Ligninolytic enzymes: Versatile biocatalysts for the elimination of endocrine‐disrupting chemicals in wastewater

Falade, Ayodeji O.; Mabinya, Leonard V.; Okoh, Anthony I.; Nwodo, Uchechukwu U.

doi:10.1002/mbo3.722

Cited by 39 publications

(15 citation statements)

References 146 publications

(237 reference statements)

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“…LPST strategy worked best for BPA using T. versicolor cultivated on a lignocellulosic substrate. At the end of the experiment, the laccase activities were 95 U mL −1 in SmF and 220 U g −1 in SSF suggesting that the disappearance of the BPA is due to the oxidative action of enzymes and more specifically laccase though, the contribution of other ligninolytic enzymes such as MnP for the transformation cannot be neglected (Falade et al 2018).…”

Section: Lpst Of Bpa and Tca With T Versicolor In Ssf And Smfmentioning

confidence: 99%

Simultaneous laccase production and transformation of bisphenol-A and triclosan using Trametes versicolor

et al. 2019

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New age micro-pollutants, bisphenol-A (BPA) and triclosan (TCA), known for their carcinogenic effects in living organisms can effectively be removed from water using laccase from Trametes versicolor. Laccase was produced from T. versicolor JSRK13 in both submerged and solid-state fermentation (SmF and SSF) conditions. In SmF, T. versicolor JSRK13 gave the maximum production of laccase on the 10th day with an activity of 22 U mL − 1 , whereas, in SSF 185 U g − 1 of the enzyme was produced on the 17th day. Maximum production of laccase was observed with Parthenium as substrate. Parthenium, with a particle size of 3-5 mm having 60% moisture was found to be a suitable substrate for laccase production and simultaneous transformation (LPST) of BPA in a synergistic manner. A one-step concentration using 85% ammonium sulphate followed by dialysis was sufficient to give 6.7-fold purification of laccase from the crude culture filtrate. Transformation of BPA was achieved in both SmF and SSF conditions along with the production of laccase, whereas TCA was degraded with free enzyme only. Above 90% of BPA (55-5 mg L − 1) was degraded using the LPST strategy with HBT acting as a mediator in the reaction. LPST strategy did not work for TCA as it completely inhibits the growth of T. versicolor JSRK13. TCA was degraded up to 75% (1.5-0.375 mg L − 1) by the free enzyme. Our study of simultaneous laccase production and transformation proved to be efficacious in case of BPA. The results indicate that industrial and sewage wastewater containing BPA can potentially be treated with T. versicolor JSRK13 laccase. The described strategy can further be used to develop a bioprocess which can work both on solid and liquid wastes containing BPA.

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Section: Lpst Of Bpa and Tca With T Versicolor In Ssf And Smfmentioning

confidence: 99%

Simultaneous laccase production and transformation of bisphenol-A and triclosan using Trametes versicolor

et al. 2019

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“…While laccases (EC 1.10.3.2) and ligninolytic peroxidases (EC 1.11.1.x) have been intensively studied and applied in different fields including food, textile and cosmetics industry, biorefineries, and bioremediation (Arregui et al 2019 ; Falade et al 2016 , 2018 ; Fillat et al 2017 ; Rodríguez Couto and Toca Herrera 2006 ; Stanzione et al 2020 ), H 2 O 2 -producing oxidases like aryl-alcohol oxidases only slowly step forward into biocatalytic applications. For example, an AAO from Pleurotus eryngii ATCC 90787 ( Pe AAO) was studied for production of 2,5-furandicarboxylic acid (FDCA), a bio-based precursor for plastics (Carro et al 2014 ; Karich et al 2018 ; Serrano et al 2019a ; Viña-Gonzalez et al 2020 ).…”

Section: Introductionmentioning

confidence: 99%

High-level expression of aryl-alcohol oxidase 2 from Pleurotus eryngii in Pichia pastoris for production of fragrances and bioactive precursors

Jankowski

Koschorreck

Urlacher

2020

Appl Microbiol Biotechnol

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The fungal secretome comprises various oxidative enzymes participating in the degradation of lignocellulosic biomass as a central step in carbon recycling. Among the secreted enzymes, aryl-alcohol oxidases (AAOs) are of interest for biotechnological applications including production of bio-based precursors for plastics, bioactive compounds, and flavors and fragrances. Aryl-alcohol oxidase 2 (PeAAO2) from the fungus Pleurotus eryngii was heterologously expressed and secreted at one of the highest yields reported so far of 315 mg/l using the methylotrophic yeast Pichia pastoris (recently reclassified as Komagataella phaffii). The glycosylated PeAAO2 exhibited a high stability in a broad pH range between pH 3.0 and 9.0 and high thermal stability up to 55 °C. Substrate screening with 41 compounds revealed that PeAAO2 oxidized typical AAO substrates like p-anisyl alcohol, veratryl alcohol, and trans,trans-2,4-hexadienol with up to 8-fold higher activity than benzyl alcohol. Several compounds not yet reported as substrates for AAOs were oxidized by PeAAO2 as well. Among them, cumic alcohol and piperonyl alcohol were oxidized to cuminaldehyde and piperonal with high catalytic efficiencies of 84.1 and 600.2 mM−1 s−1, respectively. While the fragrance and flavor compound piperonal also serves as starting material for agrochemical and pharmaceutical building blocks, various positive health effects have been attributed to cuminaldehyde including anticancer, antidiabetic, and neuroprotective effects. PeAAO2 is thus a promising biocatalyst for biotechnological applications. Key points • Aryl-alcohol oxidase PeAAO2 from P. eryngii was produced in P. pastoris at 315 mg/l. • Purified enzyme exhibited stability over a broad pH and temperature range. • Oxidation products cuminaldehyde and piperonal are of biotechnological interest. Graphical abstract

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“…Their potential for the biodegradation of organic pollutants lies in several major oxidative enzyme activities, mainly laccases (benzenediol:oxygen oxidoreductases, Lac, EC 1.10.3.2) and peroxidases, including manganese peroxidases (MnP, EC 1.11.1.13), lignin peroxidases (LiP, EC 1.11.1.14), and versatile peroxidases (VP, EC 1.11.1.16), among others [ 1 ]. These enzymes have been employed in the degradation of a wide range of pollutants, such as endocrine disrupting chemicals [ 2 ], dyes [ 3 ], pesticides [ 4 ], substituted phenols, pharmaceuticals [ 5 ], and others. Significant research efforts have been devoted to the degradation of olive oil mill wastewater (OOMW), the liquid byproduct of three-phase decanters of olive oil production plants.…”

Section: Introductionmentioning

confidence: 99%

Crosslinked Enzyme Aggregates (CLEAs) of Laccases from Pleurotus citrinopileatus Induced in Olive Oil Mill Wastewater (OOMW)

Zerva

Pentari

2020

Molecules

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The enzymatic factory of ligninolytic fungi has proven to be a powerful tool in applications regarding the degradation of various types of pollutants. The degradative potential of fungi is mainly due to the production of different types of oxidases, of which laccases is one of the most prominent enzymatic activities. In the present work, crude laccases from the supernatant of Pleurotus citrinopileatus cultures grown in olive oil mill wastewater (OOMW) were immobilized in crosslinked enzyme aggregates (CLEAs), aiming at the development of biocatalysts suitable for the enzymatic treatment of OOMW. The preparation of laccase CLEAs was optimized, resulting in a maximum of 72% residual activity. The resulting CLEAs were shown to be more stable in the presence of solvents and at elevated temperatures compared to the soluble laccase preparation. The removal of the phenolic component of OOMW catalyzed by laccase-CLEAs exceeded 35%, while they were found to retain their activity for at least three cycles of repetitive use. The described CLEAs can be applied for the pretreatment of OOMW, prior to its use for valorization processes, and thus, facilitate its complete biodegradation towards a consolidated process in the context of circular economy.

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Ligninolytic enzymes: Versatile biocatalysts for the elimination of endocrine‐disrupting chemicals in wastewater

Cited by 39 publications

References 146 publications

Simultaneous laccase production and transformation of bisphenol-A and triclosan using Trametes versicolor

Simultaneous laccase production and transformation of bisphenol-A and triclosan using Trametes versicolor

High-level expression of aryl-alcohol oxidase 2 from Pleurotus eryngii in Pichia pastoris for production of fragrances and bioactive precursors

Crosslinked Enzyme Aggregates (CLEAs) of Laccases from Pleurotus citrinopileatus Induced in Olive Oil Mill Wastewater (OOMW)

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