Non-Covalent Immobilization of Quince (Cydonia Oblonga) Polyphenol Oxidase

Authors : Hülya YAĞAR, Ayten SAĞIROĞLU

Pages : 751-758

View : 10 | Download : 5

Publication Date : 0000-00-00

Article Type : Research Paper

Abstract :A partially purified polyphenol oxidase from quince insert ignore into journalissuearticles values(Cydonia oblonga); was immobilized on bentonite by simple adsorption at pH 6.8. The properties of the immobilized enzyme were compared to those of the free enzyme. Optimum pH and temperature were determined to be 9.0 and 45°C, respectively, showing the alteration of pH and temperature profiles by immobilization. No drastic change was observed in the Km value after immobilization. Catechol, L-DOPA, p-cresole and pyrogallol were tested as substrates. Thermal and storage stability and reusability experiments were carried out. It was observed that the immobilized enzyme had storage stability for a period of one year but had no reusability in the batch process.
Keywords : Bentonite, polyphenol oxidase, purification, non covalent immobilization, characterization