Glucose oxidase
| Glucose oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifiers | |||||||||
| EC number | 1.1.3.4 | ||||||||
| CAS number | 9001-37-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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The glucose oxidase enzyme (GOx) (EC 1.1.3.4) is an oxido-reductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. In cells, it aids in breaking the sugar down into its metabolites.
Glucose oxidase is widely used for the determination of free glucose in body fluids (diagnostics), in vegetal raw material, and in the food industry. It also has many applications in biotechnologies, typically enzyme assays for biochemistry including biosensors in nanotechnologies.[1] It is often extracted from Aspergillus niger.
Structure
GOx is a dimeric protein, the 3D structure of which has been elucidated. The active site where glucose binds is in a deep pocket. The enzyme, like many proteins that act outside of cells, is covered with carbohydrate chains.
Activity
At pH 7, glucose exists in solution in cyclic hemiacetal form as 63.6% β-D-glucopyranose and 36.4% α-D-glucopyranose, the proportion of linear and furanose form being negligible. The glucose oxidase binds specifically to β-D-glucopyranose and does not act on α-D-glucose. It is able to oxidise all of the glucose in solution because the equilibrium between the α and β anomers is driven towards the β side as it is consumed in the reaction. [1]
Glucose oxidase catalyzes the oxidation of β-D-glucose into D-glucono-1,5-lactone, which then hydrolyzes to gluconic acid.
In order to work as a catalyst, GOx requires a cofactor, flavin adenine dinucleotide (FAD). FAD is a common component in biological oxidation-reduction (redox reactions). Redox reactions involve a gain or loss of electrons from a molecule. In the GOx-catalyzed redox reaction, FAD works as the initial electron acceptor and is reduced to FADH2. Then FADH2 is oxidized by the final electron acceptor, molecular oxygen (O2), which can do so because it has a higher reduction potential. O2 is then reduced to hydrogen peroxide (H2O2).
Applications
Glucose oxidase is widely used, coupled to peroxidase reaction that visualizes colorimetrically the formed H2O2, for the determination of free glucose in sera or blood plasma for diagnostics, using spectrometric assays manually or with automated procedures, and even point of use rapid assays.[1][2] Similar assays allows to monitor glucose levels in fermentation, bioreactors, and to control glucose in vegetal raw material and food products.[citation needed]
Enzymatic glucose biosensors use an electrode instead of O2 to take up the electrons needed to oxidize glucose and produce an electronic current in proportion to glucose concentration.[3] This is the technology behind the disposable glucose sensor strips used by diabetics to monitor serum glucose levels.[4]
In manufacturing, GOx is used as an additive thanks to its oxidizing effects: it prompts for stronger dough in bakery, replacing oxidants such as bromate.[citation needed] It also helps remove oxygen from food packaging, or D-glucose from egg white to prevent browning.[citation needed]
Glucose oxidase is found in honey and acts as a natural preservative. GOx at the surface of the honey reduces atmospheric O2 to hydrogen peroxide (H2O2), which acts as an antimicrobial barrier. GOx similarly acts as a bactericide in many cells (fungi, immune cells).[citation needed]
Related enzymes: Notatin and other names
Notatin, extracted from antibacterial cultures of Penicillium notatum, was originally named Penicillin A, but was renamed to avoid confusion with penicillin.[5] Notatin was shown to be identical to Penicillin B and glucose oxidase, enzymes extracted from other molds besides P. notatum;[6] it is now generally known as glucose oxidase.[2]
Early experiments showed that notatin exhibits in vitro antibacterial activity (in the presence of glucose) due to hydrogen peroxide formation.[5][7] In vivo tests showed that notatin was not effective in protecting rodents from Streptococcus haemolyticus, Staphylococcus aureus, or salmonella, and caused severe tissue damage at some doses.[7]
See also
References
- ↑ 1.0 1.1 1.2 Technical sheet of Glucose Oxidase, Interchim
- ↑ 2.0 2.1 Julio Raba and Horacio A. Mottola (1995). "Glucose Oxidase as an Analytical Reagent". Critical Reviews in Analytical Chemistry 25 (1): 1–42. doi:10.1080/10408349508050556.
- ↑ Blanford, Christopher F. (2013-10-17). "The birth of protein electrochemistry". Chemical Communications (Royal Society of Chemistry) 49: 11130–11132. doi:10.1039/C3CC46060F. Retrieved 2014-01-15.
- ↑ Cass, Anthony E. G.; Davis, Graham; Francis, Graeme D.; Hill, H. Allen O.; Aston, William J.; Higgins, I. John; Plotkin, Elliot V.; Scott, Lesley D. L. et al. (1984-04-01). "Ferrocene-mediated enzyme electrode for amperometric determination of glucose". Analytical Chemistry (American Chemical Society) 56: 667–671. doi:10.1021/ac00268a018. Retrieved 2014-01-15.
- ↑ 5.0 5.1 Coulthard CE, Michaelis R, Short WF, Sykes G (1945). "Notatin: an anti-bacterial glucose-aerodehydrogenase from Penicillium notatum Westling and Penicillium resticulosum sp. nov". Biochem. J. 39 (1): 24–36. PMC 1258144. PMID 16747849.
- ↑ KEILIN D, HARTREE EF (January 1952). "Specificity of glucose oxidase (notatin)". Biochem. J. 50 (3): 331–41. PMC 1197657. PMID 14915954.
- ↑ 7.0 7.1 Broom WA, Coulthard CE, Gurd MR, Sharpe ME (December 1946). "Some pharmacological and chemotherapeutic properties of notatin". Br J Pharmacol Chemother 1 (4): 225–233. PMC 1509745. PMID 19108091.
External links
- "Glucose Oxidase: A much used and much loved enzyme in biosensors" at University of Paisley
- Glucose Oxidase at the US National Library of Medicine Medical Subject Headings (MeSH)