Solvent effects in horseradish peroxidase-catalyzed polyphenol synthesis

Enzyme-solvent-monomer molecular interactions and their effect on horseradish peroxidase-catalyzed polymerization of m-cresol in ethanol/water mixtures were studied. A mechanistic approach of the effect of reaction medium composition on the poly (m-cresol) molecular weight and polydispersity was elucidated from the standpoint molecular interactions. Solvent effects on the enzyme activity and structure were studied by reaction kinetics and spectroscopic methods including UV-vis, fluorescence, circular dichroism and electron paramagnetic spectroscopy (EPR). In view of the results from these studies, the observed polymer molecular weight profile could be deduced from the solubility of the polymer as well as the partitioning of the monomer between solvent and the enzyme active site.