Depolymerization of lignosulfonates by submerged cultures of the basidiomycete Irpex consors and cloning of a putative versatile peroxidase

Imami, Adrian; Riemer, Stephanie J.L.; Schulze, Marcus; Amelung, F.; Gorshkov, Vladimir; Rühl, Martin; Ammenn, J.; Zorn, Holger

doi:10.1016/j.enzmictec.2015.07.007

Cited by 9 publications

(3 citation statements)

References 33 publications

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“…Homologous and heterologous expression of VP has been studied in a variety of prokaryotic and eukaryotic hosts (Table 2) [19,46,[52][53][54][55][56][57][58][59][60][61][62][63][64][65]. Expression of Bjerkandera adusta VP in prokaryotic E. coli BL21 (DE3) yielded 322 U/L of rVP [58].…”

Section: Discussionmentioning

confidence: 99%

Improvement of Saccharification and Delignification Efficiency of Trichoderma reesei Rut-C30 by Genetic Bioengineering

et al. 2020

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Trichoderma reesei produces various saccharification enzymes required for biomass degradation. However, the lack of an effective lignin-degrading enzyme system reduces the species’ efficiency in producing fermentable sugars and increases the pre-treatment costs for biofuel production. In this study, we heterologously expressed the Ganoderma lucidum RMK1 versatile peroxidase gene (vp1) in the Rut-C30 strain of T. reesei. The expression of purified 6×His-tag–containing recombinant G. lucidum-derived protein (rVP1) was confirmed through western blot, which exhibited a single band with a relative molecular weight of 39 kDa. In saccharification and delignification studies using rice straw, the transformant (tVP7, T. reesei Rut-C30 expressing G. lucidum-derived rVP1) showed significant improvement in the yield of total reducing sugar and delignification, compared with that of the parent T. reesei Rut-C30 strain. Scanning electron microscopy (SEM) of tVP7-treated paddy straw showed extensive degradation of several layers of its surface compared with the parent strain due to the presence of G. lucidum-derived rVP1. Our results suggest that the expression of ligninolytic enzymes in cellulase hyperproducing systems helps to integrate the pre-treatment and saccharification steps that may ultimately reduce the costs of bioethanol production.

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Section: Discussionmentioning

confidence: 99%

Improvement of Saccharification and Delignification Efficiency of Trichoderma reesei Rut-C30 by Genetic Bioengineering

et al. 2020

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“…Aiming at the liberation of glucose enclosed in lignocellulosics for biofuel production, a lot of the recent research focused on lignin degradation and consequently on oxidoreductases, such as peroxidases [60][61][62] and laccases [63,64], which are secreted by xylophilic basidiomycetes to secure their nutrient demands.…”

Section: Redox Processesmentioning

confidence: 99%

Improved Foods Using Enzymes from Basidiomycetes

Berger

Ersoy

2022

Processes

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Within the kingdom of fungi, the division Basidiomycota represents more than 30,000 species, some with huge genomes indicating great metabolic potential. The fruiting bodies of many basidiomycetes are appreciated as food (“mushrooms”). Solid-state and submerged cultivation processes have been established for many species. Specifically, xylophilic fungi secrete numerous enzymes but also form smaller metabolites along unique pathways; both groups of compounds may be of interest to the food processing industry. To stimulate further research and not aim at comprehensiveness in the broad field, this review describes some recent progress in fermentation processes and the knowledge of fungal genetics. Processes with potential for food applications based on lipases, esterases, glycosidases, peptidases and oxidoreductases are presented. The formation and degradation of colourants, the degradation of harmful food components, the formation of food ingredients and particularly of volatile and non-volatile flavours serve as examples. In summary, edible basidiomycetes are foods—and catalysts—for food applications and rich donors of genes to construct heterologous cell factories for fermentation processes. Options arise to support the worldwide trend toward greener, more eco-friendly and sustainable processes.

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“…Direct or indirect involvement of versatile peroxidase in degrading phenolic and non-phenolic pollutants, lignosulfonates, and xenobiotics has been discovered for many lignin-utilizing basidiomycetes [ 119 , 120 ]. As a hybrid of MnP and LiP, VP has been found in Pleurotus eryngii , Bjerkandera sp., P. pulmonarius, P. ostreatus , and B. adusta .…”

Section: Linking Oxidative Ability Of Lignin-degrading Enzymes To mentioning

confidence: 99%

Linking Enzymatic Oxidative Degradation of Lignin to Organics Detoxification

Wang

Yao

2018

IJMS

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The major enzymes involved in lignin degradation are laccase, class II peroxidases (lignin peroxidase, manganese peroxidase, and versatile peroxidase) and dye peroxidase, which use an oxidative or peroxidative mechanism to deconstruct the complex and recalcitrant lignin. Laccase and manganese peroxidase directly oxidize phenolic lignin components, while lignin peroxidase and versatile peroxidase can act on the more recalcitrant non-phenolic lignin compounds. Mediators or co-oxidants not only increase the catalytic ability of these enzymes, but also largely expand their substrate scope to those with higher redox potential or more complicated structures. Neither laccase nor the peroxidases are stringently selective of substrates. The promiscuous nature in substrate preference can be employed in detoxification of a range of organics.

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Depolymerization of lignosulfonates by submerged cultures of the basidiomycete Irpex consors and cloning of a putative versatile peroxidase

Cited by 9 publications

References 33 publications

Improvement of Saccharification and Delignification Efficiency of Trichoderma reesei Rut-C30 by Genetic Bioengineering

Improvement of Saccharification and Delignification Efficiency of Trichoderma reesei Rut-C30 by Genetic Bioengineering

Improved Foods Using Enzymes from Basidiomycetes

Linking Enzymatic Oxidative Degradation of Lignin to Organics Detoxification

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