Chitosan based metal-chelated copolymer nanoparticles: Laccase immobilization and phenol degradation studies

Alver, Erol; Metin, Ayşegül Ülkü

doi:10.1016/j.ibiod.2017.07.012

Cited by 73 publications

(28 citation statements)

References 63 publications

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“…After eight cycles of continuous use, the immobilized enzyme retained above 50% [103] Polyacrylonitrile-biochar composite nanofibrous membrane…”

Section: Immobilization System Results Referencementioning

confidence: 99%

“…Rouhani et al (2018) achieved laccase stabilization for up to 10 reaction cycles with only a 10% loss of initial activity when it was immobilized in a Graphene oxide/CuFe 2 O 4 nanocomposite for the synthesis of arylsulfonyl benzenediols [102]. Other reports show that immobilized laccase in Cu (II)-chelated chitosan-graft-poly (glycidyl methacrylate) nanoparticles and Polyacrylonitrile-biochar composite nanofibrous membrane was stable, with a loss of about 50% after 7 reaction cycles [103,104]. Good results in terms of stability and activity have also been reported after immobilizing laccase in other kinds of more conventional materials.…”

Section: Laccase Immobilizationmentioning

confidence: 97%

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Dioxygen Activation by Laccases: Green Chemistry for Fine Chemical Synthesis

2018

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Laccases are enzymes with attractive features for the synthesis of fine chemicals. The friendly reaction conditions of laccases and their high conversion and selectivity make them particularly suitable for green methods of synthesis. In addition, laccases are enzymes with broad substrate variability, ease of production, and no need of cofactors or aggressive oxidizing agents. Among molecules oxidized by laccases are polycyclic aromatic hydrocarbons, azo dyes, pesticides, phenols, and pharmaceuticals. This article reviews the laccase-mediated oxidation of fine chemicals for the production of biologically active compounds. The main aspects of the enzymatic oxidation are summarized; potentials and limitations are identified and proposals to develop more robust catalysts are analyzed.

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“…After eight cycles of continuous use, the immobilized enzyme retained above 50% [103] Polyacrylonitrile-biochar composite nanofibrous membrane…”

Section: Immobilization System Results Referencementioning

confidence: 99%

Section: Laccase Immobilizationmentioning

confidence: 97%

Dioxygen Activation by Laccases: Green Chemistry for Fine Chemical Synthesis

2018

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“…Biocompatibility refers to the biological nature events that do not interfere with those of electronic signal transduction and vice versa. Metallic nanoparticles are promising materials that increase the electroactive area and improve the sensitivity and stability of the attached enzymes on the electrodes, bringing the enzymatic active site close to the electrode (the redox cofactor should not exceed a 20 Å distance) to achieve direct charge transfer reactions [14,[18][19][20][21][22][23].…”

Section: Covalent Immobilization Through Alkanethiol Linkersmentioning

confidence: 99%

Design of Bioelectrochemical Interfaces Assisted by Molecular Dynamics Simulations

Vidal-Limón¹,

Huerta-Miranda²,

García-García³

et al. 2021

Homology Molecular Modeling - Perspectives and Applications

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The design of bioelectrochemical interfaces (BEI) is an interesting topic that recently demands attention. The synergy between biomolecules and chemical components is necessary to achieve high molecular selectivity and sensitivity for the development of biosensors, synthesis of different compounds, or catalytic processes. For most BEI, the charge transfer process occurs in environments with particular chemical conditions; modeling these environments is a challenging task and requires multidisciplinary efforts. These interfaces can be composed of biomolecules, such as proteins, DNA, or more complex systems like microorganisms. Oxidoreductases enzymes are good candidates, among others, due to their catalytic activities and structural characteristics. In BEI, enzymes are immobilized on conductive surfaces to improve charge transfer processes. Covalent immobilization is the most common method to prolong lifetime or modulate the detection process. However, it is necessary to implement new methodologies that allow the selection of the best candidates for a more efficient design. Homology modeling of oxidoreductases combined with Molecular Dynamics (MD) simulation methods are alternative and already routinely used tools to investigate the structure, dynamics, and thermodynamics of biological molecules. Our motivation is to show different techniques of molecular modeling (Homology Modeling, Gaussian accelerated molecular dynamics, directed adaptive molecular dynamics and electrostatic surface calculations), and using horseradish peroxidase as a model to understand the interactions between biomolecules and gold nanoclusters (as current collector). Additionally, we present our previous studies considering molecular simulations and we discuss recent advances in biomolecular simulations aimed at biosensor design.

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“…4a, free and immobilized laccases exhibited the greatest activity at pH 3 and 3.5, which is probably due to the limited mobility of laccase due to ionic interactions between the enzyme and MBC. [39][40][41] Hence, in the subsequent experiments, the activity assays were all performed at pH 3.5. It was also found that the laccase immobilized on MBC had a broader range of working pH values when compared to the free laccase, suggesting that L-MBC was more favorable than free laccase at various pH conditions.…”

Section: Stability Of L-mbcmentioning

confidence: 99%