Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide.
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 H(2)O(2) stability. Additionally, five single- and one pentuple-consensus mutants were investigated. Most mutants displayed little or no alteration in H(2)O(2) stability; however, three (K232N, K241F and T110V) exhibited significantly increased H(2)O(2) tolerances of 25- (T110V), 18- (K232N), and 12-fold (K241F). This improved stability may be due to an altered enzyme-H(2)O(2) catalysis pathway or to removal of potentially oxidisable residues.
Ryan
Barry J
BJ
School of Biotechnology and National Centre for Sensors Research, Dublin City University, Dublin 9, Ireland.
O'Fágáin
Ciarán
C
D019943:Amino Acid Substitution; D002384:Catalysis; D004795:Enzyme Stability / Q000235:genetics; D006735:Horseradish Peroxidase / Q000235:genetics* / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism*; D009154:Mutation
D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase