Abstract: The Supramolecular inclusion complex of iron-5, 10, 15, 20-tetrakis[4-sulfophenyl]-21H, 23H-porphin (FeTPPS₄) with p-cyclodextrin cross-linking polymer(β-CDP) was obtained and used as an analogue for peroxide proteinase. The effects of variedfactors on formation constant of the inclusion complex were investigated. The mechanism ofimmobilized supramolecular complex catalyzing p-chlorophnic acid by hydrogen peroxide wasstudied in detail. The immobilized inclusion complex as mimests of horseradish peroxidasewas very stable and found to exhibit the high proteinase-like activity, which have beendemonstrated by enzymatic methods of analysis. The method was applied to determinehydrogen peroxide with 4-aminoantipyrine and p-chlorophenic acid. The calibration curve forabsorbance-concentration(H₂O₂) was linear from O to 3. 0 μg/mLand the linear correlationcoefficient was 0. 9994.

Key words: β-Cyclodextrin cross-linking polymer, Metalloporphyrin, Immobilized supramolecule, Peroxide proteinase, H₂O₂ enzymatic analysis