Enzyme discovery for environmental and industrial biotechnology
Enzymes play a pivotal role in many biotechnological applications, including use as biocatalysts to make high value chemicals, in the saccharification of biomass for biofuel production and for environmental remediation of polluted sites. Recent developments in ‘omics technologies, bioinformatics and gene synthesis are providing powerful approaches to finding new and novel industrial enzymes from natural systems.
Research in Neil’s lab largely focuses on enzymes mediating plant and microbial metabolism of xenobiotic compounds. In particular, we have been studying the chemistry, biochemistry and molecular genetics of explosives metabolism. Explosive compounds 2,4,6-trinitrotoluene (TNT) and hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) used in munitions are highly toxic and the potential for progressive accumulation of such compounds in soil, plants and groundwater is a significant concern at military sites. We are characterising the enzymes involved in the detoxification and metabolism of explosives in plants and microbes and are using this knowledge to successfully engineer transgenic plants able to remediate toxic explosive pollutants. An innovative aspect of our work has been the use of synthetic biology to combine the biodegradative capabilities of explosives-degrading bacteria with the high biomass, stability and detoxification systems inherent in plants.
Transgenic switch grass remediating soil contaminated with the explosive RDX
Neil’s lab is also discovering new enzymes and associated proteins for biomass degradation. We have been using a multi ‘omics approach, combining the power of extracellular proteomics and transcriptomics, to identify proteins critical for lignocellulose deconstruction from microbial communities and animals obtained from marine and terrestrial environments. This approach is allowing the identification of new types of lignocellulose active proteins, both broadening our fundamental understanding of this process, as well as providing novel activities for research and industrial applications.
Structure of a lytic polysaccharide monoxygenase from Thermobia domestica