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Pathways for degradation of lignin in bacteria and fungi

Covering: up to 2011 Lignin is a heterogeneous aromatic polymer found as 10-35% of lignocellulose, found in plant cell walls. The bio-conversion of plant lignocellulose to glucose is an important part of second generation biofuel production, but the resistance of lignin to breakdown is a major obsta...

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Bibliographic Details
Published in:Natural product reports 2011-01, Vol.28 (12), p.1883-1896
Main Authors: Bugg, Timothy D. H, Ahmad, Mark, Hardiman, Elizabeth M, Rahmanpour, Rahman
Format: Article
Language:English
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Summary:Covering: up to 2011 Lignin is a heterogeneous aromatic polymer found as 10-35% of lignocellulose, found in plant cell walls. The bio-conversion of plant lignocellulose to glucose is an important part of second generation biofuel production, but the resistance of lignin to breakdown is a major obstacle in this process, hence there is considerable interest in the microbial breakdown of lignin. White-rot fungi are known to break down lignin with the aid of extracellular peroxidase and laccase enzymes. There are also reports of bacteria that can degrade lignin, and recent work indicates that bacterial lignin breakdown may be more significant than previously thought. The review will discuss the enzymes for lignin breakdown in fungi and bacteria, and the catabolic pathways for breakdown of the β-aryl ether, biphenyl and other components of lignin in bacteria and fungi. The review will also discuss small molecule phenolic breakdown products from lignin that have been identified from lignin-degrading microbes, and includes a bioinformatic analysis of the occurrence of known lignin-degradation pathways in Gram-positive and Gram-negative bacteria. Lignin is a major component of plant lignocellulose, the feedstock for conversion to biofuels and biorefinery products. This article describes recent progress in the understanding of the microbial breakdown of lignin, and catabolic pathways for the breakdown of lignin components.
ISSN:0265-0568
1460-4752
DOI:10.1039/c1np00042j