Engineered Enzyme Mimics for Detergents

Nature controls chemical reactions by very specific catalysis called enzymes. Enzymes consist of globular peptides creating a catalytic active site, which is where the reaction takes place. In today's laundry detergents, enzymes such as proteases are some of the active ingredients. Proteases and esterases have an active site consisting of a catalytic triad. The catalytic triad is three amino acid residues that interact to perform the catalytic function of the enzyme. The goal of this research is to mimic the chemistry of the catalytic triad. A benefit to creating a synthetic mimic is stability can be increased. Enzymes can easily be denatured, and have specific conditions to which they function optimally. However a synthetic mimic could be designed to operate under varied conditions, and thus enhance performance of the catalytic triad. This project will design a series of molecules that contain the three functional groups of the catalytic triad, a hydroxyl, an imidazole and a carboyxylate group, thus designed to mimic the enzyme. These compounds will then be analyzed by various spectroscopies including Nuclear Magnetic Resonance, UV/Vis, and mass. Finally the molecules will be screened for enzymatic activity using kinetic analysis with calorimetric assays in order to understand and optimize the synthetic mimic.

Project Mentor: Luke Connal

Faculty Advisor: Craig Hawker