5-19: Sequence analysis of glycoside hydrolase family 7 cellobiohydrolases for research and licensing opportunities

Monday, May 2, 2011
Grand Ballroom C-D, 2nd fl (Sheraton Seattle)
Stacy A. Cremers1, Gregg T. Beckham2, William S. Adney3, Michael E. Himmel3, Eric Payne1 and John Stolpa1, (1)Commercialization and Technology Transfer, NREL, Golden, CO, (2)National Bioenergy Science Center, NREL, Golden, CO, (3)Biosciences Center, NREL, Golden, CO
Members of the glycoside hydrolase family 7 cellobiohydrolases (Cel7A) are one of the most important classes of industrial enzymes as they provide significant hydrolytic potential in enzyme cocktails for biomass conversion. Here we develop and describe a database of the sequence and mutation space for Family 7 cellulases from patents and the open literature. All papers and patents describing mutant Cel7A protein sequences were compared, analyzed and placed into a sequence alignment database. Each mutation was classified according to its intended purpose (e.g., to improve thermostability, product inhibition, remove glycosylation, specific activity, etc). Conserved regions were identified across species, and structural models were constructed for each mutation and species from homology to known crystal structures and computational models of Cel7A. This sequence landscape for Cel7A outlines previous enzyme engineering work and will aid in identifying potential targets for future protein engineering.
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