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{{Short description|Class of enzymes}}
{{ambox | text = This page contains a copy of the infobox ({{tl|chembox}}) taken from revid of page ] with values updated to verified values.}}
{{Infobox enzyme
| Name = Glucose oxidase
| EC_number = 1.1.3.4
| CAS_number = 9001-37-0
| GO_code = 0046562
| image = 077-GlucoseOxidase-1gpe-composite.png
| width =
| caption = Structure of glucose oxidase dimer (dark and light blue) complexed with ] (salmon) and ]s (aquamarine) from '']''.<ref name = "Goodsell_2006">{{PDB|1gpe}}; {{cite journal |url= https://pdb101.rcsb.org/motm/77 |title= Molecule of the Month: Glucose Oxidase |author= Goodsell D |journal= RCSB Protein Data Bank |date= May 2006 |doi= 10.2210/rcsb_pdb/mom_2006_5}}</ref>
}}

{{Chembox {{Chembox
⚫ | ImageFile = Poly-(1-4)-alpha-D-Glucose.svg
⚫ | Verifiedfields = changed
| ImageSize =
⚫ | verifiedrevid = 443634049
⚫ | OtherNames = Oxidase, glucose
⚫ | ImageFile = Poly-(1-4)-alpha-D-Glucose.svg
| ImageSize = | IUPACName =
⚫ | Section1 = {{Chembox Identifiers
| IUPACName =
⚫ | OtherNames =
⚫ | Section1 = {{Chembox Identifiers
| CASNo_Ref = {{cascite|correct|CAS}} | CASNo_Ref = {{cascite|correct|CAS}}
| CASNo = 9004-53-9 | CASNo = 9001-37-0
| PubChem = | EINECS = 232-601-0
| PubChem =
| KEGG_Ref = {{keggcite|correct|kegg}} | KEGG_Ref = {{keggcite|correct|kegg}}
| KEGG = C00721 | KEGG = 1.1.3.4
| UNII_Ref = {{fdacite|correct|FDA}} | UNII_Ref = {{fdacite|correct|FDA}}
| UNII = 2NX48Z0A9G | UNII = 0T8392U5N1
| SMILES = | SMILES =
| ChemSpiderID_Ref = {{chemspidercite|changed|chemspider}} | ChemSpiderID_Ref = {{chemspidercite|changed|chemspider}}
| ChemSpiderID = NA}} | ChemSpiderID = none}}
| Section2 = {{Chembox Properties | Section2 = {{Chembox Properties
| Formula = (C<sub>6</sub>H<sub>10</sub>O<sub>5</sub>)<sub>''n''</sub> | Formula = (C<sub>6</sub>H<sub>10</sub>O<sub>5</sub>)<sub>''n''</sub>
| MolarMass = variable | MolarMass = variable
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| BoilingPt = | BoilingPt =
| Solubility = }} | Solubility = }}
| Section3 = {{Chembox Hazards | Section3 = {{Chembox Hazards
| MainHazards = | MainHazards =
| FlashPt = | FlashPt =
| Autoignition = }} | AutoignitionPt = }}
⚫ | Verifiedfields = changed
⚫ | verifiedrevid = 477166401
}} }}
The '''glucose oxidase''' enzyme ('''GOx''' or '''GOD''') also known as '''notatin''' (EC number 1.1.3.4) is an ] that catalyses the oxidation of ] to ] and ]. This enzyme is produced by certain species of fungi and insects and displays ] activity when oxygen and glucose are present.<ref name="Wong_2008">{{cite journal |vauthors= Wong CM, Wong KH, Chen XD |title= Glucose oxidase: natural occurrence, function, properties and industrial applications |journal= Applied Microbiology and Biotechnology |volume= 78 |issue= 6 |date= Apr 2008 |pages= 927–938 |pmid= 18330562 |doi= 10.1007/s00253-008-1407-4|s2cid= 2246466 }}</ref>

]

Glucose oxidase is widely used for the determination of free glucose in body fluids (]ing), in vegetal raw material, and in the food industry. It also has many applications in ], typically enzyme assays for ] including ]s in ].<ref name=GOxTechData>{{cite web |url= http://www.interchim.fr/ft/1/12718A.pdf |title= Glucose Oxidase Technical sheet |publisher= ]}}{{dead link|date=October 2017 |bot=InternetArchiveBot |fix-attempted=yes}}</ref><ref name="ghoshdastider">{{cite journal |vauthors= Ghoshdastider U, Xu R, Trzaskowski B, Mlynarczyk K, Miszta P, Viswanathan S, Renugopalakrishnan V, Filipek S |year= 2015 |title= Molecular Effects of Encapsulation of Glucose Oxidase Dimer by Graphene |journal= RSC Advances |volume= 5 |issue= 18 |pages= 13570–8 |doi= 10.1039/C4RA16852F|bibcode= 2015RSCAd...513570G }}</ref> It was first isolated by ] in 1928 from '']''.<ref>{{cite web |title=Detlev Müller discovers glucose oxidase |url=https://tacomed.com/chapter-x-modern-glucose-measuring/detlev-muller-discovers-glucose-oxidase/ |website=Tacomed.com |access-date=13 June 2017 |url-status=usurped |archive-url=https://web.archive.org/web/20180418032642/https://tacomed.com/chapter-x-modern-glucose-measuring/detlev-muller-discovers-glucose-oxidase/ |archive-date=18 April 2018}}</ref>

==Function==

Several species of fungi and insects synthesize glucose oxidase, which produces hydrogen peroxide, which kills bacteria.<ref name="Wong_2008"/>

'''Notatin''', extracted from antibacterial cultures of '']'', was originally named '''Penicillin A''', but was renamed to avoid confusion with ].<ref name=pmid16747849>{{cite journal | vauthors = Coulthard CE, Michaelis R, Short WF, Sykes G | title = Notatin: an anti-bacterial glucose-aerodehydrogenase from ''Penicillium notatum'' Westling and ''Penicillium resticulosum'' sp. nov | journal = The Biochemical Journal | volume = 39 | issue = 1 | pages = 24–36 | year = 1945 | pmid = 16747849 | pmc = 1258144 | doi = 10.1042/bj0390024}}</ref> Notatin was shown to be identical to '''Penicillin B''' and glucose oxidase, enzymes extracted from other molds besides ''P. notatum'';<ref name=pmid14915954>{{cite journal | vauthors = Keilin D, Hartree EF | title = Specificity of glucose oxidase (notatin) | journal = The Biochemical Journal | volume = 50 | issue = 3 | pages = 331–41 | date = Jan 1952 | pmid = 14915954 | pmc = 1197657 | doi = 10.1042/bj0500331}}</ref> it is now generally known as glucose oxidase.<ref name=JulioRaba/>

Early experiments showed that notatin exhibits ''in vitro'' antibacterial activity (in the presence of glucose) due to hydrogen peroxide formation.<ref name=pmid16747849/><ref name=pmid19108091>{{cite journal | vauthors = Broom WA, Coulthard CE, Gurd MR, Sharpe ME | title = Some pharmacological and chemotherapeutic properties of notatin | journal = British Journal of Pharmacology and Chemotherapy | volume = 1 | issue = 4 | pages = 225–233 | date = Dec 1946 | pmid = 19108091 | pmc = 1509745 | doi = 10.1111/j.1476-5381.1946.tb00041.x }}</ref> ''In vivo'' tests showed that notatin was not effective in protecting rodents from '']'', '']'', or ], and caused severe tissue damage at some doses.<ref name=pmid19108091/>

Glucose oxidase is also produced by the hypopharyngeal glands of ] and deposited into honey where it acts as a natural preservative. GOx at the surface of the honey reduces atmospheric O<sub>2</sub> to ] (H<sub>2</sub>O<sub>2</sub>), which acts as an ] barrier.<ref>{{cite journal | vauthors = Bucekova M, Valachova I, Kohutova L, Prochazka E, Klaudiny J, Majtan J | title = Honeybee glucose oxidase--its expression in honeybee workers and comparative analyses of its content and H<sub>2</sub>O<sub>2</sub>-mediated antibacterial activity in natural honeys | journal = Die Naturwissenschaften | volume = 101 | issue = 8 | date = Aug 2014 | pages = 661–670 | pmid = 24969731 | doi = 10.1007/s00114-014-1205-z | bibcode = 2014NW....101..661B | s2cid = 16338921 }}</ref>

== Structure ==
]
GOx is a ]ic 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 ] chains. GOx is a glucose oxidising enzyme with a molecular weight of 160 kDa. It is a dimeric glycoprotein consisting of two subunits each weighing 80 kDa. Flavinadenine dinucleotide (FAD) in the active site is buried approximately 1.5&nbsp;nm inside the protein shell and acts as the initial electron acceptor.<ref>{{cite journal |last1=Mano |first1=Nicolas |title=Engineering glucose oxidase for bioelectrochemical applications. |journal=Bioelectrochemistry |date=2019 |volume=128 |pages=218–240}}</ref>

== Mechanism ==

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 ] form being negligible. The glucose oxidase binds specifically to β-D-glucopyranose and does not act on α-D-glucose. It oxidises 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.<ref name=GOxTechData />

Glucose oxidase ]s the oxidation of β-D-glucose into ], which then ]s into ].

In order to work as a catalyst, GOx requires a ], ] (FAD). FAD is a common component in biological oxidation-reduction (]) 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 FADH<sup>−</sup>.<ref>{{cite journal |last1=Sanner |first1=Christoph |display-authors=etal |title=15N‐ and 13C‐NMR investigations of glucose oxidase from Aspergillus niger |journal=European Journal of Biochemistry |date=March 1991 |volume=196 |issue=3 |pages=663–672 |doi=10.1111/j.1432-1033.1991.tb15863.x |pmid=2013289 |doi-access=free }}</ref> Then FADH<sup>−</sup> is oxidized by the final electron acceptor, molecular ] (O<sub>2</sub>), which can do so because it has a higher reduction potential. O<sub>2</sub> is then reduced to ] (H<sub>2</sub>O<sub>2</sub>).

== Applications ==
=== Glucose monitoring ===
Glucose oxidase is widely used coupled to ] reaction that visualizes colorimetrically the formed H<sub>2</sub>O<sub>2</sub>, for the determination of free glucose in ] or ] for diagnostics, using spectrometric assays manually or with automated procedures, and even point-of-use rapid assays.<ref name=GOxTechData /><ref name=JulioRaba>{{cite journal |vauthors= Raba J, Mottola HA |title= Glucose Oxidase as an Analytical Reagent |journal= Critical Reviews in Analytical Chemistry |volume= 25 |issue= 1 |pages= 1–42 |year= 1995 |doi= 10.1080/10408349508050556 |url= http://www.biosensing.net/EBLA/Corso/Lezione%2001/GOD.PDF |access-date= 2009-01-08 |archive-date= 2021-01-10 |archive-url= https://web.archive.org/web/20210110064251/http://www.biosensing.net/EBLA/Corso/Lezione%2001/GOD.PDF |url-status= dead }}</ref>

Similar assays allows the monitoring of glucose levels in fermentation, ], and to control glucose in vegetal raw material and food products.{{Citation needed|date=August 2012}} In the glucose oxidase assay, the glucose is first oxidized, catalyzed by glucose oxidase, to produce gluconate and hydrogen peroxide. The hydrogen peroxide is then oxidatively coupled with a ] to produce a colored compound which may be measured spectroscopically. For example, hydrogen peroxide together with ] (4-AAP) and phenol in the presence of peroxidase yield a red quinoeimine dye that can be measured at 505&nbsp;nm. The absorbance at 505&nbsp;nm is proportional to concentration of glucose in the sample.

Enzymatic glucose ]s use an ] instead of O<sub>2</sub> to take up the electrons needed to oxidize glucose and produce an electronic current in proportion to glucose concentration.<ref>{{cite journal |vauthors= Blanford CF |title= The birth of protein electrochemistry |journal= Chemical Communications |volume= 49 |issue= 95 |pages= 11130–11132 |date= Dec 2013 |pmid= 24153438 |doi= 10.1039/C3CC46060F |publisher= Royal Society of Chemistry}}</ref> This is the technology behind the disposable glucose sensor strips used by ] to monitor serum glucose levels.<ref>{{cite journal |vauthors= Cass AE, Davis G, Francis GD, Hill HA, Aston WJ, Higgins IJ, Plotkin EV, Scott LD, Turner AP |title= Ferrocene-mediated enzyme electrode for amperometric determination of glucose |journal= Analytical Chemistry |volume =56 |issue= 4 |pages= 667–671 |date= Apr 1984 |pmid= 6721151 |doi= 10.1021/ac00268a018 |publisher= American Chemical Society}}</ref>

=== Food preservation ===
In manufacturing, GOx is used as an additive thanks to its oxidizing effects: it prompts for stronger dough in ], replacing oxidants such as bromate.<ref>{{cite journal |vauthors= Wong CM, Wong KH, Chen XD |title= Glucose oxidase: natural occurrence, function, properties and industrial applications |journal= Applied Microbiology and Biotechnology |volume= 78 |issue= 6 |pages= 927–38 |date= April 2008 |pmid= 18330562 |doi= 10.1007/s00253-008-1407-4|s2cid= 2246466 }}</ref> It is also used as a food preservative to help remove oxygen and glucose from food when packaged such as dry egg powder to prevent unwanted browning and undesired taste.<ref>{{cite journal |vauthors= Dubey MK, Zehra A, Aamir M, Meena M, Ahirwal L, Singh S, Shukla S, Upadhyay RS, Bueno-Mari R, Bajpai VK |display-authors= 6 |title= Improvement Strategies, Cost Effective Production, and Potential Applications of Fungal Glucose Oxidase (GOD): Current Updates |journal= Frontiers in Microbiology |volume= 8 |pages= 1032 |date= 2017 |pmid= 28659876 |pmc= 5468390 |doi= 10.3389/fmicb.2017.01032|doi-access= free }}</ref>

=== Wound treatment ===
Wound care products, such as "Flaminal Hydro" make use of an alginate hydrogel containing glucose oxidase and other components as an oxidation agent.

== Clinical trials ==

A nasal spray from a ] device that mixes glucose oxidase with glucose has undergone ]s in 2016 for the prevention and treatment of the ].<ref name="NCT01883427">{{ClinicalTrialsGov|NCT01883427|Nasal Spray With Glucose Oxidase Preventing Common Cold in Pre-school Children}}</ref><ref name="NCT01883440">{{ClinicalTrialsGov|NCT01883440|Glucose Oxidase as Treatment Against Common Cold}}</ref><ref name="NCT01883453">{{ClinicalTrialsGov|NCT01883453|A Nasal Spray With Glucose Oxidase as a Treatment of Common Cold}}</ref>

== See also ==
* ]
* ]

== References ==
{{reflist|33em}}

== External links ==
* at ]
* {{MeSH name|Glucose+Oxidase}}

{{Alcohol oxidoreductases}}
{{Enzymes}}
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