Application of eukaryotic and prokaryotic laccases in biosensor and biofuel cells: recent advances and electrochemical aspects

Zhang, Yue; Lv, Ziyao; Zhou, Jie; Xin, Fengxue; Ma, Jiangfeng; Wu, Hao; Fang, Yan; Jiang, Min; Dong, Weiliang

doi:10.1007/s00253-018-9421-7

Cited by 28 publications

(15 citation statements)

References 138 publications

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“…Laccase biosensors have been recently developed to monitor some toxic and/or harmful chemicals like phenolic compounds . They have also been tested for immune assays, hormone monitoring in clinical diagnosis and the quantitative analysis of beverages . Regarding the latter, several types of laccase biosensors have been developed to determine for instance the tannins in wine or polyphenols in tea infusions and other beverages …”

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

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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

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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

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“…At present, more than 100 fungal laccases have been purified and characterized, most of which were isolated from white rotting fungi ( Rivera-Hoyos et al, 2013 ; Zhang et al, 2018 ). Meanwhile, there are a large number of litter-decomposing fungi in the forest surface, which play an important role in the process of forest litter biodegradation.…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of a Thermo- and pH-Stable Laccase From the Litter-Decomposing Fungus Gymnopus luxurians and Laccase Mediator Systems for Dye Decolorization

et al. 2021

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An extracellular laccase (GLL) was purified from fermentation broth of the litter-decomposing fungus Gymnopus luxurians by four chromatography steps, which resulted in a high specific activity of 118.82 U/mg, purification fold of 41.22, and recovery rate of 42.05%. It is a monomeric protein with a molecular weight of 64 kDa and N-terminal amino acid sequence of AIGPV TDLHI, suggesting that GLL is a typical fungal laccase. GLL demonstrated an optimum temperature range of 55°C–65°C and an optimum pH 2.2 toward 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS). It displayed considerably high thermostability and pH stability with about 63% activity retained after 24 h at 50°C, and 86% activity retained after 24 h at pH 2.2, respectively. GLL was significantly enhanced in the presence of K+, Na+, and Mg2+ ions. It demonstrated Km of 539 μM and kcat/Km of 140 mM–1⋅s–1 toward ABTS at pH 2.2 and 37°C. Acetosyringone (AS) and syringaldehyde (SA) were the optimal mediators of GLL (0.4 U/ml) for dye decolorization with decolorization rates of about 60%–90% toward 11 of the 14 synthetic dyes. The optimum reaction conditions were determined to be mediator concentration of 0.1 mM, temperature range of 25°C –60°C, and pH 4.0. The purified laccase was the first laccase isolated from genus Gymnopus with high thermostability, pH stability, and effective decolorization toward dyes, suggesting that it has potentials for textile and environmental applications.

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“…The current body of research establishes that laccase cathodes suffer from current density losses attributable to short enzyme lifetimes, suboptimal enzymatic reaction velocities, enzyme inactivation, and low enzyme adsorption [20][21][22][23]. In order to mitigate these deficiencies, attempts have been made to engineer laccases with faster reaction velocities [24][25][26][27][28][29][30].…”

Section: Introductionmentioning

confidence: 99%

A Hybrid Microbial–Enzymatic Fuel Cell Cathode Overcomes Enzyme Inactivation Limits in Biological Fuel Cells

2021

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The construction of optimized biological fuel cells requires a cathode which combines the longevity of a microbial catalyst with the current density of an enzymatic catalyst. Laccase-secreting fungi were grown directly on the cathode of a biological fuel cell to facilitate the exchange of inactive enzymes with active enzymes, with the goal of extending the lifetime of laccase cathodes. Directly incorporating the laccase-producing fungus at the cathode extends the operational lifetime of laccase cathodes while eliminating the need for frequent replenishment of the electrolyte. The hybrid microbial–enzymatic cathode addresses the issue of enzyme inactivation by using the natural ability of fungi to exchange inactive laccases at the cathode with active laccases. Finally, enzyme adsorption was increased through the use of a functionally graded coating containing an optimized ratio of titanium dioxide nanoparticles and single-walled carbon nanotubes. The hybrid microbial–enzymatic fuel cell combines the higher current density of enzymatic fuel cells with the longevity of microbial fuel cells, and demonstrates the feasibility of a self-regenerating fuel cell in which inactive laccases are continuously exchanged with active laccases.

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Application of eukaryotic and prokaryotic laccases in biosensor and biofuel cells: recent advances and electrochemical aspects

Cited by 28 publications

References 138 publications

Laccases as versatile enzymes: from industrial uses to novel applications

Laccases as versatile enzymes: from industrial uses to novel applications

Purification and Characterization of a Thermo- and pH-Stable Laccase From the Litter-Decomposing Fungus Gymnopus luxurians and Laccase Mediator Systems for Dye Decolorization

A Hybrid Microbial–Enzymatic Fuel Cell Cathode Overcomes Enzyme Inactivation Limits in Biological Fuel Cells

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