New efficient laccase immobilization strategy using ionic liquids for biocatalysis and microbial fuel cells applications

Kacem, Sihem Haj; Galai, Said; Ríos, Antonia Pérez de los; Fernández, Francisco José Hernández; Smaali, Issam

doi:10.1002/jctb.5337

Cited by 25 publications

(14 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Nafion polymer laccase possibly retained better activity compared to Cu-Alg due to lower leaching of the enzyme and well-protected microenvironment in the polymer micelle. Apart from Nafion, there have been work carried out with immobilization of laccase in other ionic liquids; the immobilization efficiency was high, but the voltage and power in MFC was much lower than the Nafion used in this study (Haj Kacem et al, 2018 ).…”

Section: Resultsmentioning

confidence: 90%

Laccase Immobilization Strategies for Application as a Cathode Catalyst in Microbial Fuel Cells for Azo Dye Decolourization

et al. 2021

View full text Add to dashboard Cite

Enzymatic biocathodes have the potential to replace platinum as an expensive catalyst for the oxygen reduction reaction in microbial fuel cells (MFCs). However, enzymes are fragile and prone to loss of activity with time. This could be circumvented by using suitable immobilization techniques to maintain the activity and increase longevity of the enzyme. In the present study, laccase from Trametes versicolor was immobilized using three different approaches, i.e., crosslinking with electropolymerized polyaniline (PANI), entrapment in copper alginate beads (Cu-Alg), and encapsulation in Nafion micelles (Nafion), in the absence of redox mediators. These laccase systems were employed in cathode chambers of MFCs for decolourization of Acid orange 7 (AO7) dye. The biocatalyst in the anode chamber was Shewanella oneidensis MR-1 in each case. The enzyme in the immobilized states was compared with freely suspended enzyme with respect to dye decolourization at the cathode, enzyme activity retention, power production, and reusability. PANI laccase showed the highest stability and activity, producing a power density of 38 ± 1.7 mW m−2 compared to 25.6 ± 2.1 mW m−2 for Nafion laccase, 14.7 ± 1.04 mW m−2 for Cu-Alg laccase, and 28 ± 0.98 mW m−2 for the freely suspended enzyme. There was 81% enzyme activity retained after 1 cycle (5 days) for PANI laccase compared to 69% for Nafion and 61.5% activity for Cu-alginate laccase and 23.8% activity retention for the freely suspended laccase compared to initial activity. The dye decolourization was highest for freely suspended enzyme with over 85% decolourization whereas for PANI it was 75.6%, Nafion 73%, and 81% Cu-alginate systems, respectively. All the immobilized laccase systems were reusable for two more cycles. The current study explores the potential of laccase immobilized biocathode for dye decolourization in a microbial fuel cell.

show abstract

Section: Resultsmentioning

confidence: 90%

Laccase Immobilization Strategies for Application as a Cathode Catalyst in Microbial Fuel Cells for Azo Dye Decolourization

et al. 2021

View full text Add to dashboard Cite

show abstract

“…The immobilization of laccase enzymes on the surfaces of different materials to constitute a biosensing platform is however, a critical factor in the development of bioelectrochemical sensing devices. In this sense, copper oxide nanoparticles, nanocomposites containing molybdenum disulfide, graphene quantum dots and ionic liquid membranes have become compatible matrices for laccase immobilization in biosensing devices.…”

Section: Laccases As Versatile Enzymes: Traditional and New Industriamentioning

confidence: 99%

Laccases as versatile enzymes: from industrial uses to novel applications

Moreno

Ibarra²,

Eugenio³

et al. 2019

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

The application of enzymes offers an enormous potential in the improvement of existing industrial procedures and in the establishment of new processes for obtaining high-added value products. Enzymes provide cleaner and more efficient industrial processes and contribute to the sustainability concept. In this sense, laccases are very versatile biocatalysts currently used in food, textile and pulp and paper sectors among others. During the last years, scientific efforts have been diverted to the exploitation of such interesting enzymes in novel fields like lignocellulosic biorefineries, biosensors or enzymatic biofuel cells. This review provides a general vision of the use of laccase enzymes describing their main characteristics and mode of action. Furthermore, their current uses in industrial processes are summarized and the most novel potential application of laccases are revealed. The increasing interest on laccases is also demonstrated by the research efforts on enzyme engineering as it is detailed in this review. wileyonlinelibrary.com/jctb www.soci.org AD Moreno et al. J Chem Technol Biotechnol 2020; 95: 481-494

show abstract

“…Lin et al (2018) added laccase from Ganoderma lucidum to the broth in the cathode chamber, favouring the redox reaction, and obtained 84% of COD removal in the anode chamber and a power density of 40 mW cm 2 , maintaining electricity energy for 45 days. Kacem et al (2017) immobilised commercial laccase in polymer inclusion ionic liquid membranes and applied it in single-chamber air-cathode MFC obtaining a COD removal rate of 70%, in fresh wastewater collected from a mineral oil manufacturing company. Similarly to these studies, other authors (Schaetzle et al 2009;Sané et al 2014) also consider laccase as a relevant component that improves the performance of MFCs, and this approach as a promising sustainable technology is not only for bioenergy production but also for wastewater treatment.…”

Section: Chemical Oxygen Demand Removal and Co-generation Electricitymentioning

confidence: 99%

Microbial fuel cell-induced production of fungal laccase to degrade the anthraquinone dye Remazol Brilliant Blue R

et al. 2019

View full text Add to dashboard Cite

The anthraquinone dye Remazol Brilliant Blue R is largely used in the textile industry. However, its removal from wastewaters is costly and complex. Many methods have been tested to solve this ecological problem, but there is still a need for efficient methods. We propose here an alternative use of a two-chambered microbial fuel cell (MFC), fuelled with domestic wastewater in the anodic chamber, to degrade a simulated textile dye effluent made of Remazol Brilliant Blue R inoculated with an immobilised fungal strain, Pleurotus ostreatus URM 4809, as a laccase producer, in the cathodic chamber. The MFC showed continuous synthesis of laccase in the cathodic chamber, which, in turn, promoted the rapid decolourisation, of more than 86% of the textile dye effluent. The yield was further increased by the addition of glycerol. Electrochemical monitoring also indicated an increase in power density and current density. After 20 days of MFC operation, 62.1% of organic matter was removed in the anodic compartment, thus leaving the effluent with a much lower toxicity.

show abstract

New efficient laccase immobilization strategy using ionic liquids for biocatalysis and microbial fuel cells applications

Cited by 25 publications

References 29 publications

Laccase Immobilization Strategies for Application as a Cathode Catalyst in Microbial Fuel Cells for Azo Dye Decolourization

Laccase Immobilization Strategies for Application as a Cathode Catalyst in Microbial Fuel Cells for Azo Dye Decolourization

Laccases as versatile enzymes: from industrial uses to novel applications

Microbial fuel cell-induced production of fungal laccase to degrade the anthraquinone dye Remazol Brilliant Blue R

Contact Info

Product

Resources

About