Engineering of a fungal laccase to develop a robust, versatile and highly-expressed biocatalyst for sustainable chemistry

Salas, Felipe de; Aza, Pablo; Gilabert, Joan F.; Santiago, Gerard; Kılıç, Sibel; Sener, M. Emre; Vind, Jesper; Guallar, Vı́ctor; Martínez, Ángel T.; Camarero, Susana

doi:10.1039/c9gc02475a

Cited by 39 publications

(69 citation statements)

References 56 publications

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“…Recent approaches have used the creation of stable and robust HRPLs mutant libraries coupled with screening assays in various directed evolution strategies, including classical adaptive evolution, consensus design, and chimeragenesis [73,74] Structure-guided evolution of HRPLs has been shown to increase thermal stability through the development of double mutants or chimeras [74,75]. The thermostability of a fungal laccase has been improved significantly, doubling its half-life at 80°C, using computer-assisted directed evolution [76,77]. In another approach, an evolved HRPL mutant from white-rot fungi subjected to structure-guided evolution displayed enhanced thermostability because of increased rigidity of flexible surface loops [74].…”

Section: Exo-type Oxidationmentioning

confidence: 99%

Non-Hydrolyzable Plastics – An Interdisciplinary Look at Plastic Bio-Oxidation

Inderthal

Tai

Harrison

2021

Trends in Biotechnology

109

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Section: Exo-type Oxidationmentioning

confidence: 99%

Non-Hydrolyzable Plastics – An Interdisciplinary Look at Plastic Bio-Oxidation

Inderthal

Tai

Harrison

2021

Trends in Biotechnology

109

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“…Pleurotus species are known to be potent degraders of phenol-rich contaminants [ 10 , 11 ], while their oxidative activity is mainly based on the production of multiple laccase enzymes [ 12 ], resulting in the production of high laccase titers during growth in phenol-containing media [ 1 , 13 ]. However, despite their high potential towards the oxidation of a wide variety of persistent pollutants, the enzymes derived from basidiomycetes usually are characterized by a low tolerance against extreme temperatures and pH, as well as the presence of solvents and inhibitors, as shown by numerous efforts to enhance their stability [ 14 , 15 , 16 ]. All these properties result in low stability of the enzymes in industrial process conditions.…”

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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“…It has been applied in various sectors, such as biomedical [2], dye degradation [3], paper industries for delignification [4][5], bioremediation [6], in biosensors [7], as melanin degraders in the cosmetic industry [8], as an enzymatic biofuel [9] and used in juice clarification [10]. Furthermore, laccase is a key biological mediator and the best alternative for chemical mediators; thus, it is regarded as a green enzyme in dye degradation, which is a new era for dye degradation [11]. Synthetic dyes are broadly used in a wide range of industries, including textiles, paper, printing, cosmetics, and pharmaceuticals.…”

Section: Introductionmentioning

confidence: 99%

Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes

Sayyed

Bhamare²,

Sapna

et al. 2020

PLoS ONE

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Although laccase has been recognized as a wonder molecule and green enzyme, the use of low yielding fungal strains, poor production, purification, and low enzyme kinetics have hampered its large-scale application. Thus,this study aims to select high yielding fungal strains and optimize the production, purification, and kinetics of laccase of Aspergillus sp. HB_RZ4. The results obtained indicated that Aspergillus sp. HB_RZ4 produced a significantly large amount of laccase under meso-acidophilic shaking conditions in a medium containing glucose and yeast extract. A 25 μM CuSO 4 was observed to enhance the enzyme yield. The enzyme was best purified on a Sephadex G-100 column. The purified enzyme resembled laccase of A. flavus. The kinetics of the purified enzyme revealed high substrate specificity and good velocity of reaction,using ABTS as a substrate. The enzyme was observed to be stable over various pH values and temperatures. The peptide structure of the purified enzyme was found to resemble laccase of A. kawachii IFO 4308. The fungus was observed to decolorize various dyes independent of the requirement of a laccase mediator system. Aspergillus sp. HB_RZ4 was observed to be a potent natural producer of laccase, and it decolorized the dyes even in the absence of a laccase mediator system. Thus, it can be used for bioremediation of effluent that contains non-textile dyes.

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Engineering of a fungal laccase to develop a robust, versatile and highly-expressed biocatalyst for sustainable chemistry

Abstract: From laccase design to application of the overexpressed biocatalyst in an industrial environment for eco-friendly synthesis of polyaniline and dyes.

Cited by 39 publications

References 56 publications

Non-Hydrolyzable Plastics – An Interdisciplinary Look at Plastic Bio-Oxidation

Non-Hydrolyzable Plastics – An Interdisciplinary Look at Plastic Bio-Oxidation

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

Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes

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