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Non-Covalent Immobilization of Quince (Cydonia Oblonga) Polyphenol Oxidase
2002
Journal:  
Turkish Journal of Chemistry
Author:  
Abstract:

A partially purified polyphenol oxidase from quince (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.

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Turkish Journal of Chemistry

Field :   Fen Bilimleri ve Matematik

Journal Type :   Uluslararası

Metrics
Article : 2.410
Cite : 1.692
2023 Impact : 0.068
Details
Turkish Journal of Chemistry