Immobilized laccase in the form of (magnetic) cross-linked enzyme aggregates for sustainable diclofenac (bio)degradation

Primožič, Mateja; Kravanja, Gregor; Knez, Željko; Crnjac, Anton; Leitgeb, Maja

doi:10.1016/j.jclepro.2020.124121

Cited by 79 publications

(32 citation statements)

References 80 publications

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“…For instance, by the preparation of cross-linked enzyme aggregates, the 3D structure of the enzyme is remarkably changed. Cross-linked laccase aggregated have been used for immobilization of the enzyme; meanwhile, the biocatalytic activity of the enzyme was preserved [50][51][52] . In order to verify the effect of any change in laccase tertiary structure, uorescence spectroscopy was employed.…”

Section: Structural Studiesmentioning

confidence: 99%

Instantaneous synthesis of organic-inorganic laccase-cobalt phosphate hybrid nanoflowers: Structural and biocatalytic characterization

Vojdanitalab

Jafari-Nodoushan

Mojtabavi

et al. 2022

Preprint

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Organic-inorganic hybrid nanoflowers (HNFs) have been synthesized by soft biomineralization procedures and are mainly used in biocatalysis and biosensing. Previously-reported methods for the synthesis of HNFs have so far required a 3-day incubation, bath sonication, or shear stress tension, which possibly introduces damage to the organic component. In this study, a novel method for instant fabrication of laccase@Co3(PO4)2•HNFs was developed without using harsh conditions. The prepared HNFs were assembled instantly by the “concentrated method,” which resulted in the fast growth of the flower-shaped nanostructures by a higher collision rate of the primary nucleation sites. The obtained results indicated that catalytic efficiency and enzymatic activity of laccase@Co3(PO4)2•HNFs were 113% and 110%, respectively, compared to the free enzyme. Also, the stability of the immobilized enzyme was enhanced by 400% in basic pH values. The activity of laccase@Co3(PO4)2•HNFs declined to 50% of the initial value after 10 reusability cycles, indicating successful immobilization of the enzyme. Structural studies revealed a 32% increase in the α-helix content after hybridization with cobalt phosphate, which improved the activity and stability of the immobilized laccase. Furthermore, the fabricated HNFs exhibited a considerable ability to remove moxifloxacin as an emerging pollutant. The antibiotic (10 mg/L) was removed by 24% and 75% after 24 h through adsorption and biodegradation mechanisms, respectively. This study introduces a new method for synthesizing HNFs, which could be used for the instant fabrication of efficient biocatalysts, biosensors, and adsorbents to be potentially employed in industrial, biomedical, and environmental applications.

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Section: Structural Studiesmentioning

confidence: 99%

Instantaneous synthesis of organic-inorganic laccase-cobalt phosphate hybrid nanoflowers: Structural and biocatalytic characterization

Vojdanitalab

Jafari-Nodoushan

Mojtabavi

et al. 2022

Preprint

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“…Alteration of the enzyme tertiary structure by one of the components required for CLEA preparation or steric hindrance within the aggregate of high particle size hampering inner A wide variety of enzymes, including hydrolases, oxidoreductases, lyases, and transferases have been used as CLEAs especially for organic synthesis [172,173], displaying enhanced stability under various conditions: protection against organic solvents [174], enhanced thermostability [175], reduced substrate inhibition [176,177], enhanced stability in acidic or alkaline conditions [178,179] or under storage [180]. Magnetic CLEAs combined the advantages of CLEAs and covalent immobilization onto Fe 3 O 4 magnetic particles and may show increased stability to changes of pH and temperature [181,182]. Enzyme cascade can also be combined as CLEAs showing enhanced thermal and pH stability [183,184].…”

Section: Cross-linked Enzyme Aggregates (Cleas)mentioning

confidence: 99%

From Enzyme Stability to Enzymatic Bioelectrode Stabilization Processes

et al. 2021

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Bioelectrocatalysis using redox enzymes appears as a sustainable way for biosensing, electricity production, or biosynthesis of fine products. Despite advances in the knowledge of parameters that drive the efficiency of enzymatic electrocatalysis, the weak stability of bioelectrodes prevents large scale development of bioelectrocatalysis. In this review, starting from the understanding of the parameters that drive protein instability, we will discuss the main strategies available to improve all enzyme stability, including use of chemicals, protein engineering and immobilization. Considering in a second step the additional requirements for use of redox enzymes, we will evaluate how far these general strategies can be applied to bioelectrocatalysis.

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“…One pharmaceutical frequently used to evaluate the efficiency of enzymatic treatment is diclofenac, which is a nonsteroidal anti-inflammatory drug. In water, diclofenac causes genetic and systemic damage to various living organisms [70,72]. Xu et al [73] employed functionalized carbon nanotubes as the support matrix for laccase to prepare a polyvinyl alcohol (PVA)/chitosan (CS)/multi-walled carbon nanotubes (MWNTs) composite nanofibrous membrane.…”

Section: Pharmaceutically Active Compoundsmentioning

confidence: 99%

Functionalized Materials as a Versatile Platform for Enzyme Immobilization in Wastewater Treatment

Kołodziejczak-Radzimska

Nghiem

Jesionowski

2021

Curr Pollution Rep

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Purpose of Review Untreated wastewater discharge can significantly and negatively impact the state of the environment. Rapid industrialization and economic development have directly contributed to land and water pollution resulting from the application of many chemicals such as organic dyes, pharmaceuticals, and industrial reagents. The removal of these chemicals before effluent discharge is crucial for environmental protection. This review aims to explore the importance of functionalized materials in the preparation of biocatalytic systems and consider their application in eliminating water pollutants. Recent Findings Wastewater treatment methods can be classified into three groups: (i) chemical (e.g., chemical oxidation and ozonation), (ii) physical (e.g., membrane separation and ion exchange), and (iii) biological processes. Biological treatment is the most widely used method due to its cost-effectiveness and eco-friendliness. In particular, the use of immobilized enzymes has recently become more attractive as a result of scientific progress in advanced material synthesis. The selection of an appropriate support plays an important role in the preparation of such biologically active systems. Recent studies have demonstrated the use of various materials for enzyme immobilization in the purification of water. Summary This review identifies and discusses different biocatalytic systems used in the enzymatic degradation of various water pollutants. Materials functionalized by specific groups can serve as good support matrices for enzyme immobilization, providing chemical and thermal stability to support catalytic reactions. Enzymatic biocatalysis converts the pollutants into simpler products, which are usually less toxic than their parents. Due to immobilization, the enzyme can be used over multiple cycles to reduce the cost of wastewater treatment. Future studies in this field should focus on developing new platforms for enzyme immobilization in order to improve degradation efficiency.

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Immobilized laccase in the form of (magnetic) cross-linked enzyme aggregates for sustainable diclofenac (bio)degradation

Cited by 79 publications

References 80 publications

Instantaneous synthesis of organic-inorganic laccase-cobalt phosphate hybrid nanoflowers: Structural and biocatalytic characterization

Instantaneous synthesis of organic-inorganic laccase-cobalt phosphate hybrid nanoflowers: Structural and biocatalytic characterization

From Enzyme Stability to Enzymatic Bioelectrode Stabilization Processes

Functionalized Materials as a Versatile Platform for Enzyme Immobilization in Wastewater Treatment

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