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Turkish Journal of Chemistry

Authors

ERSEN GÖKTÜRK

DOI

10.3906/kim-2005-32

Abstract

In this study, the catalytic activity and stability of flowerlike hybrid horseradish peroxidase (HRP) nanobiocatalyst (HRP-Cu$^{2+}$) obtained from Cu$^{2+}$ ions and HRP enzyme in the polymerization reaction of guaiacol were analyzed. We demonstrated that HRP-Cu$^{2+}$ and hydrogen peroxide (H$_{2}$O$_{2}$) initiator showed significantly increased catalytic activity and stability on the polymerization of guaiacol compared to that of free HRP enzyme. Poly(guaiacol) was observed with quite high yields (88%) and molecular weights (38,000 g/mol) under pH 7.4 phosphate-buffered saline (PBS) conditions at 60 °C with 5 weight% of HRP-Cu$^{2+}$ loading. HRP-Cu$^{2+}$ also shows very high thermal stability and works even at 70 °C reaction temperature; free HRP enzyme denatures at that temperature. Furthermore, HRP-Cu$^{2+}$ provided considerable repeated use and showed some degree of catalytic activity, even after the fourth recycle, in the polymerization of guaiacol.

Keywords

Horseradish peroxidase, hybrid nanoflowers, polymerization, guaiacol

First Page

1285

Last Page

1292

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