Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: December 18, 2009
Publication Date: March 12, 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 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.