28 by: Khaedren Bos

Student – Khaedren Bos

Enzyme: Glucose Oxidase, EC 1.1.3.4

This enzyme is produced by several fungi, such as the entire Dioszegia family, Flavodon flavus and Leucosporidium fragarium. It has also been found in a few insects, such as the honey bee, beet armyworm, and the cotton bollworm.

The primary function of glucose oxidase is to convert glucose and oxygen gas into d-glucono-δ-lactone and hydrogen peroxide. This is essential for the organisms that use it, as it allows them to break down glucose into something that can be further broken down by other enzymes. In industry, glucose oxidase can be used to improve the quality of baked goods, as the glucose oxidase in the dough improves the durability of the final product, while the hydrogen peroxide can increase the doughs elasticity and viscosity. It has also been used to break down glucose and remove oxygen surrounding products susceptible to bacterial infestation, such as dried eggs. Its most important synthetic function is as a blood glucose biosensor, where the enzyme can be used on blood samples to detect glucose.

While commonly shortened to Gox, some papers shorten glucose oxidase to GOd, meaning that it can reasonably be described as the God molecule, which I thought was humorous. Additionally, the speed of the reaction alongside the molecule’s relative durability have lead to some researchers calling it the “Ferrari” of enzymes.

 

 

References

Bauer, J.A., Zámocká, M., Majtán, J., Bauerová-Hlinková, V. (2022). Glucose Oxidase, an Enzyme “Ferrari”: Its Structure, Function, Production and Properties in the Light of Various Industrial and Biotechnological Applications. Biomolecules, 12(3), 472. https://www.mdpi.com/2218-273X/12/3/472

Brenda Enzyme Database. (2023, January). Information on EC 1.1.3.4 – glucose oxidase. https://www.brenda-enzymes.org/enzyme.php?ecno=1.1.3.4

Deng, L., Hu, C., Qin, X., Li, L., Zhang, Y., Li, P., Chen, X., (2018). The remote arginine promoting the dehydrogenation of glucose in glucose oxidase via a proton-coupled double-electron transfer mechanism. Journal of Catalysts, 367, 150-158. https://www.sciencedirect.com/science/article/abs/pii/S0021951718303440?via%3Dihub

Fesliyan, D. (2018). Silly Chicken [Song]. FesliyanStudios.

Frederick, K.R., Tung, J., Emerick, R.S., Masiarz, F.R., Chamberlain, S.H., Vasavada, A., Rosenberg, S., Chakraborty, S., Schopfer, L.M., et al., (1990). Glucose oxidase from Aspergillus niger. Cloning, gene sequence, secretion from Saccharomyces cerevisiae and kinetic analysis of a yeast-derived enzyme. Journal of Biological Chemistry, 265(7), 793-802. https://pubmed.ncbi.nlm.nih.gov/2406261/

Goodsell, G., (2006, May). Molecule of the Month: Glucose Oxidase. PDB-101. https://pdb101.rcsb.org/motm/77

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