- Polymer degrading enzymes (Glycoside hydrolases, Lytic polysaccharide monooxygenases, Cellobiose dehydrogenases, Nylon Hydrolases)
- Electron and proton transfers
- Enzymatic mechanisms
- Protein-protein interactions
- Protein flexibility
- Biopolymer matrices and enzyme immobilization
- X-ray/neutron crystallography
- Small-angle X-ray/neutron scattering
- Quantum chemistry
Research SummaryCellulose deconstruction
: We are interested in the enzymatic cellulose degradation, a key challenge remaining to be overcome for efficient cellulosic biofuel production. Understanding how wood degrading organism enzymes function is required to guide enzyme engineering and design of more efficient enzymes. Two types of extracellular enzymatic systems have been identified in microorganisms capable of cellulose degradation: a hydrolytic system and an oxidative system. Effort in our lab is focused on gaining insight into the structures, dynamics and functions of enzymes from both systems.
Nylon depolymerization: We are interested to characterize and understand common structural features that determine activity and substrate/product selectivity of nylon hydrolases, a family of enzymes that depolymerizes nylon. While the high crystallinity of nylon makes it a strong engineering plastic, it also makes it recalcitrant to enzymatic depolymerization. We use X-ray and neutron scattering to gain structural and dynamics understanding of the nylon hydrolysis reaction. This knowledge will be used to guide the rational engineering of enzymes with improved efficiency. (This project is a collaboration with the Dr Josh Michener at ORNL.)
Enzyme immobilization: We are using X-ray and neutron scattering to study the structure and dynamics of biopolymer matrices and immobilized enzymes. This project is part of the BIG collaboration funded by the Novo Nordisk Foundation and led by Dr Sonja Salmon at NC State.
We use primarily a combination of X-ray and neutron diffraction and scattering to probe enzyme structure, dynamics and function.