Synthesis and characterization of an acid phosphatase-polyresorcinol complex

A stable acid phosphatase-polyresorcinol complex, retaining about 90% of the original enzymatic activity, was synthesized in the presence of peroxidase. The complex was disturbed by chaotropic agents, as 4 M urea, indicating that the enzyme linked the phenolic moiety by non-covalent bonds. The immobilized phosphatase was more stable than the free enzyme towards pH, temperature and proteolysis: however, when added to soil, free and immobilized phosphatase showed comparable stability. It appears that the polymerization conditions used, favouring the interaction between enzyme and polyphenol through secondary linkages, give rise to a fully active complex resembling those which naturally generate in soil.