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.",

keywords = "Horseradish peroxidase, Mutagenesis, Peroxide, Recombinant, Stabilisation",

author = "Ryan, \{Barry J.\} and Ciar{\'a}n {\'O}'F{\'a}g{\'a}in",

year = "2007",

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doi = "10.1016/j.biochi.2007.03.013",

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TY - JOUR

T1 - Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide

AU - Ryan, Barry J.

AU - Ó'Fágáin, Ciarán

PY - 2007/8

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N2 - 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.

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.

KW - Horseradish peroxidase

KW - Mutagenesis

KW - Peroxide

KW - Recombinant

KW - Stabilisation

UR - https://www.scopus.com/pages/publications/34447094807

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DO - 10.1016/j.biochi.2007.03.013

M3 - Article

C2 - 17482746

AN - SCOPUS:34447094807

SN - 0300-9084

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SP - 1029

EP - 1032

JO - Biochimie

JF - Biochimie

IS - 8

ER -

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

Abstract

Keywords

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