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Updated: Jun 9, 2026
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Published on: August 20, 2014
Immobilization of chloroperoxidase onto highly hydrophilic polyethylene chains via bio-conjugation: catalytic
Gulay Bayramoglu1, Begum Altintas, Meltem Yilmaz
1Biochemical Processing and Biomaterial Research Laboratory, Faculty of Arts and Sciences, Department of Environmental Sciences, Gazi University, 06500 Teknikokullar, Ankara, Turkey. g_bayramoglu@hotmail.com
Abstract:
Chloroperoxidase (CPO) was covalently immobilized on poly(hydroxypropyl methacrylate-co-polyethyleneglycole-methacrylate) membranes, which were characterized, by swelling test, FT-IR spectroscopy, scanning electron microscopy, and contact angle measurement. The Km and Vmax values for free and immobilized CPO were found to be 34.6 and 47.2 μM, and 287.5 and 245.2 U/mg protein, respectively. The optimum pH for both the free and immobilized enzyme was observed at 3.0. The immobilized enzyme showed wide pH and temperature profiles. Most importantly, the increased thermal, storage and operational stability of immobilized CPO should depend on the creation of a comfortable strong hydrophilic microenvironment on the designed support to the host enzyme molecule.
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