Characterization of Thiamine Diphosphate-Dependent 4-Hydroxybenzoylformate Decarboxylase Enzymes from Rhodococcus jostii RHA1 and Pseudomonas fluorescens Pf-5 Involved in Degradation of Aryl C2 Lignin Degradation Fragments

Wei, Zhen; Wilkinson, Rachael C.; Rashid, Goran M. M.; Brown, D. J. A.; Fülöp, Vilmos; Bugg, Timothy D. H.

doi:10.1021/acs.biochem.9b00177

Cited by 21 publications

(32 citation statements)

References 48 publications

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“…3). In particular, glcD and HAO could be accessory enzymes for lignin degradation, by generating hydrogen peroxide for peroxidase enzymes, and potentially detoxifying aldehyde byproducts [44]. These findings can be an indication of the large enzymatic potential to breakdown lignin in the soil-derived consortia.…”

Section: Abundance Of Lignin-transforming Enzyme-encoding Genesmentioning

confidence: 95%

Exploring the Lignin Catabolism Potential of Soil-Derived Lignocellulolytic Microbial Consortia by a Gene-Centric Metagenomic Approach

2020

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An exploration of the ligninolytic potential of lignocellulolytic microbial consortia can improve our understanding of the eco-enzymology of lignin conversion in nature. In this study, we aimed to detect enriched lignin-transforming enzymes on metagenomes from three soil-derived microbial consortia that were cultivated on "pre-digested" plant biomass (wheat straw -WS1-M, switchgrass -SG-M and corn stover -CS-M). Of 60 selected enzyme-encoding genes putatively involved in lignin catabolism, 20 genes were significantly abundant in WS1-M, CS-M and/or SG-M consortia compared with the initial forest soil inoculum metagenome (FS1). These genes could be involved in lignin oxidation (e.g. superoxide dismutases), oxidative stress responses (e.g. catalase/peroxidases), generation of protocatechuate (e.g. vanAB genes), catabolism of gentisate, catechol and 3phenylpropionic acid (e.g. gentisate 1,2-dioxygenases, muconate cycloisomerases and hcaAB genes), the beta-ketoadipate pathway (e.g. pcaIJ genes) and tolerance to lignocellulose-derived inhibitors (e.g. thymidylate synthases). The taxonomic affiliation of 22 selected lignin-transforming enzymes from WS1-M and CS-M consortia metagenomes revealed that Pseudomonadaceae, Alcaligenaceae, Sphingomonadaceae, Caulobacteraceae, Comamonadaceae and Xanthomonadaceae are the key bacterial families in the catabolism of lignin. We sketched out a predictive "model" where each microbial population has the potential to metabolize an array of aromatic compounds through different pathways, suggesting that lignin catabolism can follow a "task division" strategy.Here, we have established an association between functions and taxonomy, allowing a better 2 understanding of lignin transformations in soil-derived lignocellulolytic microbial consortia, and pinpointing some bacterial taxa and catabolic genes as ligninolytic trait-markers.

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Section: Abundance Of Lignin-transforming Enzyme-encoding Genesmentioning

confidence: 95%

Exploring the Lignin Catabolism Potential of Soil-Derived Lignocellulolytic Microbial Consortia by a Gene-Centric Metagenomic Approach

2020

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“…The microbial degradation of large aromatic polymers such as lignin and its derivatives has gained extensive attention as an essential strategy for future bio-refineries, and circular bio-economy 1 – 3 . More so, the biological conversion of lignin and its derivatives has been an area of interest for many researchers due to the product specificity and mild conditions of the conversion processes 4 . The utilization of fungal systems, such as extracellular peroxidase and laccase from white and brown rot fungi 5 – 7 , on lignin derivatives degradation has been well established.…”

Section: Introductionmentioning

confidence: 99%

A novel Bacillus ligniniphilus catechol 2,3-dioxygenase shows unique substrate preference and metal requirement

Adewale

Lang

Huang

et al. 2021

Sci Rep

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Identification of novel enzymes from lignin degrading microorganisms will help to develop biotechnologies for biomass valorization and aromatic hydrocarbons degradation. Bacillus ligniniphilus L1 grows with alkaline lignin as the single carbon source and is a great candidate for ligninolytic enzyme identification. The first dioxygenase from strain L1 was heterologously expressed, purified, and characterized with an optimal temperature and pH of 32.5 °C and 7.4, respectively. It showed the highest activity with 3-ethylcatechol and significant activities with other substrates in the decreasing order of 3-ethylcatechol > 3-methylcatechol > 3-isopropyl catechol > 2, 3-dihydroxybiphenyl > 4-methylcatechol > catechol. It did not show activities against other tested substrates with similar structures. Most reported catechol 2,3-dioxygenases (C23Os) are Fe2+-dependent whereas Bacillus ligniniphilus catechol 2,3-dioxygenase (BLC23O) is more Mn2+- dependent. At 1 mM, Mn2+ led to 230-fold activity increase and Fe2+ led to 22-fold increase. Sequence comparison and phylogenetic analyses suggested that BL23O is different from other Mn-dependent enzymes and uniquely grouped with an uncharacterized vicinal oxygen chelate (VOC) family protein from Paenibacillus apiaries. Gel filtration analysis showed that BLC23O is a monomer under native condition. This is the first report of a C23O from Bacillus ligniniphilus L1 with unique substrate preference, metal-dependency, and monomeric structure.

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“…A copper-dependent oxidase enzyme has been identified in Thermobifida fusca, that has been shown to result in reduced lignin content in sugarcane bagasse, and generates dilignol products [47]. A new pathway for metabolism of aryl-C2 lignin fragments in Rhodococcus jostii RHA1 has also been shown to involve an FMNdependent oxidase enzyme that can oxidise aldehyde intermediates and simultaneously generate hydrogen peroxide [48].…”

Section: Lignin Degradation Accessory Enzymesmentioning

confidence: 99%

Bacterial enzymes for lignin depolymerisation: new biocatalysts for generation of renewable chemicals from biomass

Bugg

Williamson

Rashid

2020

Current Opinion in Chemical Biology

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Characterization of Thiamine Diphosphate-Dependent 4-Hydroxybenzoylformate Decarboxylase Enzymes from Rhodococcus jostii RHA1 and Pseudomonas fluorescens Pf-5 Involved in Degradation of Aryl C₂ Lignin Degradation Fragments

Abstract: Please refer to published version for the most recent bibliographic citation information. If a published version is known of, the repository item page linked to above, will contain details on accessing it.

Cited by 21 publications

References 48 publications

Exploring the Lignin Catabolism Potential of Soil-Derived Lignocellulolytic Microbial Consortia by a Gene-Centric Metagenomic Approach

Exploring the Lignin Catabolism Potential of Soil-Derived Lignocellulolytic Microbial Consortia by a Gene-Centric Metagenomic Approach

A novel Bacillus ligniniphilus catechol 2,3-dioxygenase shows unique substrate preference and metal requirement

Bacterial enzymes for lignin depolymerisation: new biocatalysts for generation of renewable chemicals from biomass

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