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Journal article

Mapping the polysaccharide degradation potential of Aspergillus niger

From

Department of Systems Biology, Technical University of Denmark1

Center for Microbial Biotechnology, Department of Systems Biology, Technical University of Denmark2

Technical University of Denmark3

CBS-KNAW Fungal Biodiversity Centre4

Chalmers University of Technology5

Background: The degradation of plant materials by enzymes is an industry of increasing importance. For sustainable production of second generation biofuels and other products of industrial biotechnology, efficient degradation of non-edible plant polysaccharides such as hemicellulose is required. For each type of hemicellulose, a complex mixture of enzymes is required for complete conversion to fermentable monosaccharides.

In plant-biomass degrading fungi, these enzymes are regulated and released by complex regulatory structures. In this study, we present a methodology for evaluating the potential of a given fungus for polysaccharide degradation. Results: Through the compilation of information from 203 articles, we have systematized knowledge on the structure and degradation of 16 major types of plant polysaccharides to form a graphical overview.

As a case example, we have combined this with a list of 188 genes coding for carbohydrate-active enzymes from Aspergillus niger, thus forming an analysis framework, which can be queried. Combination of this information network with gene expression analysis on mono-and polysaccharide substrates has allowed elucidation of concerted gene expression from this organism.

One such example is the identification of a full set of extracellular polysaccharide-acting genes for the degradation of oat spelt xylan. Conclusions: The mapping of plant polysaccharide structures along with the corresponding enzymatic activities is a powerful framework for expression analysis of carbohydrate-active enzymes.

Applying this network-based approach, we provide the first genome-scale characterization of all genes coding for carbohydrate-active enzymes identified in A. niger.

Language: English
Publisher: BioMed Central
Year: 2012
Pages: 313
ISSN: 14712164
Types: Journal article
DOI: 10.1186/1471-2164-13-313
ORCIDs: Andersen, Mikael Rørdam

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