STUDY ON IMMOBILIZED SUPRAMOLECULAR INCLUSION COMPLEX OF IRON-PORPHYRIN AS AN ANALOG FOR PEROXIDE PROTEINASE

The Supramolecular inclusion complex of iron-5, 10, 15, 20-tetrakis[4- sulfophenyl]-21H, 23H-porphin (FeTPPS4) with beta-cyclodextrin cross-l inking polymer (beta-CDP) was obtained and used as an analogue for per oxide proteinase. The effects of varied factors on formation constant of the inclusion complex were investigated. The mechanism of immobiliz ed supramolecular complex catalysing p-chlorophnic acid by hydrogen pe roxide was studied in detail. The immobilized inclusion complex as mim esis of horseradish peroxidase was very stable and found to exhibit th e high proteinase-like activity, which have been demonstrated by enzym atic methods of analysis. The method was applied to determine hydrogen peroxide with 4-aminoantipyrine and p-chlorophenic acid. The calibrat ion curve for absorbance-concentration (H2O2) was linear from 0 to 3.0 mu g/mL and the linear correlation coefficient was 0.999 4.