Many enzyme processes, and indeed most industrial enzyme reactions, occur at an interface rather than in the aqueous bulk. Some examples include immobilized enzymes and enzymes attacking insoluble substrate such as lipids, polysaccharides or precipitated proteins. In spite of the prevalence of interfacial processes, however, rigorous kinetic descriptions of enzymes usually rely on bulk-reaction theory.
In the Interfacial Enzymology Group, we strive to develop more realistic approaches that adequately takes the heterogeneous environment of the interface into account.
Currently, the group has particular focus on rational design of enzymes for industrial breakdown of plant biomass. This process plays a vital role in upcoming bio-refineries that produce sustainable fuels and alternatives to petrochemicals using residue from farming and forestry as feedstock.
The group’s work pivots around a comprehensive kinetic characterization of enzymes that deconstruct the biomass. We use the kinetic information to elucidate molecular mechanisms of the enzymatic process and ultimately to identify the rate-limiting step of the process under industrial conditions. Based on this, we design and produce mutant enzymes that are more efficient in the technical process.
Our work relies on expertise within a range of experimental and theoretical disciplines including chemical kinetics, mathematical modeling, computer simulation as well as bioinformatics and the expression and purification of recombinant enzymes. We are also strongly devoted to the development of experimental assays for the activity of interfacial enzymes.