795.13 - Kinetic and stability study on the immobilized enzymatic step of one-pot dimerization of 2-[2-(dimethylamino)ethoxy]ethanol

Kurt Espinosa (James Madison University), Jonathan Schmitz (James Madison University), J.J. Fitzhenry (James Madison University), Madison Beck (James Madison University), Linette Watkins (James Madison University)

Tertiary amine catalysts (TACs) are essential organic molecules used in polyurethane manufacturing. Synthesis of these chemicals involves the use of catalytic transition metals at high temperatures and high pressures. Simple amine systems react easily with transition metals; however, amine systems with multiple hydroxyl groups and methylamine complexes produce significant byproducts. In this study, synthesis that forgo transition metals is explored. Enzymes can provide a clean industrial alternative to transition metal use. 2-[2-(dimethylamino)ethoxy]ethanol (DMAEE) is the monomer used in the synthesis of a model TAC. When DMAEE is first enzymatically oxidized, the aldehyde can serve as an electrophile for 2-(methylamino)ethanol (MMEA), forming the DMAEE dimer. Choline oxidase catalysis is the first step of this pathway. Steady state kinetic parameters of choline oxidase with choline and DMAEE as substrates, optimum pH, and temperature stability are reported in this study. The effect of MMEA on the enzymatic reaction is examined as well. In an industrial application, immobilized enzymes can enhance stability over a broad range of temperature and pH. Therefore, choline oxidase was immobilized on CNBr-activated Sepharose beads, and the effects of immobilization are reported in this study.

This material is based upon work supported by
The National Science Foundation under Grant No. CHE-1757874, Huntsman Corporation (Dr. Matt Forkner), and JMU College of Science and Mathematics.