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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 13 Feb 2017 11:47

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