McMahon, Colm P. and Rocchitta, Gaia Giovanna Maria and Serra, Pier Andrea and Kirwan, Sarah M. and Lowry, John P. and O'Neill, Robert D. (2006) The Efficiency of immobilised glutamate oxidase decreases with surface enzyme loading: an electrostatic effect, and reversal by a polycation significantly enhances biosensor sensitivity. Analyst, Vol. 131 (1), p. 68-72. eISSN 1364-5528. Article.
Full text not available from this repository.
The apparent Michaelis constant, KM, for glutamate oxidase (GluOx) immobilised on Pt electrodes increased systematically with enzyme loading. The effect was due, at least in part, to electrostatic repulsion between neighbouring oxidase molecules and the anionic substrate, glutamate (Glu). This understanding has allowed us to increase the Glu sensitivity of GluOx-based amperometric biosensors in the linear response region (100 ± 11 nA cm−2 µM−1 at pH 7.4; SD, n = 23) by incorporating a polycation (polyethyleneimine, PEI) to counterbalance the polyanionic protein. Differences in the behaviour of glucose biosensors of a similar configuration highlight a limitation of using glucose oxidase as a model enzyme in biosensor design.
I documenti depositati in UnissResearch sono protetti dalle leggi che regolano il diritto d'autore
Repository Staff Only: item control page