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Catalase is a metalloenzyme commonly found in almost all plant and animal tissues and catalyzes the conversion of hydrogen peroxide to less reactive molecules. It is used for the elimination of hydrogen peroxide in biological, biomedical, food and textile applications. For this purpose, a novel affinity sorbent [poly(methacrylic acid- N-isopropyl acrylamide-CB-Fe3+, (p(MAA-NIPAAM)-CB-Fe3+)] for the determination and it was first developed using MAA and NIPAAM monomers. After characterization with Fourier transform infrared spectroscopy (FTIR), scanning electron microscopy (SEM), thermogravimetric analysis (TGA), X-ray Photoelectron Spectroscopy (XPS), adsorption parameters were determined. Reusability of p(MAA-NIPAAM)-CB-Fe3+ sorbent was determined after by determining the appropriate desorption agent for desorption of adsorbed catalase in the developed sorbent. It was determined that catalase adsorption could be performed with 0.01 g of sorbent in 45 min. The maximum adsorption capacity for catalase adsorption was determined as 243.17 mg/g with the use of sorbent. The operational and storage stability of the immobilized catalase was found to be high as expected. The conversion of H2O2 can be successfully performed by the immobilized enzyme in the prepared sorbent. It has been proven that the affinity of catalase for its substrate is increased by immobilization.