied as support for the immobilization of laccase. The MGO-laccase was characterized by transmission electron microscopy (TEM) and a vibrating sample magnetometer (VSM). Compared with free laccase, the MGO-laccase exhibited better pH and thermal stabilities. The optimum pH and temperature were confirmed as pH 3.0 and 35 °C. Moreover, the MGO-laccase exhibited sufficient magnetic response and satisfied reusability after being retained by magnetic separation. The MGO-laccase maintained 59.8% activity after ten uses. MGO-laccase were finally utilized in the decolorization of dye solutions and the decolorization rate of crystal violet (CV), malachite green (MG), and brilliant green (BG) reached 94.7% of CV, 95.6% of MG, and 91.4% of BG respectively. The experimental results indicated the MGO-laccase nanomaterials had a good catalysis ability to decolorize dyes in aqueous solution. Compared with the free enzyme, the employment of MGO as enzyme immobilization support could efficiently enhance the availability and facilitate the application of laccase.

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“…Laccase needs only dissolved oxygen as a co-substrate, while others need hydrogen peroxidase. Therefore, laccase might be more green option [6,7]. Furthermore, the oxidation of the phenolic compounds with laccase forms large insoluble polymers that are easily removed by filtration or sedimentation in the aqueous phase [8].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Laccase from Trametes hirsuta onto CMC Coated Magnetic Nanoparticles

Sadeghzadeh

Ghazvini

Hejazi

et al. 2020

IJE

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In this study, Fe3O4/CMC magnetic nanoparticles were synthesized through co-precipitation method. Afterward, laccase from Trametes hirsuta was immobilized onto Carboxymethyl cellulose (CMC)coated magnetic Fe3O4 nanoparticles by covalent bonding between carboxyl groups of carboxymethyl cellulose and amine group of laccases. Also, the resulted magnetic nanoparticles and immobilized laccase were characterized by Fourier-transform infrared spectroscopy (FTIR), scanning electron microscope (SEM) and dynamic light scattering (DLS) analysis. Moreover, the vital factors in enzyme immobilization, such as contact time, amount of N-hydroxysuccinimide (NHS), and the amount of nanoparticles were optimized, which successively 48 h, 0.01 g, and 0.0125 g were achieved for 0.01g of N-ethyl-N′-(3-dimethylaminopropyl)carbodiimide (EDC). Activity recovery of 51 ± 0.8% was achieved by optimizing the immobilization process. The results also indicated that the loading of laccase onto carboxymethyl cellulose-coated Fe3O4 nanoparticles was approximately 120 (mg/g). Finally, the immobilized laccases on magnetic support could save nearly 50% of their initial activity after five consecutive cycles.

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Degradation of tetracycline by immobilized laccase and the proposed transformation pathway

Cited by 200 publications

References 41 publications

Laccases: Production, Expression Regulation, and Applications in Pharmaceutical Biodegradation

Laccases: Production, Expression Regulation, and Applications in Pharmaceutical Biodegradation

Enhanced Performance of Magnetic Graphene Oxide-Immobilized Laccase and Its Application for the Decolorization of Dyes

Immobilization of Laccase from Trametes hirsuta onto CMC Coated Magnetic Nanoparticles

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