<p>Phenolic compounds pose a major threat to water pollution due to their high toxicity. Enzymes have emerged over recent years to act as a green alternative for cleaning up and utilizing phenolic compounds in nature. DyP peroxidases, a member of the oxidoreductase family, have shown promising ability to convert dyes into harmless compounds and have been found indispensable tools for green polymerization. In this study, three recombinant DyP peroxidases were used to convert pyrogallol (PG) into a polymer which upon characterization using Fourier-transform infrared spectroscopy (FT-IR), Raman spectroscopy, powder X-ray diffraction (XRD) and scanning electron microscopy (SEM) have revealed intricate details characteristic of poly(pyrogallol) (PPG). The synthesized polymer showed a rigid structure, with potential use in material science applications such as coatings or binding agents, as well as broader aspects in environmental and biomedical research.</p>