Breaking Down Lignin to High-Value Chemicals: The Conversion of Lignocellulose to Vanillin in a Gene Deletion Mutant of <i>Rhodococcus jostii</i> RHA1

Sainsbury, P. D.; Hardiman, Elizabeth M.; Ahmad, Masroor; Otani, Hiroshi; Seghezzi, Nicolas; Eltis, Lindsay D.; Bugg, Timothy D. H.

doi:10.1021/cb400505a

Cited by 230 publications

(188 citation statements)

References 23 publications

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“…We have shown that a vanillin dehydrogenase gene deletion mutant of R. jostii RHA1 is able to accumulate vanillin, a high value aromatic product, when grown in minimal media containing wheat straw lignocellulose as carbon source [14]. We have also identified a B-type DyP in…”

Section: Introductionmentioning

confidence: 92%

Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds

Rahmanpour

Rea

Jamshidi

et al. 2016

Archives of Biochemistry and Biophysics

105

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A Dyp-type peroxidase enzyme from thermophilic cellulose degrader Thermobifida fusca (TfuDyP) was investigated for catalytic ability towards lignin oxidation. TfuDyP was characterised kinetically against a range of phenolic substrates, and a compound I reaction intermediate was observed via pre-steady state kinetic analysis at max 404 nm. TfuDyP showed reactivity towards Kraft lignin, and was found to oxidise a -aryl ether lignin model compound, forming an oxidised dimer. A crystal structure of TfuDyP was determined, to 1.8Å resolution, which was found to contain a diatomic oxygen ligand bound to the heme centre, positioned close to active site residues Asp-203 and Arg-315. The structure contains two channels providing access to the heme cofactor for organic substrates and hydrogen peroxide. Site-directed mutant D203A showed no activity towards phenolic substrates, but reduced activity towards ABTS, while mutant R315Q showed no activity towards phenolic substrates, nor ABTS.

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Section: Introductionmentioning

confidence: 92%

Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds

Rahmanpour

Rea

Jamshidi

et al. 2016

Archives of Biochemistry and Biophysics

105

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“…Another DyP from R. jostii, which was expressed in its native host, was shown to be active against wheat straw lignocellulose and produced potentially valuable products, namely vanillin and smaller amounts of ferulic acid and 4-hydroxybenzaldehyde. 61 …”

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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“…In contrast to fungal peroxidases, several bacterial DyPtype peroxidases and laccases have been expressed at high levels in Escherichia coli [81,82] and efficient lignin degradation has been demonstrated for DyP-type peroxidases [83]. For example, a bacterial DyP-type peroxidase expressed in a gene deletion strain of Rhodococcus jostii (its native producer) efficiently degraded wheat straw lignocellulose and produced vanillin and small amounts of ferulic acid and 4-hydroxybenzaldehyde [83]. Such processes have proven feasible in the laboratory, and the next challenge is to scale up production to industrial levels.…”

Section: Bacterial Lignin Degradationmentioning

confidence: 99%

Lignin Degradation Processes and the Purification of Valuable Products

Schoenherr¹,

Ebrahimi²,

Czermak³

2018

Lignin - Trends and Applications

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Lignin is a heterogeneous, phenolic and polydisperse biopolymer which resists degradation due to its aromatic and highly branched structure. Lignin is the most abundant renewable source of aromatic molecules on earth. The valorization of lignin could therefore provide a sustainable alternative to petroleum refineries for the production of valuable aromatic compounds. Even so, paper mills and lignocellulose feedstock biorefineries treat lignin largely as a waste product. In paper mills, 98% of technical lignin is incinerated for internal energy recovery while only 2% is used commercially (e.g. for the production of aromatics such as vanillin). The reasons for the underutilization of lignin include its recalcitrance to degradation and the challenge of separating mixtures of numerous degradation products. The successful valorization of lignin in the future thus depends on a broad understanding of biological and technical degradation processes, and the implementation of efficient product purification strategies. This article describes enzymatic, photocatalytic and thermochemical lignin degradation processes and considers purification methods for valuable lignin-derived degradation products. We focus on the potential of membrane-based separation technology, including data from our own recent research.

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Breaking Down Lignin to High-Value Chemicals: The Conversion of Lignocellulose to Vanillin in a Gene Deletion Mutant of Rhodococcus jostii RHA1

Cited by 230 publications

References 23 publications

Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds

Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds

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

Lignin Degradation Processes and the Purification of Valuable Products

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