Publication: Research - peer-review › Journal article – Annual report year: 2012
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.
|Citations||Web of Science® Times Cited: 1|
- 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
No data available