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 ur ea, indicating that the enzyme linked the phenolic moiety by non-coval ent bonds. The immobilized phosphatase was more stable than the free e nzyme 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 intera ction between enzyme and polyphenol through secondary linkages, give r ise to a fully active complex resembling those which naturally generat e in soil. Copyright (C) 1996 Elsevier Science Ltd