Enzymes and Catalysis on Interfaces
Enzymes are the protein catalysts that nature uses in all metabolic processes for energy generation, storage and even defense purposes. Whenever we produce enzymes or apply them technologically, they interact with surfaces or interfaces. E.g. in downstream processing, enzymes adsorb to chromatographic resins, in a catalytic reactor they either interact with the vessel, membrane or liquid surface and finally, immobilised catalytic enzymes are hopefully beneficially bound non-/covalently to a carrier material. In order to identify suitable materials, we need to understand quantitatively, how the surface interaction changes the enzyme activity, selectivity, and stability. This tutorial lecture will cover the basics of enzyme kinetic analysis to yield information on activity, selectivity and stability. Concepts of coupled transport and reaction serve as a quantitative basis for the interfacial effects on enzymes. A range of examples covering kinetic analysis, enzyme immobilisation, degradation of biomass particles, and liquid/gas/solid interface effects will accompany the theoretical fundament.
Prof. Dr. A. Spieß
Antje C. Spiess has studied chemical engineering at Technical University Hamburg-Harburg and Pisa University, she did her PhD at TU Hamburg-Harburg and gained industry experience at Procter & Gamble before pursuing her habilitation research in Biochemical Engineering at RWTH Aachen University in the field of enzymes in non-conventional media and for biomass conversion. In 2010 Antje Spiess became professor for Enzyme Process Technology at Aachener Verfahrenstechnik, RWTH. One year later, she joined DWI’s scientific board which became Leibniz-Institute in 2014. Her research focusses on biocatalytic and chemical engineering and modeling of reaction kinetics.