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Enhanced delignification of steam-pretreated poplar by a bacterial laccase.

Identifieur interne : 001408 ( Main/Exploration ); précédent : 001407; suivant : 001409

Enhanced delignification of steam-pretreated poplar by a bacterial laccase.

Auteurs : Rahul Singh [Canada] ; Jinguang Hu [Canada] ; Matthew R. Regner [États-Unis] ; James W. Round [Canada] ; John Ralph [États-Unis] ; John N. Saddler [Canada] ; Lindsay D. Eltis [Canada]

Source :

RBID : pubmed:28169340

Descripteurs français

English descriptors

Abstract

The recalcitrance of woody biomass, particularly its lignin component, hinders its sustainable transformation to fuels and biomaterials. Although the recent discovery of several bacterial ligninases promises the development of novel biocatalysts, these enzymes have largely been characterized using model substrates: direct evidence for their action on biomass is lacking. Herein, we report the delignification of woody biomass by a small laccase (sLac) from Amycolatopsis sp. 75iv3. Incubation of steam-pretreated poplar (SPP) with sLac enhanced the release of acid-precipitable polymeric lignin (APPL) by ~6-fold, and reduced the amount of acid-soluble lignin by ~15%. NMR spectrometry revealed that the APPL was significantly syringyl-enriched relative to the original material (~16:1 vs. ~3:1), and that sLac preferentially oxidized syringyl units and altered interunit linkage distributions. sLac's substrate preference among monoaryls was also consistent with this observation. In addition, sLac treatment reduced the molar mass of the APPL by over 50%, as determined by gel-permeation chromatography coupled with multi-angle light scattering. Finally, sLac acted synergistically with a commercial cellulase cocktail to increase glucose production from SPP ~8%. Overall, this study establishes the lignolytic activity of sLac on woody biomass and highlights the biocatalytic potential of bacterial enzymes.

DOI: 10.1038/srep42121
PubMed: 28169340
PubMed Central: PMC5294454


Affiliations:


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Le document en format XML

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<term>Bacterial Proteins (chemistry)</term>
<term>Bacterial Proteins (isolation & purification)</term>
<term>Biocatalysis (MeSH)</term>
<term>Biofuels (supply & distribution)</term>
<term>Biomass (MeSH)</term>
<term>Cellulase (chemistry)</term>
<term>Humans (MeSH)</term>
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<term>Laccase (chemistry)</term>
<term>Laccase (isolation & purification)</term>
<term>Lignin (chemistry)</term>
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<term>Actinobacteria (composition chimique)</term>
<term>Actinobacteria (enzymologie)</term>
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<term>Cellulase (composition chimique)</term>
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<term>Laccase (isolement et purification)</term>
<term>Lignine (composition chimique)</term>
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<term>Protéines bactériennes (composition chimique)</term>
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<term>Laccase</term>
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<term>Laccase</term>
<term>Lignine</term>
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<div type="abstract" xml:lang="en">The recalcitrance of woody biomass, particularly its lignin component, hinders its sustainable transformation to fuels and biomaterials. Although the recent discovery of several bacterial ligninases promises the development of novel biocatalysts, these enzymes have largely been characterized using model substrates: direct evidence for their action on biomass is lacking. Herein, we report the delignification of woody biomass by a small laccase (sLac) from Amycolatopsis sp. 75iv3. Incubation of steam-pretreated poplar (SPP) with sLac enhanced the release of acid-precipitable polymeric lignin (APPL) by ~6-fold, and reduced the amount of acid-soluble lignin by ~15%. NMR spectrometry revealed that the APPL was significantly syringyl-enriched relative to the original material (~16:1 vs. ~3:1), and that sLac preferentially oxidized syringyl units and altered interunit linkage distributions. sLac's substrate preference among monoaryls was also consistent with this observation. In addition, sLac treatment reduced the molar mass of the APPL by over 50%, as determined by gel-permeation chromatography coupled with multi-angle light scattering. Finally, sLac acted synergistically with a commercial cellulase cocktail to increase glucose production from SPP ~8%. Overall, this study establishes the lignolytic activity of sLac on woody biomass and highlights the biocatalytic potential of bacterial enzymes.</div>
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