Laccase–syringaldehyde-mediated degradation of trace organic contaminants in an enzymatic membrane reactor: Removal efficiency and effluent toxicity

Nguyen, Dinh Duc; Merwe, Jason P. van de; Hai, Faisal I.; Leusch, Frédéric D.L.; Kang, Jinguo; Price, William E.; Roddick, Felicity; Magram, Saleh Faraj

doi:10.1016/j.biortech.2015.10.054

Cited by 89 publications

(50 citation statements)

References 30 publications

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“…Laccases have the ability to oxidize a wide range of aromatic and non-aromatic compounds which includes substituted phenols, some inorganic ions, and variety of non-phenolic compounds (Matera et al 2008;Songulashvili et al 2016;Nguyen et al 2016;Surwase et al 2016). Due to its low substrate specificity, it can act on a broad range of substrates and has attracted considerable attention in different environmental, industrial, and biotechnological sectors (Afreen et al 2016).…”

Section: Introductionmentioning

confidence: 99%

Fungal laccase discovered but yet undiscovered

Agrawal

Chaturvedi

Verma

2018

Bioresour. Bioprocess.

191

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Laccases belongs to multinuclear copper-containing oxidase and can act on a variety of aromatic and non-aromatic compounds. Due to their broad substrate specificity, they are considered as a promising candidate in various industrial and biotechnological sectors. They are regarded as a "Green Tool"/"Green Catalyst" in biotechnology. The present review focuses on structure, reaction mechanism, categories, applications, economic feasibility, limitations, and future prospects of fungal laccases. Thus, this review would help in understanding laccases along with the areas, which has not been focused and requires attention. Since past, immense work has been carried out on laccases: yet, new discoveries and application are ever increasing which includes bio-fuel, bio-sensor, fiber board synthesis, bioremediation, clinical, textile industry, food, cosmetics, and many more. Hence, it can be stated that fungal laccase is an enzyme which is "discovered but yet undiscovered".

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Section: Introductionmentioning

confidence: 99%

Fungal laccase discovered but yet undiscovered

Agrawal

Chaturvedi

Verma

2018

Bioresour. Bioprocess.

191

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“…An overall degradation of only 40-65% was achieved by the MD-EMBR for a number of non-phenolic TrOCs (Figure 2), however, these removal efficiencies in fact compare favorably with those reported in the literature [12,15,37]. For instance, laccase catalyzed degradation of carbamazepine, clofibric acid, fenoprop and atrazine has been reported to be less than 10% in both batch and continuous flow ultrafiltration based enzymatic bioreactors [15,18,40].…”

Section: Troc Degradation In Enzymatic Bioreactormentioning

confidence: 53%

“…Indeed Margot et al [12] observed that degradation of diclofenac by laccase was significantly higher in the mixture of TrOCs containing diclofenac, bisphenol A and mefenamic acid than its degradation as a single compound. It is possible that complete retention of phenoxyl radicals formed due to the degradation of phenolic TrOCs aided better degradation of non-phenolic TrOCs by MD-EMBR as compared to previously developed UF-EMBR [18,37]. Further investigation would be required to substantiate this hypothesis but that is beyond the scope of this study.…”

Section: Troc Degradation In Enzymatic Bioreactormentioning

confidence: 63%

“…The well degraded non-phenolic TrOCs include metronidazole, benzophenone, amitriptyline and octocrylene. High laccase-catalyzed degradation (80-99%) in continuous flow UF-EMBR has been previously reported [18,37] Table S1). High enzymatic degradation of metronidazole following its complete retention by the MD membrane in MD-EMBR can be attributed to the prolonged contact time that may have promoted the interaction of laccase with the EDGs of metronidazole.…”

Section: Troc Degradation In Enzymatic Bioreactormentioning

confidence: 99%

“…Samples for toxicity analysis were collected from the enzymatic bioreactor and permeate tank at end of each experiment. Toxicity, expressed as a relative toxicity unit (rTU), was analyzed by measuring the inhibition of luminescence in the naturally bioluminescent bacteria, Photobacterium leiognathi, as previously described [37,38].…”

Section: Enzymatic Activity Orp and Toxicity Assaymentioning

confidence: 99%

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Degradation of Trace Organic Contaminants by a Membrane Distillation—Enzymatic Bioreactor

et al. 2017

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A high retention enzymatic bioreactor was developed by coupling membrane distillation with an enzymatic bioreactor (MD-EMBR) to investigate the degradation of 13 phenolic and 17 non-phenolic trace organic contaminants (TrOCs). TrOCs were effectively retained (90-99%) by the MD membrane. Furthermore, significant laccase-catalyzed degradation (80-99%) was achieved for 10 phenolic and 3 non-phenolic TrOCs that contain strong electron donating functional groups. For the remaining TrOCs, enzymatic degradation ranged from 40 to 65%. This is still higher than those reported for enzymatic bioreactors equipped with ultrafiltration membranes, which retained laccase but not the TrOCs. Addition of three redox-mediators, namely syringaldehyde (SA), violuric acid (VA) and 1-hydroxybenzotriazole (HBT), in the MD-EMBR significantly broadened the spectrum of efficiently degraded TrOCs. Among the tested redox-mediators, VA (0.5 mM) was the most efficient and versatile mediator for enhanced TrOC degradation. The final effluent (i.e., membrane permeate) toxicity was below the detection limit, although there was a mediator-specific increase in toxicity of the bioreactor media.

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Immobilization of Enzymes in/on Membranes and their Applications

et al. 2019

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Enzyme membrane reactors (EMRs) are becoming increasingly interesting for application in bioconversion processes in food processing, pharmaceutics, biorefinery and wastewater treatment. Integrating the highly efficient enzymatic reaction with selectable membrane separation technology, the EMRs are able to reduce product inhibition, improve the stability of the enzyme, increase the number of reaction cycles and sustainably separate products from biotransformation solutions. Generally, in EMRs, enzymes can be either free in the solution, immobilized on an additional carrier or immobilized directly in/on a porous structure of the membrane, of which the system with the enzyme immobilized directly in/on the membrane (EIM) is a relatively simple and most widely applied method. The EIM system not only facilitates recycling of the enzymes but also in many cases additionally enhances enzyme properties such as the stability and viability. A membrane with a porous structure is usually considered as a potential carrier for enzyme immobilization. A series of immobilization methods has been developed to fix the enzymes on the membranes. The purpose of this review is to systemically summarize the immobilization methods of enzymes in/on membranes and the applications of the EIM system for biocatalysis.

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Laccase–syringaldehyde-mediated degradation of trace organic contaminants in an enzymatic membrane reactor: Removal efficiency and effluent toxicity

Cited by 89 publications

References 30 publications

Fungal laccase discovered but yet undiscovered

Fungal laccase discovered but yet undiscovered

Degradation of Trace Organic Contaminants by a Membrane Distillation—Enzymatic Bioreactor

Immobilization of Enzymes in/on Membranes and their Applications

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