Lignin‐degrading enzymes

Pollegioni, Loredano; Tonin, Fabio; Rosini, Elena

doi:10.1111/febs.13224

Cited by 388 publications

(321 citation statements)

References 130 publications

(165 reference statements)

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“…12 Non-phenolic structures are thought to be degraded by LiP due to its high redox potential. MnP can oxidize phenolic model compounds via the oxidation of Mn 2C to Mn…”

Section: Lignin-degrading Enzymesmentioning

confidence: 99%

Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases

et al. 2016

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Lignin is 1 of the 3 major components of lignocellulose. Its polymeric structure includes aromatic subunits that can be converted into high-value-added products, but this potential cannot yet been fully exploited because lignin is highly recalcitrant to degradation. Different approaches for the depolymerization of lignin have been tested, including pyrolysis, chemical oxidation, and hydrolysis under supercritical conditions. An additional strategy is the use of lignin-degrading enzymes, which imitates the natural degradation process. A versatile set of enzymes for lignin degradation has been identified, and research has focused on the production of recombinant enzymes in sufficient amounts to characterize their structure and reaction mechanisms. Enzymes have been analyzed individually and in combinations using artificial substrates, lignin model compounds, lignin and lignocellulose. Here we consider progress in the production of recombinant lignin-degrading peroxidases, the advantages and disadvantages of different expression hosts, and obstacles that must be overcome before such enzymes can be characterized and used for the industrial processing of lignin.

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“…12 Non-phenolic structures are thought to be degraded by LiP due to its high redox potential. MnP can oxidize phenolic model compounds via the oxidation of Mn 2C to Mn…”

Section: Lignin-degrading Enzymesmentioning

confidence: 99%

Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases

et al. 2016

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“…Lignin degrading enzymes include laccase, manganese peroxidase (MnP) and lignin peroxidase (LiP) (Pollegioni et al, 2015). While laccase requires oxygen for its activity, MnP and LiP require hydrogen peroxide.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of 18 isolates of basidiomycetes for Lignocellulose degrading enzymes

Kathirgamanathan¹,

Abayasekara²,

Kulasooriya³

et al. 2017

Ceylon J. Sci.

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Since fossil fuel resources are limited there is a necessity to produce alternative types of fuel that are renewable and eco-friendly. Basidiomycetes are potential sources of enzymes that can be used for biofuel production. The current study aimed to isolate basidiomycetes from Sri Lanka, screen them for lignocellulose degrading enzymes, namely cellulase, xylanase, laccase, Mn peroxidase and lignin peroxidase and study the effect of potential inducers of laccase production. Among the eighteen basidiomycetes isolated, Pycnoporus sp. produced the highest cellulase activity (0.23 FPU/ml) whereas Phlebiopsis sp. produced the highest xylanase activity (5.4 U/ml). Earliella scabrosa produced the highest laccase (91.2 U/l) and Mn peroxidase (17.5 U/l) activities. Lignin peroxidase activity was not detected from the isolates. Effect of alkali lignin, Cu 2+ and rice bran, three potential inducers, on laccase production by E. scabrosa, Pycnoporus sp. and Trametes hirsuta (M40) was studied. Results indicated that alkali lignin (2 g/l) significantly increased laccase production from Pycnoporus sp. and T. hirsuta (M40) while Cu 2+ increased laccase production from E. scabrosa and T. hirsuta at 200 µM. Use of rice bran (10 g/l) resulted in higher laccase production from E. scabrosa and Pycnoporus sp. High laccase activity (79600 U/l) was obtained from E. scabrosa by using 50 g/l of rice bran and by extending the incubation period to 18 days. The study concluded that some of the basidiomycetes isolated can produce significant lignocellulose degrading enzyme activities.

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“…More favorable techniques, based on the use of lignin-degrading enzymes, such as laccase and lignin peroxidase, have long been identified; however, their utilization in the biofuel production process is currently limited (7). Laccases (EC 1.10.3.2) are wellstudied blue multicopper oxidases (type 1) found in fungi, plants, and microorganisms that catalyze the oxidation of a wide variety of phenolic and nonphenolic compounds, with concomitant reduction of molecular oxygen to water (8)(9)(10). The broad substrate range of laccases allows their use in numerous types of industrial and biotechnological fields, such as the paper, textile, and food industries (11)(12)(13)(14).…”

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confidence: 99%

Toward combined delignification and saccharification of wheat straw by a laccase-containing designer cellulosome

Davidi

Moraïs

Artzi

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Efficient breakdown of lignocellulose polymers into simple molecules is a key technological bottleneck limiting the production of plant-derived biofuels and chemicals. In nature, plant biomass degradation is achieved by the action of a wide range of microbial enzymes. In aerobic microorganisms, these enzymes are secreted as discrete elements in contrast to certain anaerobic bacteria, where they are assembled into large multienzyme complexes termed cellulosomes. These complexes allow for very efficient hydrolysis of cellulose and hemicellulose due to the spatial proximity of synergistically acting enzymes and to the limited diffusion of the enzymes and their products. Recently, designer cellulosomes have been developed to incorporate foreign enzymatic activities in cellulosomes so as to enhance lignocellulose hydrolysis further. In this study, we complemented a cellulosome active on cellulose and hemicellulose by addition of an enzyme active on lignin. To do so, we designed a dockerin-fused variant of a recently characterized laccase from the aerobic bacterium Thermobifida fusca. The resultant chimera exhibited activity levels similar to the wild-type enzyme and properly integrated into the designer cellulosome. The resulting complex yielded a twofold increase in the amount of reducing sugars released from wheat straw compared with the same system lacking the laccase. The unorthodox use of aerobic enzymes in designer cellulosome machinery effects simultaneous degradation of the three major components of the plant cell wall (cellulose, hemicellulose, and lignin), paving the way for more efficient lignocellulose conversion into soluble sugars en route to alternative fuels production.

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Lignin‐degrading enzymes

Cited by 388 publications

References 130 publications

Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases

Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases

Evaluation of 18 isolates of basidiomycetes for Lignocellulose degrading enzymes

Toward combined delignification and saccharification of wheat straw by a laccase-containing designer cellulosome

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