A new versatile peroxidase from <i>Pleurotus</i>

Ruíz-Dueñas, Francisco J.; Camarero, Susana; Pérez-Boada, Marta; Martı́nez, Marı́a Jesús; Martı́nez, Ángel T.

doi:10.1042/bst0290116

Cited by 110 publications

(13 citation statements)

References 8 publications

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“…This is the case for basidiomycete peroxidases including: Coprinus cinereus peroxidase (CIP), that is expressed with high yields in A. oryzae (CIP* is commercialized by Novozymes, Denmark); P. chrysosporium MnP and Caldariomyces fumago chloroperoxidase, which can be expressed with low yields in A. niger [22,24,50] and, in the case of MnP, also in A. oryzae [20]; and P. chrysosporium LiP, which failed to be expressed in any of the above systems [51]. It has been shown that the P. eryngii VP is more related to LiP than MnP in both protein sequence (and molecular structure) and gene regulation [14,52]. Therefore, the heterologous expression yields reported here, as well as in previous studies [12], are especially relevant, although they should be improved for biotechnological applications in sectors such as paper pulp bleaching and dye decolorization where high amounts of low price enzyme are required.…”

Section: Vp* Production In Aspergillus Nigermentioning

confidence: 99%

Effect of culture temperature on the heterologous expression of Pleurotus eryngii versatile peroxidase in Aspergillus hosts

Eibes

Lú-Chau

Ruíz-Dueñas

et al. 2008

Bioprocess Biosyst Eng

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Production of recombinant versatile peroxidase in Aspergillus hosts was optimized through the modification of temperature during bioreactor cultivations. To further this purpose, the cDNA encoding a versatile peroxidase of Pleurotus eryngii was expressed under control of the alcohol dehydrogenase (alcA) promoter of Aspergillus nidulans. A dependence of recombinant peroxidase production on cultivation temperature was found. Lowering the culture temperature from 28 to 19 degrees C enhanced the level of active peroxidase 5.8-fold and reduced the effective proteolytic activity twofold. Thus, a maximum peroxidase activity of 466 U L(-1) was reached. The same optimization scheme was applied to a recombinant Aspergillus niger that bore the alcohol dehydrogenase regulator (alcR), enabling transformation with the peroxidase cDNA under the same alcA promoter. However, with this strain, the peroxidase activity was not improved, while the effective proteolytic activity was increased between 3- and 11-fold compared to that obtained with A. nidulans.

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Section: Vp* Production In Aspergillus Nigermentioning

confidence: 99%

Effect of culture temperature on the heterologous expression of Pleurotus eryngii versatile peroxidase in Aspergillus hosts

Eibes

Lú-Chau

Ruíz-Dueñas

et al. 2008

Bioprocess Biosyst Eng

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“…to Mn 3+ at around pH 5.0 while aromatic compounds at around pH 3.0, despite the presence of Mn 2+ (Heinfling et al, 1998;Ruiz-Duenas et al, 2001). …”

Section: +mentioning

confidence: 99%

Bio-removal of Azo Dyes: A Review

Singh

2017

Int J Appl Sci Biotechnol

141

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Synthetic dyes are widely used in textile, paper, food, cosmetics and pharmaceutical industries with the textile industry as the largest consumer. Among all the available synthetic dyes, azo dyes are the largest group of dyes used in textile industry. Textile dyeing and finishing processes generate a large amount of dye containing wastewater which is one of the main sources of water pollution problems worldwide. Several physico-chemical methods have been applied to the treatment of textile wastewater but these methods have many limitations due to high cost, low efficiency and secondary pollution problems. As an alternative to physico-chemical methods, biological methods comprise bacteria, fungi, yeast, algae and plants and their enzymes which received increasing interest due to their cost effectiveness and eco-friendly nature. Decolorization of azo dyes by biological processes may take place either by biosorption or biodegradation. A variety of reductive and oxidative enzymes may also be involved in the degradation of dyes. This review provides an overview of decolorization and degradation of azo dyes by biological processes and establishes the fact that these microbial and plant cells are significantly effective biological weapon against the toxic azo dyes.

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“…Therefore, LRET pathways from the exterior of the enzyme to the heme cofactor represent a reasonable alternative to explain oxidation of redox mediators, aromatic substrates, and even polymeric lignin performed by LiPs and VPLs enzymes (Pérez-Boada et al, 2005; Morgenstern et al, 2008). Different studies applying crystallographic models (Pérez-Boada et al, 2005; Sundaramoorthy et al, 2005) and site-directed mutagenesis (Gelpke et al, 2002; Pérez-Boada et al, 2005) demonstrated experimentally the occurrence of the LRET I and II pathways in VPLs from Pleurotus eryngii (Pérez-Boada et al, 2005; Ruiz-Dueñas et al, 2009) and in LiPs from Phanerochaete chrysosporium (Ruiz-Dueñas et al, 2001). However, the LRET III is absent from the crystal structure of the VPLs of Pleurotus eryngii and has not been confirmed experimentally in LiPs (Morgenstern et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

Diversity of Ligninolytic Enzymes and Their Genes in Strains of the Genus Ganoderma: Applicable for Biodegradation of Xenobiotic Compounds?

Torres-Farradá

León²,

Rineau

et al. 2017

Front. Microbiol.

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White-rot fungi (WRF) and their ligninolytic enzymes (laccases and peroxidases) are considered promising biotechnological tools to remove lignin related Persistent Organic Pollutants from industrial wastewaters and contaminated ecosystems. A high diversity of the genus Ganoderma has been reported in Cuba; in spite of this, the diversity of ligninolytic enzymes and their genes remained unexplored. In this study, 13 native WRF strains were isolated from decayed wood in urban ecosystems in Havana (Cuba). All strains were identified as Ganoderma sp. using a multiplex polymerase chain reaction (PCR)-method based on ITS sequences. All Ganoderma sp. strains produced laccase enzymes at higher levels than non-specific peroxidases. Native-PAGE of extracellular enzymatic extracts revealed a high diversity of laccase isozymes patterns between the strains, suggesting the presence of different amino acid sequences in the laccase enzymes produced by these Ganoderma strains. We determined the diversity of genes encoding laccases and peroxidases using a PCR and cloning approach with basidiomycete-specific primers. Between two and five laccase genes were detected in each strain. In contrast, only one gene encoding manganese peroxidase or versatile peroxidase was detected in each strain. The translated laccases and peroxidases amino acid sequences have not been described before. Extracellular crude enzymatic extracts produced by the Ganoderma UH strains, were able to degrade model chromophoric compounds such as anthraquinone and azo dyes. These findings hold promises for the development of a practical application for the treatment of textile industry wastewaters and also for bioremediation of polluted ecosystems by well-adapted native WRF strains.

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A new versatile peroxidase from Pleurotus

Cited by 110 publications

References 8 publications

Effect of culture temperature on the heterologous expression of Pleurotus eryngii versatile peroxidase in Aspergillus hosts

Effect of culture temperature on the heterologous expression of Pleurotus eryngii versatile peroxidase in Aspergillus hosts

Bio-removal of Azo Dyes: A Review

Diversity of Ligninolytic Enzymes and Their Genes in Strains of the Genus Ganoderma: Applicable for Biodegradation of Xenobiotic Compounds?

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