Demir, H.Gur, A.Yilidz, A.Gur, T.2025-05-102025-05-1020080973-12452-s2.0-51249113919https://hdl.handle.net/20.500.14720/18155It is known that immobilized enzymes more useful and advantageous than free enzymes. In this work, polyphenol oxidase purifed by affinity chromatography from lgdir apricot was immobilized onto natural bardakci-clay by physical adsorption method. The properties of the immobilized enzyme were compared to the tree enzyme. The PPO activity of immobilized clay was determined, and then the effects of reaction optimum temperature, thermostability, optimum pH, ionic effect and kinetic parameters were investigated. Catechol was used as substrate, the activities of immobilized and free polyphenol oxidase were determined in the reaction mixture containing substrate catechol. The results obtained from experiments indicated that physical adsorption is favourable for attachment of enzyme onto bardakci-clay.eninfo:eu-repo/semantics/closedAccessClayImmobilizationPolyphenol OxidasePurificationArticle51N/AN/A9398