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![(a) Yield of decolorization of RBBR (Ydec%, bars) and relative laccase activity (%) in the IL‐rich phase (symbols) in six cycles comprising both the recovery and reuse of the enzyme and of the [Ch][DHC]‐rich phase, at 25°C. (b) Schematic overview of ABS as novel liquid supports for enzyme immobilization and reuse. ABS, aqueous biphasic systems; RBBR, Remazol Brilliant Blue R [Color figure can be viewed at wileyonlinelibrary.com]](publication/350381416/figure/fig4/AS:11431281255432758@1719419105782/a-Yield-of-decolorization-of-RBBR-Ydec-bars-and-relative-laccase-activity-in.png)
(a) Yield of decolorization of RBBR (Ydec%, bars) and relative laccase activity (%) in the IL‐rich phase (symbols) in six cycles comprising both the recovery and reuse of the enzyme and of the [Ch][DHC]‐rich phase, at 25°C. (b) Schematic overview of ABS as novel liquid supports for enzyme immobilization and reuse. ABS, aqueous biphasic systems; RBBR, Remazol Brilliant Blue R [Color figure can be viewed at wileyonlinelibrary.com]
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Novel liquid supports for enzyme immobilization and reuse based on aqueous biphasic systems (ABS) constituted by cholinium‐based ionic liquids (ILs) and polymers for the degradation of dyes are here proposed. The biocatalytic reaction for dye decolorization using laccase occured in the biphasic medium, with the enzyme being “supported” in the IL‐ri...
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Citations
... 2-fold higher activity compared to that of the non-ILimmobilized cellulose. 61 Various types of immobilized materials have been employed for laccase; ILs, 122,123 carbon nanotubes−ionic liquid nanocomposite, 117 sol-gel-silica, 124,125 modified silica, 126 glyoxyl-agarose bead, 127 organic-inorganic nanocomposite, 131 magnetic nanoparticles, 128,129,133,136,137 carbon nanotube (CNTs)-IL composite, polymer included IL, 130,145 porous wood, 134 sponge like cellulose composite polymer, 132 mesoporous silica, 133 DES,135 hydrogel,138 ...
Selective oxidative depolymerization of a lignocellulosic biomass is the first step in the valorisation process. Chemical oxidations generally require hazardous reagents and harsh reaction conditions; thus, the resulting produced compounds are low-value molecules or complicated mixtures. Laccases are copper ion-containing oxidases and catalyze the oxidation of polyphenol or amine derivatives using molecular oxygen; laccase-mediated reaction systems thus allow the depolymerization of lignocellulosic compounds and the decomposition of aromatic pollutants in wastewater. However, due to the short distance between the active site and the surface of the laccase, the reactivity of laccase is influenced by the reaction conditions, in particular, the solvent system. Ionic liquids (ILs) and deep eutectic solvents (DESs) have now been acknowledged as not only new reaction media but also as activating agents of biocatalysts. In order to improve the activity or increasing the tolerance of laccases against ILs or DESs, three methods have been developed: the first is the direct evolution of the enzyme that is a very powerful tool for tailoring the enzyme, the second is the design of supporting materials including ILs for the immobilization of a laccase, and the third is modification of the surface of a laccase protein by chemical methods or protein engineering. This review examines laccase-mediated reactions in ILs and DESs focusing on how laccase contributes to sustainable chemistry; using laccase-mediated reactions, the depolymerization of lignocellulosic compounds, phenolic compounds, and synthetic dyes has now been accomplished. Since the reactions were accomplished under hazardous chemical reagent-free conditions, it is expected that investigation in this field of laccase-mediated oxidation might become even more important in sustainable chemistry.
... The integration of processing steps using ATPS allows the development of in situ platforms capable of reducing the number of operation units and processing steps for an idealized process. This ability of ATPS to integrate various bioprocesses has led to their application in cutting-edge biocatalytic 87,125,126 and fermentative platforms. 127,128 The application of ATPS in biocatalytic processes has two main advantages: mild conditions for enzymatic reactions and the in situ removal of products as they are released. ...
... Similarly, ATPS were used as in situ bioremediation platforms, with laccase being immobilized and reused in ATPS for the degradation of Remazol Brilliant Blue R (RBBR) dye. 125 Under optimized conditions, the complete degradation of RBBR was achieved using ATPS composed of PPG-400 and cholinium dihydrogen citrate, with a 96% of degradation yield after six consecutive reaction cycles. 125 Due to the wide plethora of phase-forming compounds and numerous processing variables that need to be considered in ATPS-based processes, high-throughput (HT) platforms have emerged as valuable tools for screening and optimizing this type of in situ platforms. ...
... 125 Under optimized conditions, the complete degradation of RBBR was achieved using ATPS composed of PPG-400 and cholinium dihydrogen citrate, with a 96% of degradation yield after six consecutive reaction cycles. 125 Due to the wide plethora of phase-forming compounds and numerous processing variables that need to be considered in ATPS-based processes, high-throughput (HT) platforms have emerged as valuable tools for screening and optimizing this type of in situ platforms. These automated and miniaturized experimental setups can be applied using microtiter plates, quickly screening a large number of experimental conditions and allowing the selection of the most suitable ATPS composition for the idealized process. ...
Aqueous Two-Phase Systems (ATPS), also known as Aqueous Biphasic Systems (ABS), have been extensively studied as platforms for the separation and purification of biomolecules and other valuable compounds. These liquid-liquid...
... Enzymes are fundamental in several fields, as they present excellent catalytic properties, selectivity, efficiency, low toxicity, and biodegradability. Laccases, for instance, are of special interest due to their capacity of oxidizing a wide range of molecules and thus, being able to catalyze several processes [65][66][67]. Without recycling, working with enzymes is expensive, so promoting their reuse with small compound losses or activity is crucial, albeit very challenging. ...
... Without recycling, working with enzymes is expensive, so promoting their reuse with small compound losses or activity is crucial, albeit very challenging. Hence, ABS have been proposed as efficient liquid supports for laccase, allowing different in situ reactions (cf. Figure 1) [66,67]. Although these works are not directly related to food processing, they show outstanding results with the use and recycling of laccase in distinct reactions. ...
Aqueous biphasic systems are widely known for their enhanced biocompatibility and selectivity in downstream processes. Hence, being a key tool for the extraction/separation of innumerous biomolecules. This is particularly important for the food industry considering the higher consumers’ awareness for the health hazards associated with chemicals used in food processing and applications as well as the replacement of synthetic food additives such as pigments and preservatives. Therefore, this mini-review offers a critical perspective on the progress done over the last 3 years regarding the application of aqueous biphasic systems i) for the extraction of food related biomolecules, ii) as analytical tools in food processing, iii) as in-situ bio-based platforms, iv) for the valorization of food waste and v) to shed some light on how molecular simulation approaches may be a key element in this framework.
... ABS consist of two immiscible aqueous-rich phases formed when water-soluble components are mixed above given concentrations (Freire et al., 2012;Pereira et al., 2020). Recently, ABS systems have been investigated as reaction media and liquid supports for enzymes since they provide a suitable and friendly environment for the maintenance of the enzymatic activity and its reuse (Ferreira et al., 2018;Capela et al., 2020;Ferreira et al., 2021;Muñiz-Mouro et al., 2021). Another advantage and application of this approach is the possibility of simultaneous extract and concentrate the reaction product by manipulating the volume of the ABS phases, using the tie-line of binodal curves (Dinis et al., 2018), while maintaining the enzyme in the opposite phase. ...
... In a recent study assessed by. Ferreira et al. (2021) it was demonstrated the recovery and reuse of laccase in an integrated reaction-separation process by applying thermoreversible ABS. No losses in the enzymatic activity were observed for at least five consecutive cycles of enzymatic reaction with 2,2′-azino-bis (3ethylbenzothiazoline-6-sulphonic acid) (ABTS). ...
... For the study of recovery and reuse of laccase, four consecutive cycles of dopamine polymerization were performed using the optimised ABS composed of 33 wt% PPG 400 + 6.4 wt% K₂HPO₄ + 20 wt% dopamine solution (3.00 mg ml −1 ) + 40.6 wt% laccase solution (1.00 mg ml −1 ). After the first reaction cycle, the PDA i -enriched top phase was removed, and the same volume of a solution containing the respective top polymer-rich phase constituents (determined by the tie-line) (Ferreira et al., 2021) was added to the remaining laccase-rich bottom phase. Dopamine solution was added to reach a final concentration of 0.60 mg ml −1 in the ABS and a new biocatalytic cycle started. ...
Polydopamine (PDA), a bioinspired polymer from mussel adhesive proteins, has attracted impressive attention as a novel coating for (nano) materials with an adequate conformal layer and adjustable thickness. Currently, PDA is obtained from dopamine chemical oxidation under alkaline conditions, limiting its use in materials sensible to alkaline environments. Envisaging a widespread use of PDA, the polymerization of dopamine by enzymatic catalysis allows the dopamine polymerization in a large range of pHs, overcoming thus the limitations of conventional chemical oxidation. Moreover, the conventional method of polymerization is a time-consuming process and produces PDA films with poor stability, which restricts its applications. On the other hand, the main bottleneck of enzyme-based biocatalytic processes is the high cost of the single use of the enzyme. In this work, laccase was used to catalyse dopamine polymerization. To improve its performance, a liquid support for integrating the laccase and its reuse together with the PDA production and recovery was developed using aqueous biphasic systems (ABS). Firstly, dopamine polymerization by laccase was optimized in terms of pH, temperature and initial dopamine concentration. It was demonstrated that the highest enzymatic polymerization of dopamine was achieved at pH 5.5, 30°C and 2 mg ml ⁻¹ of dopamine. Then, ABS composed of polymers, salts and ionic liquids were evaluated to optimize the laccase confinement in one phase while PDA is recovered in the opposite phase. The most promising ABS allowing the separation of laccase from the reaction product is composed of polypropylene glycol (400 g mol ⁻¹ ) and K 2 HPO 4 . The polymerization of dopamine in ABS leads to a remarkable improvement of polymerization of 3.9-fold in comparison to the conventional chemical PDA polymerization. The phase containing the confined laccase was reused for four consecutive reaction cycles, with a relative polymerization of 68.9% in the last cycle. The results of this work proved that ABS are a promising approach to create a liquid support for enzyme reuse allowing the process intensification efforts. The use of biocatalysts in ABS emerges as sustainable and alternative platforms from environmental and techno-economic points of view.
... In this context, the use of biphasic systems can be applied for enzyme retention in one phase, allowing enzyme recovery and reuse. For example, Ferreira et al. [188] evaluated the use of aqueous biphasic systems (ABS) as liquid support to immobilize and reuse laccase for cyclically degrading RBBR (Fig. 12) The liquid enzyme immobilization approaches present a high potential to be applied as novel techniques in dye decolourization and detoxification of wastewater. Current immobilization methods using solid supports have limitations due to enzyme leakage from the carrier, unwanted interactions between the carrier and the enzyme, or even the en- zyme's inability to react with its substrate [8]. ...
According to the European Environment Agency, the textile industry is responsible for 20% of global water pollution due to dyeing and finishing products, thus facing severe environmental challenges. It is essential to design more biocompatible and sustainable treatment processes capable of removing dyes from industrial wastewater to fight this environmental hazard. Chemical industries must change traditional chemical-based concepts to more environmentally friendly and greener processes to remove pollutants, including dyes. Enzymatic bioremediation is a smart tool and a promising alternative for environmental pollutant degradation. The use of enzymes in dye decolourization makes the process a green and clean alternative to conventional chemical treatments. Moreover, enzyme-mediated biocatalysis decreases the formation of toxic by-products compared to chemical reactions. The most used enzyme for the decolourization of dyes is laccase. Laccase is a multicopper oxidase found in diverse organisms such as fungi. It promotes the oxidation of phenolic compounds and has a wide range of substrate specificity, making it a promising enzyme for removing different dyes used by the textile industry, including recalcitrant aromatic dyes. The present article gives a comprehensive revision of textile dye decolourization, its types, recent developments in laccase-mediated dye bioremediation technologies, the mechanism of biocatalysis, and their limitations and challenges. Emphasis on the chemical pathways of laccase reaction mechanisms for dye bioremediation processes is also provided. In addition, a brief overview of textile industries and the respective traditional treatment processes for textile wastewater is also presented.
... Low-cost synthetic routes and easy preparation should also be filled. In this direction, some novel ILs have been reported, such as those composed of cholinium- [60,61] and glycine-betaine-based cations [62,63], combined, for example, with anions derived from amino acids and carboxylic acids [60,61] (Fig. 5). The use of ILs in biocatalysis bring many advantages. ...
... Low-cost synthetic routes and easy preparation should also be filled. In this direction, some novel ILs have been reported, such as those composed of cholinium- [60,61] and glycine-betaine-based cations [62,63], combined, for example, with anions derived from amino acids and carboxylic acids [60,61] (Fig. 5). The use of ILs in biocatalysis bring many advantages. ...
... Integrated process using IL-based ABS for dye decolorization and enzyme reuse. Adapted from Ferreira et al.[61]. ...
Biocatalytic processes find increasing applications in various industries due to the high efficiency of biotransformations as well as the renewable nature of the enzymes and substrates. Enzymatic biocatalysis is an attractive alternative to conventional chemical catalysis, with corresponding advances now allowing a wide range of biotransformations. However, to make the enzymatic process sustainable, it is essential to separate the product and reuse the biocatalyst while maintaining its efficiency. Liquid–liquid biphasic systems are alternative approaches to integrate the enzymatic reaction, product recovery, and reuse of the biocatalyst and phase constituents. Moreover, to expand the range of biocatalytic reactions, ionic liquids and deep eutectic solvents have been emerged as alternative reaction media due to their unique properties, in particular their ability to maintain enzymes active and stable.
In this chapter, we outline novel opportunities for using enzymes in biphasic systems based on ionic liquids and deep eutectic solvents and discuss the key points and scientific developments expanding the application of biocatalysis.
... The RMF causes change in the copper atom site which further causes change in its catalytic property (Wasak et al., 2019). Improved catalytic behaviour of laccase is reported in the presence of some metal ions and ionic liquids (Ferreira et al., 2021;Zhang et al., 2015). Metallic ions including Cu +2 , Mg +2 , K + , Cd +2 , Zn +2 , Ni +2 , Fe +2 and Mn +2 enhance the catalytic activity of laccase by maintaining the conformation of its active site (Si et al., 2021). ...
... The increased resistance to thermal denaturation after immobilization of laccase offers a potential advantage in wastewater treatment applications. Liquid supports based on an aqueous biphasic system have also demonstrated great catalytic efficiency and reusability in addition to solid supports (Ferreira et al., 2021). Laccase immobilization on various surfaces and the effect of immobilization on different parameters is shown in Table 1. ...
We are facing a high risk of exposure to emerging contaminants and increasing environmental pollution with the concomitant growth of industries. Persistence of these pollutants is a major concern to the ecosystem. Laccases, also known as “green catalysts” are multi-copper oxidases which offers an eco-friendly solution for the degradation of these hazardous pollutants to less or non-toxic compounds. Although various other biological methods exist for the treatment of pollutants, the fact that laccases catalyze the oxidation of broad range of substrates in the presence of molecular oxygen without any additional cofactor and releases water as the by-product makes them exceptional. They have a good possibility of utilization in various industries, especially for the purpose of bioremediation. Besides this, they have also been used in medical/health care, food industry, bio-bleaching, wine stabilization, organic synthesis and biosensors. This review covers the catalytic behaviour of laccases, their immobilization strategies, potential applications in bioremediation of recalcitrant environmental pollutants and their engineering. It provides a comprehensive summary of most factors to consider while working with laccases in an industrial setting. It compares the benefits and drawbacks of the current techniques. Immobilization and mediators, two of the most significant aspects in working with laccases, have been meticulously discussed.
