The successful application of glucose oxidase on glucose sensors is mainly due to its intrinsic high stability on the specific analytical and storage experimental conditions. Other enzymes with great potential to conquer a large market on specific analytical kits (e.g. alcohol, lactate, choline and glutamate oxidases, and uricase, urease, peroxidase, tyrosinase, and many others) have been largely studied. However, these enzymes continue on a development phase yet, due especially to their low long-term stability.

Some authors have studied and suggested changes at the level of environmental factors and reaction conditions to minimise enzyme deactivation. With this objective, alcohol oxidase stability was studied by an in situ strategy of H₂O₂ reaction through peroxidase with 4-aminoantipyrine and phenolsulphonic acid. This strategy has the advantage of avoiding the enzyme contact with a high concentration of H₂O₂ and simultaneously, enables its spectrophotometric detection.

Alcohol oxidase immobilised on CPG beads was tested with this strategy as an analytical reactor in a FIA system and continuous column reactors of about 20 ml. This strategy led to an excellent stability of the enzyme as it was obtained very high enzyme turn-over. In the FIA systems it was observed almost total conversion of substrate injected producing about 9 mg/L of H₂O2. The stability obtained in continuous reactors was equivalent to 50,00 injections of 25 ml in the FIA system with an enzyme deactivation lower 10%. This strategy was tested on other immobilised oxi-reductase enzymes with great success (e.g. horseradish peroxidase, Pichia pastoris alcohol oxidase, lactate and glucose oxidases, and catalase).