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a monosaccharide sugar that has several forms; an important source of physiological energy
any of the enzymes that catalyze biological oxidation

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/12/17 20:52:39」(JST)

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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[edit]

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[edit]

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[edit]

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]}

Enzyme electrode biosensors detect levels of glucose by keeping track of the number of electrons passed through the enzyme by connecting it to an electrode and measuring the resulting charge. This has a possible application in the world of nanotechnology when used in conjunction with tiny electrodes as glucose sensors for diabetics.^{[citation needed]}

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[edit]

Notatin, extracted from antibacterial cultures of Penicillium notatum, was originally named Penicillin A, but was renamed to avoid confusion with penicillin.^[3] Notatin was shown to be identical to Penicillin B and glucose oxidase, enzymes extracted from other molds besides P. notatum;^[4] 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.^[3]^[5] 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.^[5]

References[edit]

^ ^a ^b ^c Technical sheet of Glucose Oxidase, Interchim
^ ^a ^b 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.
^ ^a ^b 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. Cite uses deprecated parameters (help)
^ ^a ^b 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. Cite uses deprecated parameters (help)

External links[edit]

"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)

UpToDate Contents

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1. 成人糖尿病患者のマネージメントにおける血糖の自己モニタリング（SMBG） blood glucose self monitoring in management of adults with diabetes mellitus
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4. 慢性肉芽腫性疾患：病因、臨床症状、および診断 chronic granulomatous disease pathogenesis clinical manifestations and diagnosis
5. 薬物熱 drug fever

English Journal

Silicon/SU8 multi-electrode micro-needle for in vivo neurochemical monitoring.

Vasylieva N1, Marinesco S2, Barbier D3, Sabac A4.
Biosensors & bioelectronics.Biosens Bioelectron.2015 Oct 15;72:148-55. doi: 10.1016/j.bios.2015.05.004. Epub 2015 May 6.
Simultaneous monitoring of glucose and lactate is an important challenge for understanding brain energetics in physiological or pathological states. We demonstrate here a versatile method based on a minimally invasive single implantation in the rat brain. A silicon/SU8-polymer multi-sensing needle-s
PMID 25978443

Enzymatically catalytic deposition of gold nanoparticles by glucose oxidase-functionalized gold nanoprobe for ultrasensitive electrochemical immunoassay.

Cheng H1, Lai G2, Fu L3, Zhang H1, Yu A4.
Biosensors & bioelectronics.Biosens Bioelectron.2015 Sep 15;71:353-8. doi: 10.1016/j.bios.2015.04.061. Epub 2015 Apr 23.
A novel ultrasensitive immunoassay method was developed by combination of the enzymatically catalytic gold deposition with the prepared gold nanoprobe and the gold stripping analysis at an electrochemical chip based immunosensor. The immunosensor was constructed through covalently immobilizing captu
PMID 25932794

Self-powered competitive immunosensor driven by biofuel cell based on hollow-channel paper analytical devices.

Li S1, Wang Y1, Ge S2, Yu J3, Yan M1.
Biosensors & bioelectronics.Biosens Bioelectron.2015 Sep 15;71:18-24. doi: 10.1016/j.bios.2015.04.019. Epub 2015 Apr 7.
A mediator-less and compartment-less glucose/O2 enzymatic biofuel cell (BFC) was introduced into microfluidic paper-based analytical devices (μ-PADs) that relies on flow in hollow channels with silver nanoparticles/graphene modified paper electrode as the anodic and cathodic substrate, to implement
PMID 25880834

Japanese Journal

Glucose oxidase adsorption performance of carbonaceous mesocellular foams prepared with different carbon sources

Zhou Fengjiao,Pu Ximing,Luo Dapeng [他]
Journal of bioscience and bioengineering 120(1), 9-16, 2015-07
NAID 40020537922

部位特異的変異によるピラノース酸化酵素の色素依存性脱水素酵素活性の向上

荒木俊雄,中柄朋子,田村隆,稲垣賢二
岡山大学農学部学術報告 104, 1-4, 2015-02-01
… 　Pyranose oxidase (EC 1.1.3.10 ; … It is considered that the reactivity of PROD for 1,5‒AG is useful in the development of an amperometric-type biosensor, which is a convenient diagnostic device for selfmonitoringblood glucose (SMBG). … In the present study, we attempted to develop an O2‒insensitive oxidase that would improve the dye-mediated dehydrogenase activity. …
NAID 120005537567

交互累積法による機能性ナノ薄膜及びミクロカプセルの開発

佐藤勝彦
薬学雑誌. 乙号 135(9), 1029-1035, 2015
… In particular, glucose-sensitive LbL films have been widely studied for use as glucose sensors and in glucose-triggered drug delivery systems. … In this work, I report on glucose-sensitive LbL films that consist of concanavalin A (ConA), phenylboronic acid (PBA), and glucose oxidase (GOx). …
NAID 130005096683

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Glucose oxidase
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CAS number	9001-37-0
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英: glucose oxidase
関: グルコースオキシダーゼ

「グルコースオキシダーゼ」

　　[★]

英: glucose oxidase
関: グルコース酸化酵素

[GOxTechData-1] Technical sheet of Glucose Oxidase, Interchim

[JulioRaba-2] 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.

[pmid16747849-3] 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.

[pmid14915954-4] KEILIN D, HARTREE EF (January 1952). "Specificity of glucose oxidase (notatin)". Biochem. J. 50 (3): 331–41. PMC 1197657. PMID 14915954. Cite uses deprecated parameters (help)

[pmid19108091-5] 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. Cite uses deprecated parameters (help)

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glucose oxidase