Journal
MACROMOLECULAR BIOSCIENCE
Volume 4, Issue 5, Pages 497-502Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/mabi.200300078
Keywords
enzymes; peroxidase; polyphenol; regioselectivity; templates
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Peroxidase-catalyzed oxidative polymerization of phenol has been examined using the template, poly-(ethylene glycol) monododecyl ether (PEGMDE), in water. The role of this template, which forms a complex with phenol in the polymerization, was verified by UV measurements. During the reaction, a complex of the resulting polymer and PEGMDE was precipitated in high yields. The amount and the PEG chain length of PEGMDE strongly affected the polyphenol yield. The unit molar ratio of polyphenol and PEG of the template was about 1:09. The presence of the PEGMDE template in the aqueous medium greatly improved the regio-selectivity of the polymerization, yielding polyphenol with a phenylene unit content close to 90%. FT-IR, DSC, and XRD analyses confirmed the formation of the miscible complex of polyphenol and PEGMDE by hydrogen-bonding interactions.
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