2023
DOI: 10.1016/j.chemosphere.2022.137612
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Efficient decolorization and detoxification of triarylmethane and azo dyes by porous-cross-linked enzyme aggregates of Pleurotus ostreatus laccase

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Cited by 15 publications
(5 citation statements)
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“…The results obtained for the analysis conducted on carbon source consumption and DyP activity levels for both carbon sources analyzed in the present research suggest that the AYG dye may be co-metabolized, thus inducing the production of DyP and other oxidases not evaluated in the experiments conducted by the present study. The ability of P. ostreatus to metabolize a wide variety of toxic compounds is primarily attributed to their non-specific multi-enzyme oxidative system, which comprises manganese peroxidases (MnPs; EC1.11.1.13), versatile peroxidases (VPs (EC1.11.1.16), laccases (Lacs; EC1.10.3.2), and dye-decolorizing peroxidases (DyP;EC1.11.1.19) ( George et al, 2023 ; Kunjadia et al, 2016 ; Šlosarčíková et al, 2020 ). Our previous research reported that, when glucose was the sole carbon source, the addition of Acetyl Yellow G (AYG), Remazol Brilliant Blue R (RBBR), or Acid Blue 129 (AB129) dyes increased DyP activity, ultimately achieving complete decolorization ( Cuamatzi-Flores et al, 2019 ).…”
Section: Discussionmentioning
confidence: 99%
“…The results obtained for the analysis conducted on carbon source consumption and DyP activity levels for both carbon sources analyzed in the present research suggest that the AYG dye may be co-metabolized, thus inducing the production of DyP and other oxidases not evaluated in the experiments conducted by the present study. The ability of P. ostreatus to metabolize a wide variety of toxic compounds is primarily attributed to their non-specific multi-enzyme oxidative system, which comprises manganese peroxidases (MnPs; EC1.11.1.13), versatile peroxidases (VPs (EC1.11.1.16), laccases (Lacs; EC1.10.3.2), and dye-decolorizing peroxidases (DyP;EC1.11.1.19) ( George et al, 2023 ; Kunjadia et al, 2016 ; Šlosarčíková et al, 2020 ). Our previous research reported that, when glucose was the sole carbon source, the addition of Acetyl Yellow G (AYG), Remazol Brilliant Blue R (RBBR), or Acid Blue 129 (AB129) dyes increased DyP activity, ultimately achieving complete decolorization ( Cuamatzi-Flores et al, 2019 ).…”
Section: Discussionmentioning
confidence: 99%
“…Among the recombinant laccases, LAC 6 showed the highest ability to remove Remazol Brilliant Blue R (RBBR), Bromophenol blue (BB), Methyl orange (MO) and Malachite green (MG), with values between 73.1% and 91.5% after 24 h of incubation, suggesting that this laccase enzyme can be used for the treatment of textile industry effluents. George et al [ 191 ] utilized porous cross-linked enzyme aggregates (CLEAs) of P. ostreatus laccase for the decolorization and detoxification of triarylmethane and azo dyes, reactive blue 2 (RB) and malachite green (MG). The CLEAs of the laccase decolorized 500 ppm of MG and RB with 98.12 and 58.33% efficiency after 120 min, at a pH 5.0 and 50 °C, without a mediator.…”
Section: Bioremediation By White Rot Fungimentioning
confidence: 99%
“…CLEAs are carrier-free cross-linking methods, meaning that they are more cost-effective than other immobilization methods that use support materials. Hence, the ability of laccase-CLEAs to degrade dyes was tested [78]. Laccase-CLEAs showed good operational stability in the batch reactor (centrifuge tube), with their degradation activities being 89% and 12% at the sixth cycle for MG and RB2, respectively.…”
Section: Dyesmentioning
confidence: 99%