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Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide

Ryan, Barry J. and Ó'Fágáin, Ciarán (2007) Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide. Biochimie, 89 (8). pp. 1029-1032. ISSN 0300-9084

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Abstract

Horseradish peroxidase (HRP) is a commonly used enzyme in many biotechnological fields. Improvement of HRP stability would further increase its potential application range. In the present study, 13 single- and three double-mutants of solvent exposed, proximal lysine and glutamic acid residues were analysed for enhanced H2O2 stability. Additionally, five single- and one pentuple-consensus mutants were investigated. Most mutants displayed little or no alteration in H2O2 stability; however, three (K232N, K241F and T110V) exhibited significantly increased H2O2 tolerances of 25- (T110V), 18- (K232N), and 12-fold (K241F). This improved stability may be due to an altered enzyme-H2O2 catalysis pathway or to removal of potentially oxidisable residues.

Item Type:Article (Published)
Refereed:Yes
Uncontrolled Keywords:Recombinant; Horseradish peroxidase; Mutagenesis; Peroxide; Stabilisation
Subjects:Biological Sciences > Biotechnology
Biological Sciences > Enzymology
DCU Faculties and Centres:DCU Faculties and Schools > Faculty of Science and Health > School of Biotechnology
Research Initiatives and Centres > National Centre for Sensor Research (NCSR)
Publisher:Elsevier
Official URL:http://dx.doi.org/10.1016/j.biochi.2007.03.013
Use License:This item is licensed under a Creative Commons Attribution-NonCommercial-Share Alike 3.0 License. View License
ID Code:97
Deposited On:09 Oct 2007 by DORAS Administrator. Last Modified 30 Jan 2009 14:34

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