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

Barry J. Ryan; Ciarán Ó'Fágáin

doi:10.1016/j.biochi.2007.03.013

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

Barry J. Ryan, Ciarán Ó'Fágáin

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	1029-1032
Number of pages	4
Journal	Biochimie
Volume	89
Issue number	8
DOIs	https://doi.org/10.1016/j.biochi.2007.03.013
Publication status	Published - Aug 2007
Externally published	Yes

Keywords

Horseradish peroxidase
Mutagenesis
Peroxide
Recombinant
Stabilisation

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10.1016/j.biochi.2007.03.013

https://arrow.tudublin.ie/schfsehart/171Licence: CC BY-NC-SA

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title = "Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide",

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.",

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AU - Ryan, Barry J.

AU - Ó'Fágáin, Ciarán

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AB - 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.

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KW - Mutagenesis

KW - Peroxide

KW - Recombinant

KW - Stabilisation

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

Abstract

Keywords

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