Enhanced laccase stability through mediator partitioning into hydrophobic ionic liquids

Rehmann, Lars; Иванова, Е. М.; Gunaratne, H. Q. Nimal; Seddon, Kenneth R.; Stephens, Gill

doi:10.1039/c3gc42189a

Cited by 26 publications

(30 citation statements)

References 59 publications

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“…Evidence for the existence of these mechanisms has been provided by examining the product pattern of non-phenolic lignin degradation, and measuring the intra-molecular kinetic isotope effects (Barreca et al, 2004). In the oxidation of non-phenolic LMCs, the efficiency of LMS was reported to be independent of the enzymes properties (Rosado et al, 2012). Oxidation of non-phenolic LMCs by laccase-ABTS was reported to occur via the electron transfer route (Bourbonnais et al, 1998).…”

Section: Biodegradation Of Lignin With Laccase-mediator Systemsmentioning

confidence: 99%

Lignin Biodegradation with Laccase-Mediator Systems

2014

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Lignin has a significant and largely unrealized potential as a source for the sustainable production of fuels and bulk high-value chemicals. It can replace fossil-based oil as a renewable feedstock that would bring about socioeconomic and environmental benefits in our transition to a biobased economy. The efficient utilization of lignin however requires its depolymerization to low-molecular weight phenolics and aromatics that can then serve as the building blocks for chemical syntheses of high-value products. The ability of laccase to attack and degrade lignin in conjunction with laccase mediators is currently viewed as one of the potential "breakthrough" applications for lignin valorization. Here, we review the recent progress in lignin biodegradation with laccase-mediator systems, and research needs that need to be addressed in this field.

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Section: Biodegradation Of Lignin With Laccase-mediator Systemsmentioning

confidence: 99%

Lignin Biodegradation with Laccase-Mediator Systems

2014

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“…6) the shift of the active site location in the overall structure of the enzyme. The use of redox mediators would seem to be a possible solution but involves certain problems such as the toxicity of some compounds in environmental processes and the deactivation effect on the 100 enzyme itself 11,42 . The use of redox mediators would seem to be a possible solution but involves certain problems such as the toxicity of some compounds in environmental processes and the deactivation effect on the 100 enzyme itself 11,42 .…”

Section: About Here]mentioning

confidence: 99%

“…The desired industrial purpose is often difficult to achieve using the 30 native form of the enzyme, and recent developments in enzyme engineering have revolutionized the development of commercially available enzymes for a better use as industrial catalysts 2, 7 . However, IL research has focused not only on replacing organic solvents in biocatalysis but also on identifying new possibilities in water-enzyme applications or for improving 45 the catalytic activity or/and stability inon the aqueous media 7,11 . trans-esterification reactions), their ability to increase the solubility of organic substrates and to 40 improve process performance increasing the enzyme activity, stability and selectivity, by ensuring a comfortable medium for the enzyme 8, 9,10 .…”

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confidence: 99%

Over-activity and stability of laccase using ionic liquids: screening and application in dye decolorization

et al. 2015

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The use of a wide range of water miscible and immiscible ionic liquids (ILs) as reaction media for ABTS (2,2′-azino-bis(3ethylbenzothiazoline-6-sulfonic acid) diammonium salt) oxidation by Trametes versicolor laccase was studied. Thirteen ILs were shown to be suitable media for the laccase oxidation reaction, increasing the activity with respect to conventional media. Among them, the water-miscible IL choline dihydrogen phosphate [Chol][H 2 PO 4 ] allowed over-laccase activity with an enhancement rate of 451% at 25°C and pH 7.0. This ionic liquid improved the stability of the enzyme in the face of high temperature and high pH, while storage at room 10 temperature in aqueous medium was increased up to 4.5 times. Moreover, it was found that its use in the reaction medium for decolourizing dyes (antraquinonic and azoic) using laccase increased the decolourization rate by up to 216% and 137% for the azoic dyes Acid Black 1 and Remazol Brillant Blue R, respectively. A high decolorization rate was also obtained for a mix of dyes (80% within 8 h). To understand the effect of [Chol][H 2 PO 4 ] on the secondary protein structure of the laccase, several spectroscopic techniques were used 15 such as Circular Dichroism (CD), Fourier transform infrared (FT-IR) and Fluorescence, all of which demonstrated that the β sheets structure was affected. A shift to α-helix structure [Chol][H 2 PO 4 ] could be responsible of the enhancement of the enzyme activity observed at 300 mM 55properties of ILs, including their hydrophobicity, density, viscosity, melting point, polarity and solvent miscibility, can be finely tuned by selecting appropriate combinations of cations and anions, while an optimal IL can be designed for each specific enzymatic reaction system. Interest in these compounds, often 60 heralded as the green, high-tech media of the future, is still increasing rapidly, not only in biocatalysis but also in chemical catalysis, separation technology and analytical applications 13, 14 . Recently, the use of ILs with laccases has also been described as an efficient non-conventional catalyst system in applications such 65 as wood treatment and phenol degradation 3, 5 . On the other hand,Textile manufacturing involves the discharge of highly colored synthetic dye effluents which are aesthetically displeasing and can damage the receiving water body by impeding the penetration of light 15 . The strict environmental 70 legislation of European countries does not permit their release since they can have very severe consequences on river courses, including reducing photosynthetic activity and dissolved oxygen concentrations 16 . The great importance of effluent treatment has been underlined in many research-works 17 . In the textile 75 industry, a wide variety of dyes colors have been extensively used for textile industry, anthraquinonic and azoic dyes could be

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“…This fact contributed to the maintenance of the activity of the laccase during the potential generation by the MFC since the enzyme has an oxido‐reductase activity and is needed to oxidise the ABTS to turn on the reduction of O 2 to H 2 O. In agreement with this, Rehmann et al . reported that using ABTS with hydrophobic IL (such as [NTf2] anion ILs) could contribute not only to enhancing laccase stability but also to protecting the enzyme against its redox mediator, such as ABTS.…”

Section: Resultsmentioning

confidence: 99%

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

Kacem

Galai

Ríos

et al. 2017

J of Chemical Tech & Biotech

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Enhanced laccase stability through mediator partitioning into hydrophobic ionic liquids

Abstract: Partitioning mediators into water-immiscible ionic liquids protects laccase from inactivation.

Cited by 26 publications

References 59 publications

Lignin Biodegradation with Laccase-Mediator Systems

Lignin Biodegradation with Laccase-Mediator Systems

Over-activity and stability of laccase using ionic liquids: screening and application in dye decolorization

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

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