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1.4 CHEMICAL SCIENCES, 1.6 BIOLOGICAL SCIENCES
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.
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