S114: Glycoside hydrolase families of Acidothermus cellulolyticus and their potential for bioenergy applications

Wednesday, August 4, 2010: 10:30 AM
Seacliff CD (Hyatt Regency San Francisco)
William S. Adney1, Eric P. Knoshaug2, Jeffrey G. Linger2, Vladimir V. Lunin3, Markus Alahuhta3 and M.E. Himmel1, (1)National Renewable Energy Laboratory, Golden, CO, (2)National Bioenergy Center, National Renewable Energy Laboratory, Golden, CO, (3)Biosciences Center, National Renewable Energy Laboratory, Golden, CO
The glycosyl hydrolases encompass a large medley of diverse enzymes used in a myriad of industrial processes including the paper, pulping, food and agriculture industries. This medley of enzymes is experiencing increased interest for the enzymatic pretreatment of biomass for the production of biofuels. With the recently completed sequencing of the Acidothermus cellulolyticus 11B (ATCC43068) genome by the DOE’s Joint Genome Institute (JGI), it is now possible to investigate the cellulase and hemicellulase systems of this highly thermotolerant bacterium. The bacterium was isolated using a screen for efficient and complete cellulose degradation by microorganisms residing in acidic hot springs in Yellowstone National Park. The 2.4 MB genome is approximately 67% GC-rich and encodes a predicted total 2151 proteins. Members of the Frankia sp., mesophilic, nitrogen-fixing plant root symbionts, are the closest phylogenetic neighbors to A. cellulolyticus. We are currently characterizing a selection of the genes identified as belonging to the various glycosyl hydrolase families.