Enzymes are the protein catalysts that allow complex chemical reactions to occur under physiological conditions. There’s an enzyme or two specifically designed to make or break just about any bond or to add or remove any group. For decades, the complexity of the chemistry of enzymes prevented their use outside the research lab. Enzymes were unstable molecules of unknown structure and composition, impossible to fully characterize. And it wasn’t possible to extract and purify these proteins to the stringent levels required for analytical reagents. Biotechnology has changed this. Molecular biology enables the identification and manipulation of amino acid sequences. Protein expression techniques enable reproducible production of commercial quantities of active catalysts. So we can start using enzymes to replace standard chemical processes that require harsh conditions and high energy.

A great place to start is analytical chemistry. Many of the standard methods identified by the EPA and other organizations involve solvents, heavy metals, or concentrated acids. Enzymatic reactions are inherently greener, and generally more selective as well. Such methods are commonly used in clinical and biomedical research labs. This talk will focus on moving enzyme-based nitrate analysis from biomedical research into industrial, commercial, and environmental labs.
Nitrate reductase and its biological electron donor NADH replace cadmium for nitrate determination in samples from blood to soil to drinking water, in applications from on-site field test kits to microplates to discrete analyzers. Sensitivity, selectivity, and precision are retained.