Document Type
Article
Rights
Available under a Creative Commons Attribution Non-Commercial Share Alike 4.0 International Licence
Disciplines
1.4 CHEMICAL SCIENCES, 1.6 BIOLOGICAL SCIENCES
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, thirteen 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) exhibit 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.
DOI
https://doi.org/10.1016/j.biochi.2007.03.013
Recommended Citation
Ryan, B.J. and O'Fágáin, C. (2007). Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide. Biochimie, 89, (8), 1029-1032. http://dx.doi.org/10.1016/j.biochi.2007.03.013
Publication Details
Ryan, B.J. and O'Fágáin, C. (2007). Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide. Biochimie, 89, (8), 1029-1032.