Interfacial Enzymology
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 take the heterogeneous environment of the interface into account. We apply new basic knowledge on interfacial enzyme processes to discover and engineer novel enzymes with better performance under industrial conditions.
Currently, the group’s work addresses two main topics: enzyme assisted capture of CO2 and enzymatic degradation of plastic waste. The former involves enzyme catalysis at the air-liquid interface while the latter focuses on the interface between an aqueous phase and the solid plastic. In addition, we also have some activity within enzymatic deconstruction of lignocellulosic biomass
Enzyme assisted carbon capture: We are engaged in two major international centers within this area, both of which are supported by the Novo Nordisk Foundation. The CO2 research center CORC (https://corc.au.dk/) and the BIG-collaboration (https://biocat.ncsu.edu/). This work explores a range of enzymes and their potential to capture and convert CO2 from the atmosphere or flue gases.
Degradation of plastic waste: We study and engineer enzymes that can release the building blocks (monomers) from plastic waste and hence pave the way for a closed-loop plastic economy. One project, EnDeWa, supported by Innovation Fund Denmark works on enzymes that degrade polyester waste while another, EnZync, supported by the Novo Nordisk Foundation zooms in on thermoset plastics such as polyurethane (https://inano.au.dk/about/research-centers-and-projects/enzync/ ).
The group’s work uses comprehensive kinetic characterization of interfacial enzyme processes 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.