The main fact to deal with is that bioseparations have unique features that go beyond general separation process descriptors commonly taught in chemical engineering course work, yet each separation need not be considered a completely unique problem. The connection between the general and specific is a better understanding of the molecular-level interactions of proteins with each other and with separation media. This vital understanding links biochemistry, as it is practiced for macromolecule purification, with engineering and an understanding of the form and structure of these separation processes. To determine how molecular-level effects influence protein purification, we use many of the same tools of analysis employed by biochemists and chemical engineers. The second area pursued in my laboratory involves protein technology.
Proteins are the main molecules for energy transduction and signal sensing in living systems.
The useful properties of these molecules are their sensitivity, selectivity, and catalytic efficiency. At its root, protein technology involves developing ways to use proteins in the process environment for our own purposes and runs the gamut from immobilized enzymes to biosensor technology. A key here is to learn how to use new and old protein manipulation techniques to make these molecules more useful in processes of interest to industry. This includes developing an understanding of the immobilization process, in vitro protein modification, and directed genetic engineering of proteins to improve their stability and general usefulness in industrial processes. My third area of interest is the growth and stability of recombinant DNA-containing cells.