Recombinant expression of four oxidoreductases in Phanerochaete chrysosporium improves degradation of phenolic and non-phenolic substrates

Coconi-Linares, Nancy; Ortiz-Vázquez, Elizabeth; Fernández, Francisco; Loske, Achim M.; Gómez-Lim, Miguel Á.

doi:10.1016/j.jbiotec.2015.06.401

Cited by 42 publications

(23 citation statements)

References 45 publications

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“…43 Further strain engineering included the introduction of an additional laccase. 44 In addition to LiP, MnP and VP, fungal DyP-type peroxidases have also been expressed in various heterologous production platforms, [45][46][47][48] with yields of 0.1 mg L ¡1 purified enzyme achieved using E. coli 47 and up to 62 mg L ¡1 recovered from the supernatant of A. oryzae expression cultures. 45 The production of several recombinant bacterial lignin-degrading enzymes has also been achieved over the last few years ( Table 2).…”

Section: Recombinant Lignin-degrading Peroxidasesmentioning

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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Section: Recombinant Lignin-degrading Peroxidasesmentioning

confidence: 99%

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

et al. 2016

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“…This approach could eliminate the necessity of using different fungal species and increase the fermentability of lignocellulosic feedstocks in a single bioreactor, thus reducing the cost of biofuel production. In this regard, we previously demonstrated the successful constitutive overexpression of 4 key oxidoreductases (MnP, LiP, VP, and LAC) in the white-rot fungus P. chrysosporium [Coconi-Linares et al, 2015]. The results presented in that work demonstrated that P. chrysospo rium transformants significantly enhanced the degradation of different synthetic compounds in comparison to the control strain.…”

Section: Introductionmentioning

confidence: 84%

“…The generation and selection of recombinant P. chrysosporium TF1, TF2, TF3, and TF9 strains overexpressing the MnP1, LiPH8, VPL2, and LACIIIb oxidoreductases used in the present study have been described previously [Coconi-Linares et al, 2015]. To transform P. chrysosporium, a suspension of intact conidia was exposed to 150 shock waves at a rate of 0.5 Hz, produced with a Piezolith 2501-based experimental shock-wave generator (Richard Wolf GmbH, Knittlingen, Germany).…”

Section: Microorganism and Culture Conditionsmentioning

confidence: 99%

“…VP activity was conducted by monitoring the oxidation of 1 mM of DMP in 100 mM sodium tartrate buffer (pH 3) in the presence of 0.1 mM H 2 O 2 (ε 469 = 27,500 M -1 cm -1 ). LAC activity was determined by the oxidation of ABTS (ε 420 = 36,000 M -1 cm -1 ), DMP (ε 469 = 27,500 M -1 cm -1 ) and GUA (ε 465 = 12,100 M -1 cm -1 ) [Coconi-Linares et al, 2015]. The reaction mixture contained either 1 mM ABTS, 1 mM DMP, or 2 mM GUA in 100 mM citrate-phosphate buffer (pH 3.0).…”

Section: Enzyme Assaysmentioning

confidence: 99%

“…The white-rot fungus Phanerochaete chrysosporium is considered an exceptional organism for its ability to depolymerize and modify lignin, as well as cellulose and hemicellulose, in comparison with other basidiomycetes [Coconi-Linares et al, 2015;Shrestha et al, 2015]. For these reasons, this fungus has been widely used as a biological alternative for lignocellulosic biomass degradation [Plácido and Capareda, 2015;Yao et al, 2014].…”

Section: Introductionmentioning

confidence: 99%

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Enhanced Delignification of Lignocellulosic Biomass by Recombinant Fungus <b><i>Phanerochaete chrysosporium</i></b> Overexpressing Laccases and Peroxidases

et al. 2018

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Ligninolytic enzyme production and lignin degradation are typically the rate-limiting steps in the biofuel industry. To improve the efficiency of simultaneous bio-delignification and enzyme production, Phanerochaete chrysosporium was transformed by shock wave-induced acoustic cavitation to co-overexpress 3 peroxidases and 1 laccase and test it on the degradation of sugarcane bagasse and wheat bran. Lignin depolymerization was enhanced by up to 25% in the presence of recombinant fungi in comparison with the wild-type strain. Sugar release on lignocellulose was 2- to 6-fold higher by recombinant fungi as compared with the control. Wheat bran ostensibly stimulated the production of ligninolytic enzymes. The highest peroxidase activity from the recombinant strains was 2.6-fold higher, whereas the increase in laccase activity was 4-fold higher in comparison to the control. The improvement of lignin degradation was directly proportional to the highest peroxidase and laccase activity. Because various phenolic compounds released during lignocellulose degradation have proven to be toxic to cells and to inhibit enzyme activity, a significant reduction (over 40%) of the total phenolic content in the samples treated with recombinant strains was observed. To our knowledge, this is the first report that engineering P. chrysosporium enhances biodegradation of lignocellulosic biomass.

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Recent Developments in Synthetic Biology and their Role in Uplifting Lignocellulose Bioeconomy

Sarkar¹,

Vamsidhar²,

Khaitan³

et al. 2022

Lignocellulose Bioconversion Through White Biotechnology

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Recombinant expression of four oxidoreductases in Phanerochaete chrysosporium improves degradation of phenolic and non-phenolic substrates

Cited by 42 publications

References 45 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

Enhanced Delignification of Lignocellulosic Biomass by Recombinant Fungus <b><i>Phanerochaete chrysosporium</i></b> Overexpressing Laccases and Peroxidases

Recent Developments in Synthetic Biology and their Role in Uplifting Lignocellulose Bioeconomy

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