In the first case, the enzymatic activity of GOx/HRP (as model enzyme for the development of biosensors ) was measured and analyzed as a function of time. For these experiments, 1% ALG, 5% ALG, and ALGPODES beads were prepared containing the combination of GOx/HRP-ODI as a model reporter and maintained at room temperature during the period of the experiment. These conditions were specifically selected to challenge the stability of the enzyme, considering that lower temperatures would extend the lifetime of the sensor 67 and that the selected redox dye (ODI) would remain within the beads (vide infra). Thus, at the selected times, three beads of each composition were placed into the Plexiglas ® cell (Figure ) containing 1 mL of a 0.1 mM glucose solution and their color development followed, capturing pictures every 5 seconds for 600 seconds. While only the average color intensity of the beads at 600 seconds was used for the herein described analysis, this procedure was adopted for all experiments to ensure consistency. As it can be observed in Figure , all the beads showed catalytic activity when exposed to glucose, confirming the accessibility of the enzymes through the pores in the external shell of the beads (Figure ). As it can also be observed in Figure , the highest response was obtained for the ALGPODES beads, followed by the bead synthetized from 5% ALG and then those made from 1% ALG. As all these beads contain the same amount of GOx/HRP-ODI, these initial results would support the idea that the ALGPODES provide a more favorable environment for the reaction. These experiments also displayed a gradual decrease in the colorimetric response of the beads, that stabilized approximately 4 hours after the preparation. While the ALGPODES beads showed a decrease of 40 ± 3 % in the response (after 10 hours at room temperature), the color development decreased by 65 ± 2 % and by 67 ± 3 %, when beads composed of 5% ALG or 1% ALG were used. We hypothesize that these changes, which are somewhat in agreement with previous reports, could be attributed to slight conformational changes in the enzymes, induced by the ALGPODES (or ALG) matrix, that surrounds the proteins and (upon stabilization) creates a microenvironment that maintains their conformation and protects their active sites. Considering that no color development was observed outside the beads, the release of the enzymes or the redox dye to the solution is unlikely to be significant contributor to the decrease within the investigated timescale. Based on these results, ALGPODES were considered a superior platform for the development of the proposed biosensor and thus, used for the remaining experiments.