Industrial and biotechnological applications of laccases: A review

Couto, Susana Rodrı́guez; Toca-Herrera, José L.

doi:10.1016/j.biotechadv.2006.04.003

Cited by 1,116 publications

(354 citation statements)

References 165 publications

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“…The potential applications of these enzymes are enormous due to their oxidative versatility and low catalytic requirements: they use oxygen from the air and release water as the sole by-product (66). Indeed, their ability to catalyze both polymerization and degradation processes makes them suitable candidates as green biocatalysts in several sectors of industry, including textile and food industries, bioremediation, and forestry (wood and pulp) (53,63). Recent findings have also highlighted the potential of fungal laccases to be used for improving the conversion of plant biomass in future integrated lignocellulose biorefineries (16), in organic synthesis (32,52,64), and in bioelectrocatalysis (58).…”

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confidence: 99%

Engineering Platforms for Directed Evolution of Laccase from Pycnoporus cinnabarinus

Camarero

Pardo

Cañas

et al. 2012

Appl Environ Microbiol

123

173

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While the Pycnoporus cinnabarinus laccase (PcL) is one of the most promising high-redox-potential enzymes for environmental biocatalysis, its practical use has to date remained limited due to the lack of directed evolution platforms with which to improve its features. Here, we describe the construction of a PcL fusion gene and the optimization of conditions to induce its functional expression in Saccharomyces cerevisiae, facilitating its directed evolution and semirational engineering. The native PcL signal peptide was replaced by the ␣-factor preproleader, and this construct was subjected to six rounds of evolution coupled to a multiscreening assay based on the oxidation of natural and synthetic redox mediators at more neutral pHs. The laccase total activity was enhanced 8,000-fold: the evolved ␣-factor preproleader improved secretion levels 40-fold, and several mutations in mature laccase provided a 13.7-fold increase in k cat . While the pH activity profile was shifted to more neutral values, the thermostability and the broad substrate specificity of PcL were retained. Evolved variants were highly secreted by Aspergillus niger (ϳ23 mg/ liter), which addresses the potential use of this combined-expression system for protein engineering. The mapping of mutations onto the PcL crystal structure shed new light on the oxidation of phenolic and nonphenolic substrates. Furthermore, some mutations arising in the evolved preproleader highlighted its potential for heterologous expression of fungal laccases in yeast (S. cerevisiae).

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mentioning

confidence: 99%

Engineering Platforms for Directed Evolution of Laccase from Pycnoporus cinnabarinus

Camarero

Pardo

Cañas

et al. 2012

Appl Environ Microbiol

123

173

View full text Add to dashboard Cite

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“…In 2001, the company Zytex from India developed the formulation based on a laccase mediator system (LMS) Zylite ® capable of degrading indigo. Due to laccases potential to degrade dyes of diverse chemical structure, it seems an attractive solution for removal of dyes from industrial effl uents (Couto et al, 2006). Production of chemical pulp paper requires separation and degradation of lignin in wood pulp, pretreatments of wood pulp with ligninolytic enzymes provides milder and cleaner strategies than polluting chlorine-based procedures.…”

Section: Successful Application Of Laccasementioning

confidence: 99%

Laccase Application for Upgrading of Lignocellulose Fibers

Gabrič

Pohleven

2015

Drvna ind.

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“…Laccase purification from plant crude extracts is complex, and for this reason it has not been studied extensively [9]. In addition, Rodriguez Couto and Toca Herrera(2006) [11][13] [14] demonstrated in Trametes hirsuta that sequential addition of different carbon sources, such as glucose followed by glycerol, resulted in a higher laccase production rate, compared to cultures supplemented only with glucose or cellulose. Addition of mediators extend the use of laccases for industrial processes related to bioremediation; including delignification of lignocellulosics [10] [15].…”

Section: Introductionmentioning

confidence: 99%

White rot fungi 4222 degrade lignocellulose of corn straw

Hua¹,

Yan-li²,

Li³

et al. 2016

Proceedings of the 2016 6th International Conference on Advanced Design and Manufacturing Engineering (ICADME 2016)

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Abstract. The laccase of 4222 produced was investigated to the degradation ability of lignin and cellulose in the corn stalk powder solid Medium. The results showed that laccase peak was lat er than the liquid culture, arrived 1842.9 U/L on 15d. The training period of 30d, weight loss of powder dry straw was 82.48%, the lignin of 83.57% and the cellulose of 86.85% is degraded. 4222 has well ability to degrade of corn stove, and it is as a good candidate for lignin degradation.

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Industrial and biotechnological applications of laccases: A review

Cited by 1,116 publications

References 165 publications

Engineering Platforms for Directed Evolution of Laccase from Pycnoporus cinnabarinus

Engineering Platforms for Directed Evolution of Laccase from Pycnoporus cinnabarinus

Laccase Application for Upgrading of Lignocellulose Fibers

White rot fungi 4222 degrade lignocellulose of corn straw

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