Monday, April 19, 2010
3-41

Structure, function, and synergy of mono-and bi-functional arabinofuranosidases from Saccharophagus degradans in biomass conversion

Michael G. Resch1, Michael E. Himmel1, Steven R. Decker1, and Larry E. Taylor III2. (1) Chemical and Biosciences Center, National Renewable Energy Laboratory, 1617 Cole Blvd., Golden, CO 80401, (2) Biosciences Center, National Renewable Energy Laboratory, 1617 Cole Blvd, MS 3233, Golden, CO 80401

Obtaining fermentable sugars from biomass requires balancing pretreatment severity and enzyme digestion costs to attain yield and economic constraints.  In an effort to obtain maximal fermentable monosaccharides and minimal degradation and inhibitor formation, we have screened cellulase, hemicellulase, and accessory enzyme cocktails for optimal deconstruction of the plant cell wall carbohydrates.  The marine bacterium Saccharophagus degradans contains a large number of glycoside hydrolases and is capable of digesting many complex polysaccharides.  We have cloned, expressed and purified mono and bi-functional arabinofuranosidases from the genomic DNA of Saccharophagus degradans.  We have characterized the biophysical and structural properties of these proteins using analytical ultracentrifugation and x-ray crystallography.  The purified mono-and bi-functional arabinofuranosidases were evaluated for synergy with a variety of hemicellulases and cellulases by digestion of pretreated and non-pretreated cornstover.   Together these results show the advantage of using specific hemicellulases to improve the release of soluble sugars from cellulosic feedstocks. 

See more of Poster Session One Sponsored by Genencor
See more of General Submissions

See more of The 32nd Symposium on Biotechnology for Fuels and Chemicals (April 19-22, 2010)