EC Number   |
Application |
Reference |
|---|
   1.1.3.4 | agriculture |
the enzyme can be used as pest control agent against Ephestia kuehniella. The enzyme shows approximately similar damage on the Ephestia kuehniella midgut including rupture and disintegration of the epithelial layer and cellular vacuolization |
-, 762785 |
| 1.1.3.4 | agriculture |
the enzyme shows antifungal activity. It could become a natural alternative to synthetic fungicides to control certain important plant microbial diseases. The enzyme displays a wide inhibitory spectrum toward different fungi at a concentration of 20 AU. It has a strong inhibitor effect on mycelia growth and spore germination of Pythium ultimum |
-, 762806 |
| 1.1.3.4 | analysis |
application in glucose biosensors. An unmediated, reagentless glucose biosensor is prepared with two polyethylenimine/glucose oxidase bilayers-modified pyrolytic graphite electrodes. A calibration linear range of glucose is 0.5-8.9 mM with a detection limit of 0.05 mM and sensitivity of 0.76 microA per mM |
654185 |
| 1.1.3.4 | analysis |
biosensor system prepared for continuous flow analysis of enzyme activity |
389787 |
| 1.1.3.4 | analysis |
co-confined glucose oxidase and horseradish peroxidase bienzyme system as a biosensor for the detection of glucose gives a wider linear range of glucose than for free enzymes in solution |
723947 |
| 1.1.3.4 | analysis |
coupling of the enzyme with Fenton's reagent used for the determination of glucose produced as a result of the hydrolysis of cellobiose catalyzed by beta-glucosidase |
389795 |
| 1.1.3.4 | analysis |
enzyme immobilized in Bombyx mori silk fibroin membrane applied to glucose sensor |
389786 |
| 1.1.3.4 | analysis |
GOx is the main component in glucose biosensors for determination of glucose in industrial solutions and in body fluids such as blood and urine |
-, 743775 |
| 1.1.3.4 | analysis |
immobilized enzyme on polyacrylamide employed for the determination of glucose concentration in blood sera |
389793 |
| 1.1.3.4 | analysis |
mutant glucose oxidase (B11-GOx) is obtained from directed protein evolution and wild-type enzyme. Higher glucose oxidation currents are obtained from B11-GOx both in solution and polymer electrodes compared to wild type enzyme. Improved electrocatalytic activity towards electrochemical oxidation of glucose from the mutant enzyme. The enzyme electrode with the mutant enzyme B11-GOx shows a faster electron transfer indicating a better electronic interaction with the polymer mediator. Promising application of enzymes developed by directed evolution tailored for the applications of biosensors and biofuel cells |
746771 |
