Natural systems possess many powerful mechanisms for deconstructing lignocellulosic biomass. In the Microbial and Enzyme Discovery Group, we use a variety of techniques and systems to harness this power to improve the conversion of plant biomass to biofuels and biochemicals. We focus on the deconstruction and transformation of lignin, the most complex and recalcitrant portion of the plant cell wall. We leverage expertise in cultivating and analyzing microbiomes, isolating key microorganisms and characterizing enzymes to discover new mechanisms for lignin deconstruction. Our work involves close collaborations with the Feedstocks Division to provide plants with lignin modifications and with the Biofuels and Bioproducts Division to convert depolymerized lignin streams with engineered microbes.
Projects
- Cultivating microbiomes to understand lignin modification and depolymerization during biomass deconstruction
- Using microbiomes and novel microbial isolates to understand aromatic uptake and conversion
- Rewiring bacterial metabolism to improve the efficiency of lignocellulose conversion to fuels and chemicals
- Deciphering fungal mechanisms of lignin conversion and glycoside hydrolase expression
- Characterizing oxidative enzymes involved in lignin depolymerization
- Interrogating anaerobic fungi for novel mechanisms for anaerobic lignin deconstruction
Featured Media
To Find New Biofuel Enzymes, It Can Take a Microbial Village
Trash into treasure: Sandia could help biofuel pay for itself with goods made from waste
Featured Publications
- “Guanidine riboswitch-regulated efflux transporters protect bacteria against ionic liquid toxicity,” Journal of Bacteriology (2019)
- “Natural variation in the multidrug efflux pump SGE1 underlies ionic liquid tolerance in yeast,” Genetics (2018)
- “Jungle Express is a versatile repressor system for tight transcriptional control,” Nature Communications (2018)
- “A bacterial pioneer produces cellulase complexes that persist through community succession”, Nature Microbiology (2017)
- “Structure of aryl O-demethylase offers molecular insight into a catalytic tyrosine-dependent mechanism”, PNAS (2017)