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Enzymatic polymerization of  m -substituted phenols has been achieved in the presence of 2,6-di- O -methyl-β-cyclodextrin (DM-β-CD) in a buffer. A watersoluble complex of the monomer and DM-β-CD was formed and polymerization was performed by peroxidase catalyst to give the polymer in high yields. Formation of the inclusion complex was confirmed by NOESY NMR. The association constant was determined by NMR and found to depend on the monomer structure.

Enzymatic polymerization of m-substituted phenols in the presence of 2,6-di-O-methyl-β-cyclodextrin in water