In the pursuit of more efficient methods for producing polymeric materials, researchers are increasingly investigating <i>in vitro</i> enzymatic catalysis. Proteins as renewable biomolecules are often used for their potential in “green chemistry” reactions; however, they also afford a means for controlling polymerization. Enzymes, catalysts that are driven by concentration-dependent kinetics, can conduct polymerization reactions with the resulting products having extremely low polydispersities. In the present study, we report a new polymerization of 2-ethynylpyridine (2-EP) in water using only hen egg white lysozyme (HEWL) as the singular protein catalyst. We propose that HEWL is able to direct the dimerization and subsequent polymerization of 2-EP monomers in a mechanism analogous to the traditional acid-catalyzed method for synthesis of poly-2-EP. Although the details remain to be elucidated, HEWL acts as a proton donor in the polymerization event which appears to occur partially dependent on the active site. Protein-catalyzed poly-2-EP was purified using simple organic extraction techniques and the polymer was characterized by several spectrometric methods. This discovery marks the first time lysozyme has been observed catalyzing a synthetic polymerization and warrants additional research into further applications.

Lysozyme-Catalyzed polymerization of an ionically conductive polyacetylene

254th National Meeting (2017)

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