Abstract
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.
Original language | English |
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Journal | B M C Genomics |
Volume | 13 |
Number of pages | 17 |
ISSN | 1471-2164 |
DOIs | |
Publication status | Published - 2012 |
Keywords
- BIOTECHNOLOGY
- GENETICS
- ALPHA-L-ARABINOFURANOSIDASE
- FAMILY-3 BETA-GLUCOSIDASE
- TRANSCRIPTIONAL ACTIVATOR XLNR
- CELL-WALL POLYSACCHARIDES
- SITE-DIRECTED MUTAGENESIS
- PECTIN LYASE-A
- ENDO-POLYGALACTURONASE-II
- XYLAN DEGRADING ENZYMES
- FERULIC ACID ESTERASE
- 2 ENDOINULINASE GENES