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Michael Resch

Photo of Michael Resch

Michael Resch holds a Ph.D. in Biochemistry and Molecular Biology from Colorado State University. His dissertation work focused on the biophysical and structural properties of nucleosomes and chromatin arrays in vitro in the laboratories of Dr. Karolin Luger and Dr. Jeffery Hansen at Colorado State University.

Dr. Resch's NREL career began in 2008 as a postdoctoral researcher working on cellulase and hemicellulase enzyme characterization working on projects funded by the Department of Energy through the BioEnergy Science Center (BESC) and the Bioenergy Technologies Office (BETO). In early 2011, he was hired as a research scientist and has focused on comparing the saccharification mechanisms between free fungal and complexed bacterial enzyme systems. He uses protein crystallography, small-angle X-ray scattering, analytical ultracentrifugation, FPLC, HPLC, TEM, SEM, and poly-acrylamide gel electrophoresis to characterize the biophysical nature of these systems. The ultimate goal of these studies is to improve the hydrolysis efficiency of cellulase and hemicellulase enzyme digestion of biomass. This work will help NREL lower the industrial cost of lignocellulosic enzyme conversion of biomass to sugars for biofuel production.

Another source of terrestrial carbon in biomass is in the form of lignin. Lignin has historically been used for heat and power in an industrial setting. Dr. Resch is also involved in investigating biological lignin depolymerization with the ultimate goal of converting lignin into value added fuels or chemicals.

In 2014 Dr. Resch became the Section Supervisor of the Bioprocess Research Group in NREL's National Bioenergy Center. The researchers in this diverse group are involved with microbial development of photobiological and fermentation applications.

Research Interests

Illustration of plant cell walls before and after pretreatment and models of hydrolysis by free (red) and complexed (blue) enzyme systems

Illustration of plant cell walls before and after pretreatment and models of hydrolysis by free (red) and complexed (blue) enzyme systems. Free enzymes with single CBMs and catalytic units hydrolyze cell wall polysaccharides by utilizing endoglucanases and CBHs to react with accessible cellulose surfaces. Complexed enzymes with multiple catalytic and binding specificities likely have lower off-rates, and once bound at multiple points of contact, disrupt the biomass surface resulting in an increase in surface area. Combining these two enzyme paradigms on pretreated biomass synergistically deconstructs the cell walls by increasing the reactive surface area allowing free enzymes to better diffuse and processively hydrolyze the substrate. Also, by removing the majority of the lignin and hemicellulose from the cellulose fraction, CF enhances the cellulose activity enabling the benefits of combining these two deconstruction mechanisms [Resch, M. G., et al., (2014), ACS Sustainable Chemistry and Engineering].

Accepted Peer-Reviewed Publications