Design-of-experiment strategy for the formulation of laccase biocatalysts and their application to degrade bisphenol A

Demarche, Philippe; Junghanns, Charles; Mazy, Nicolas; Agathos, Spiros N.

doi:10.1016/j.nbt.2012.05.023

Cited by 29 publications

(21 citation statements)

References 34 publications

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“…This typical antagonistic behavior can be explained by substrate diffusion limitation and multiple layers of immobilized enzyme [27]. Therefore, when immobilizing an enzyme, a compromise between yield and activity has to be made [9]. The thermostability response surface (Ŷ 2 ) had a saddle shape rather complex to interpret (Fig.…”

Section: Results and Discussion Laccase Immobilizationmentioning

confidence: 99%

“…One unit (U) of laccase activity corresponds to the oxidation of 1 mmol of ABTS per minute. Immobilized laccase activity was determined according to [9].…”

Section: Laccase Activity Assaymentioning

confidence: 99%

“…The formulation of the laccase biocatalyst followed the method described by [9]. Aqueous silanization of MSS was performed according to [22].…”

Section: Laccase Biocatalystmentioning

confidence: 99%

“…Conventional physicochemical or biological treatment plants can only achieve partial degradation while advanced oxidation processes such as ozonation render variable degradation yields [8]. Some oxidoreductases such as laccase (EC 1.10.3.2, benzenediol: oxygen oxidoreductase) possess the ability to oxidize various substances, mainly phenolic, and transform them into more bioavailable oxidized products or harmless and stable water-insoluble polymers [9,10]. Laccase is a multi-copper oxidase which catalyzes one-electron oxidation of phenolic molecules with the concomitant reduction of oxygen to water.…”

Section: Introductionmentioning

confidence: 99%

“…Formulation of the immobilized enzymes (hereafter called biocatalysts) is a strategic phase in the development of enzymebased bioprocesses because it can determine to a large extent the biocatalyst performance, the production yield and the cost of the process. Biocatalyst formulation based on an undefined complex laccase preparation is an empirical process which requires the use of design of experiment (DoE) methodology and mathematical modeling to be efficient [9].…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Formulation and characterization of an immobilized laccase biocatalyst and its application to eliminate organic micropollutants in wastewater

Nair¹,

Demarche²,

Agathos³

2013

New Biotechnology

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102

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Section: Results and Discussion Laccase Immobilizationmentioning

confidence: 99%

“…One unit (U) of laccase activity corresponds to the oxidation of 1 mmol of ABTS per minute. Immobilized laccase activity was determined according to [9].…”

Section: Laccase Activity Assaymentioning

confidence: 99%

“…The formulation of the laccase biocatalyst followed the method described by [9]. Aqueous silanization of MSS was performed according to [22].…”

Section: Laccase Biocatalystmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Formulation and characterization of an immobilized laccase biocatalyst and its application to eliminate organic micropollutants in wastewater

Nair¹,

Demarche²,

Agathos³

2013

New Biotechnology

Self Cite

102

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Bioinspired production of magnetic laccase‐biotitania particles for the removal of endocrine disrupting chemicals

Ardao

Magnin

Agathos

2015

Biotech & Bioengineering

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Microbial laccases are powerful enzymes capable of degrading lignin and other recalcitrant compounds including endocrine disrupting chemicals (EDCs). Efficient EDC removal on an industrial scale requires robust, stable, easy to handle and cost-effective immobilized biocatalysts. In this direction, magnetic biocatalysts are attractive due to their easy separation through an external magnetic field. Recently, a bioinspired immobilization technique that mimics the natural biomineralization reactions in diatoms has emerged as a fast and versatile tool for generating robust, cheap, and highly stable (nano) biocatalysts. In this work, bioinspired formation of a biotitania matrix is triggered on the surface of magnetic particles in the presence of laccase in order to produce laccase-biotitania (lac-bioTiO2 ) biocatalysts suitable for environmental applications using a novel, fast and versatile enzyme entrapment technique. Highly active lac-bioTiO2 particles have been produced and the effect of different parameters (enzyme loading, titania precursor concentration, pH, duration of the biotitania formation, and laccase adsorption steps) on the apparent activity yield of these biocatalysts were evaluated, the concentration of the titania precursor being the most influential. The lac-bioTiO2 particles were able to catalyze the removal of bisphenol A, 17α-ethinylestradiol and diclofenac in a mixture of six model EDCs and retained 90% of activity after five reaction cycles and 60% after 10 cycles.

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Design and preparation of stable CPO/HRP@H‐MOF(Zr) composites for efficient bio‐catalytic degradation of organic toxicants in wastewater

Gao

Zhai

et al. 2018

J of Chemical Tech & Biotech

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BACKGROUND Immobilization of enzyme on a solid support can improve its stability, however, this is often accompanied by a decrease of the initial catalytic activity. The design and preparation of immobilized enzyme with simultaneous high activity and stability is a challenge. RESULTS A hierarchically porous metal organic framework H‐MOF(Zr) which was prepared by ‘crystal defect’ strategy was very stable in aqueous solution and possessed well‐defined, tunable and adjacent hierarchical pores. When using the H‐MOF(Zr) as support for enzyme immobilization, a single array of enzyme in a single mesoporous channel was achieved so as to avoid aggregation of the enzyme. Meanwhile the micropores can be utilized to concentrate substrates, resulting in a decrease in the mass transfer resistance of substrate compared with that in the bulk buffer due to the enzymes and substrates closely embedded on the same support. The prepared immobilized enzyme CPO/HRP@H‐MOF(Zr) was more stable at elevated temparatures, showing 58.2% enhanced activity compared with free enzymes at 70 °C for 1 h incubation. After 12 cycles, 70.7% of activity remained. When the CPO/HRP@H‐MOF(Zr) was applied in the treatment of wastewater containing isoproturon and 2,4‐dichlorophenol, complete degradation was achieved in only 15 min. CONCLUSION Both high activity and stability under harsh reaction conditions give the CPO/HRP@H‐MOF(Zr) composites potential for practical application in wastewater treatment. © 2018 Society of Chemical Industry

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Design-of-experiment strategy for the formulation of laccase biocatalysts and their application to degrade bisphenol A

Cited by 29 publications

References 34 publications

Formulation and characterization of an immobilized laccase biocatalyst and its application to eliminate organic micropollutants in wastewater

Formulation and characterization of an immobilized laccase biocatalyst and its application to eliminate organic micropollutants in wastewater

Bioinspired production of magnetic laccase‐biotitania particles for the removal of endocrine disrupting chemicals

Design and preparation of stable CPO/HRP@H‐MOF(Zr) composites for efficient bio‐catalytic degradation of organic toxicants in wastewater

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