Magnetic cross-linked laccase aggregates — Bioremediation tool for decolorization of distinct classes of recalcitrant dyes

Kumar, Vikas; Sivanesan, S.; Cabana, Hubert

doi:10.1016/j.scitotenv.2014.04.009

Cited by 142 publications

(67 citation statements)

References 51 publications

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“…6a). The pH optima of the immobilized enzymes were also determined and were found to differ from the free enzyme preparation most likely due to changes in the structural conformation of the enzyme or the microenvironment induced by the immobilization method or the matrix (Bussamara et al 2012; Guzik et al 2014; Kumar et al 2014). The laccase immobilized on agarose beads reached maximum activity at pH 6.5 and the CLEAs reached maximum activity at pH 4.5 (Fig.…”

Section: Resultsmentioning

confidence: 99%

Heterologous expression of a Streptomyces cyaneus laccase for biomass modification applications

et al. 2017

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Laccases are used for the conversion of biomass into fermentable sugars but it is difficult to produce high yields of active laccases in heterologous expression systems. We overcame this challenge by expressing Streptomyces cyaneus CECT 3335 laccase in Escherichia coli (ScLac) and we achieved a yield of up to 104 mg L−1 following purification by one-step affinity chromatography. Stability and activity assays using simple lignin model substrates showed that the purified enzyme preparation was active over a broad pH range and at high temperatures, suggesting it would be suitable for biomass degradation. The reusability of ScLac was also demonstrated by immobilizing the enzyme on agarose beads with a binding yield of 33%, and by the synthesis of cross-linked enzyme aggregates with an initial activity recovery of 72%.Electronic supplementary materialThe online version of this article (doi:10.1186/s13568-017-0387-0) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Heterologous expression of a Streptomyces cyaneus laccase for biomass modification applications

et al. 2017

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“…In the cycle runs, the Lac-PAM-CTS worked longer than the free laccase, demonstrating the better stability and lower diffusion limitation of the Lac-PAM-CTS. The pseudo-first-order degradation rate constant (k 1 ) of MG in the Lac-PAM-CTS system reached up to 0.6 h À1 , which is outstanding among the immobilized laccase [2,39,40].…”

Section: Dye Decoloration With the Lac-pam-ctsmentioning

confidence: 94%

Immobilization of laccase in a sponge-like hydrogel for enhanced durability in enzymatic degradation of dye pollutants

Sun

Yang

Huang

et al. 2015

Journal of Colloid and Interface Science

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“…Compared with their free counterparts, immobilized laccases are more tolerant to high temperatures and storage and can be reused multiple times (Fernández-Fernández et al, 2013; Asgher et al, 2014), they are also more resistant to inhibitors such as NaCl (Yang et al, 2016c). Immobilization sometimes improves the catalytic activity of laccases (Arsenault et al, 2011; Sinirlioglu et al, 2013; Kumar et al, 2014) despite the common concern of reduced enzyme flexibility, steric hindrance and diffusion limitations (Sheldon, 2011; Talekar et al, 2013). Readers can refer to reviews on preparation and applications of immobilized laccases (Ba et al, 2013; Fernández-Fernández et al, 2013; Asgher et al, 2014).…”

Section: Laccase Immobilizationmentioning

confidence: 99%

Laccases: Production, Expression Regulation, and Applications in Pharmaceutical Biodegradation

et al. 2017

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Laccases are a family of copper-containing oxidases with important applications in bioremediation and other various industrial and biotechnological areas. There have been over two dozen reviews on laccases since 2010 covering various aspects of this group of versatile enzymes, from their occurrence, biochemical properties, and expression to immobilization and applications. This review is not intended to be all-encompassing; instead, we highlighted some of the latest developments in basic and applied laccase research with an emphasis on laccase-mediated bioremediation of pharmaceuticals, especially antibiotics. Pharmaceuticals are a broad class of emerging organic contaminants that are recalcitrant and prevalent. The recent surge in the relevant literature justifies a short review on the topic. Since low laccase yields in natural and genetically modified hosts constitute a bottleneck to industrial-scale applications, we also accentuated a genus of laccase-producing white-rot fungi, Cerrena, and included a discussion with regards to regulation of laccase expression.

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Magnetic cross-linked laccase aggregates — Bioremediation tool for decolorization of distinct classes of recalcitrant dyes

Cited by 142 publications

References 51 publications

Heterologous expression of a Streptomyces cyaneus laccase for biomass modification applications

Heterologous expression of a Streptomyces cyaneus laccase for biomass modification applications

Immobilization of laccase in a sponge-like hydrogel for enhanced durability in enzymatic degradation of dye pollutants

Laccases: Production, Expression Regulation, and Applications in Pharmaceutical Biodegradation

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