Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: December 18, 2009
Publication Date: March 21, 2010
Citation: Lee, C.C., Kibblewhite, R.E., Wagschal, K.C., Wong, D., Orts, W.J. 2010. Cloning and characterization of alpha-glucuronidase enzyme. Meeting Abstract. Technical Abstract: Hemicellulose is the second largest source of biomass on Earth. Xylan, a polymer of beta-1,4-linked xylose residues, is a common component of hemicellulose. The enzymes xylanase and beta-xylosidase hydrolyze the xylan into xylose which can then be fermented into value-added products. However, the accessibility of the substrate is blocked by chemical moieties found on the xylan polymer. One of the most common of these chemical moieties is alpha-glucuronic acid which is attached to the xylose residue via a 1,2-glycosidic linkage. The alpha-glucuronidase enzyme releases the glucuronic acid from the xylose residue and thus allows for full hydrolysis of the xylan polymer. We cloned a gene encoding an alpha-glucuronidase enzyme from a mixed microbial population and biochemically characterized the enzyme and demonstrated its ability to increase overall xylan hydrolysis.