Efficient decolorization of recalcitrant dyes at neutral/alkaline pH by a new bacterial laccase-mediator system

Coria-Oriundo, Lucy L.; Battaglini, Fernando; Wirth, Sonia

doi:10.1016/j.ecoenv.2021.112237

Cited by 26 publications

(7 citation statements)

References 80 publications

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“…In both variants, no decolorization was detected in the absence of ABTS. This finding is consistent with previous studies [ 33 ], which have shown that CotA laccase cannot directly decolorize indigo carmine but the presence of the mediator ABTS could significantly enhance the decolorization [ 45 , 46 ]. When 3.33 μg/mL protein was used, the decolorization of both the wildtype BsCotA and AncCotA2 exhibited linear responses (see Figure 3 and Figure S5 ).…”

Section: Discussionsupporting

confidence: 93%

An Inferred Ancestral CotA Laccase with Improved Expression and Kinetic Efficiency

Lei

Zhao

Hou

et al. 2023

IJMS

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Laccases are widely used in industrial production due to their broad substrate availability and environmentally friendly nature. However, the pursuit of laccases with superior stability and increased heterogeneous expression to meet industry demands appears to be an ongoing challenge. To address this challenge, we resurrected five ancestral sequences of laccase BsCotA and their homologues. All five variants were successfully expressed in soluble and functional forms with improved expression levels in Escherichia coli. Among the five variants, three exhibited higher catalytic rates, thermal stabilities, and acidic stabilities. Notably, AncCotA2, the best-performing variant, displayed a kcat/KM of 7.5 × 105 M−1·s−1, 5.2-fold higher than that of the wild-type BsCotA, an improved thermo- and acidic stability, and better dye decolorization ability. This study provides a laccase variant with high application potential and presents a new starting point for future enzyme engineering.

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Section: Discussionsupporting

confidence: 93%

An Inferred Ancestral CotA Laccase with Improved Expression and Kinetic Efficiency

Lei

Zhao

Hou

et al. 2023

IJMS

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“…Relatively low redox potential limits the catalytic activity of bacterial laccases for many substrates. Previous study reveals that the redox mediators can enhance the capacity of laccases for oxidizing various substrates, including HMF [ 26 , 27 , 29 , 37 ]. The typical mediator among the synthetic mediators, 2,2,6,6-tetramethyl-1-piperidinyloxy (TEMPO), is widely used in LMS for HMF oxidation by bacterial laccase [ 34 , 35 ].…”

Section: Resultsmentioning

confidence: 99%

Effective biosynthesis of 2,5-furandicarboxylic acid from 5-hydroxymethylfurfural via a bi-enzymatic cascade system using bacterial laccase and fungal alcohol oxidase

Yang,

Liu,

et al. 2023

Biotechnol Biofuels

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Background As a cost-effective and eco-friendly approach, biocatalysis has great potential for the transformation of 5-hydroxymethylfurfural (HMF) into 2,5-furandicarboxylic acid (FDCA). However, the compatibility of each enzyme in the cascade reaction limits the transformation efficiency of HMF to FDCA. Results Coupled with an alcohol oxidase from Colletotrichum gloeosporioides (CglAlcOx), this study aims to study the potential of bacterial laccase from Bacillus pumilus (BpLac) in an enzymatic cascade for 2,5-furandicarboxylic acid (FDCA) biosynthesis from 5-hydroxymethylfurfural (HMF). BpLac showed 100% selectivity for HMF oxidation and generated 5-hydroxymethyl-2-furancarboxylic acid (HMFCA). CglAlcOx was capable of oxidizing HMFCA to 2-formyl-5-furancarboxylic acid (FFCA). Both BpLac and CglAlcOx could oxidize FFCA to FDCA. At the 5 mM scale, a complete transformation of HMF with a 97.5% yield of FDCA was achieved by coupling BpLac with CglAlcOx in the cascade reaction. The FDCA productivity in the reaction was 5.3 mg/L/h. Notably, BpLac could alleviate the inhibitory effect of FFCA on CglAlcOx activity and boost the transformation efficiency of HMF to FDCA. Moreover, the reaction was scaled up to 40 times the volume, and FDCA titer reached 2.6 mM with a yield of 58.77% at 168 h. Conclusions This work provides a candidate and novel insight for better design of an enzymatic cascade in FDCA production.

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“…To achieve these results, a laccase‐mediator system along with acetosyringone and methyl syringate was used (Blánquez et al, 2019 ). In addition, the same small laccase SilA was recombinantly expressed in E. coli and shown to achieve high decolorization levels (more than 80% indigo carmine and malachite green at different pH (6.8–8.0) within 2 h (Coria‐Oriundo et al, 2021 )). This study also revealed that β‐(10‐phenothyazyl)‐propionic acid (PhCOOG) could be used as an efficient and affordable mediator in combination with recombinant SilA and could support the decolorization of remanzol brilliant blue R (an anthraquinone dye) by >40% and 80% decolorization of xylidine ponceau (azo dye; Coria‐Oriundo et al, 2021 ).…”

Section: Biotechnological Approaches Using Streptomyces ...mentioning

confidence: 99%

Streptomyces spp. as biocatalyst sources in pulp and paper and textile industries: Biodegradation, bioconversion and valorization of waste

Cuebas-Irizarry

Grunden

2023

Microbial Biotechnology

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Complex polymers represent a challenge for remediating environmental pollution and an opportunity for microbial‐catalysed conversion to generate valorized chemicals. Members of the genus Streptomyces are of interest because of their potential use in biotechnological applications. Their versatility makes them excellent sources of biocatalysts for environmentally responsible bioconversion, as they have a broad substrate range and are active over a wide range of pH and temperature. Most Streptomyces studies have focused on the isolation of strains, recombinant work and enzyme characterization for evaluating their potential for biotechnological application. This review discusses reports of Streptomyces‐based technologies for use in the textile and pulp‐milling industry and describes the challenges and recent advances aimed at achieving better biodegradation methods featuring these microbial catalysts. The principal points to be discussed are (1) Streptomyces' enzymes for use in dye decolorization and lignocellulosic biodegradation, (2) biotechnological processes for textile and pulp and paper waste treatment and (3) challenges and advances for textile and pulp and paper effluent treatment.

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Efficient decolorization of recalcitrant dyes at neutral/alkaline pH by a new bacterial laccase-mediator system

Cited by 26 publications

References 80 publications

An Inferred Ancestral CotA Laccase with Improved Expression and Kinetic Efficiency

An Inferred Ancestral CotA Laccase with Improved Expression and Kinetic Efficiency

Effective biosynthesis of 2,5-furandicarboxylic acid from 5-hydroxymethylfurfural via a bi-enzymatic cascade system using bacterial laccase and fungal alcohol oxidase

Streptomyces spp. as biocatalyst sources in pulp and paper and textile industries: Biodegradation, bioconversion and valorization of waste

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