Glucose oxidase is an enzyme that catalyzes the oxidation of glucose to gluconic acid and hydrogen peroxide. It is widely used in various industrial applications, including food processing, diagnostics, and cosmetics, for its ability to regulate glucose levels and, in some cases, stabilize light-sensitive compounds. In the context of light stabilization, glucose oxidase can help to reduce the oxidative damage caused by exposure to light, thus enhancing the shelf-life and stability of certain products, particularly in cosmetics and personal care items.

Chemical Composition and Structure

• Enzyme Structure: Glucose oxidase is a glycoprotein composed of amino acids, with a heme group that facilitates the oxidation of glucose. The enzyme functions by using oxygen to oxidize glucose, producing hydrogen peroxide and gluconic acid as byproducts.
• Active Site: The enzyme's active site binds to glucose and facilitates the oxidation reaction, releasing hydrogen peroxide, which plays a role in controlling the oxidative processes in light-sensitive environments.

Function as a Light Stabilizer

Glucose oxidase can act as a light stabilizer by reducing the presence of free radicals and hydrogen peroxide that are generated by light exposure. This reduction in oxidative stress helps to:

• Prevent photo-oxidation: By breaking down glucose and producing hydrogen peroxide in a controlled manner, glucose oxidase can reduce the harmful effects of light exposure on sensitive compounds.
• Enhance the stability of formulations: In cosmetics and personal care products, this enzyme helps prevent the degradation of active ingredients or sensitive compounds in formulations that are prone to light-induced degradation.
• Extend shelf life: By stabilizing light-sensitive components, glucose oxidase helps extend the shelf life of products exposed to light during storage or usage.

Applications

Cosmetics and Personal Care Products

• Light-sensitive ingredients: In formulations containing ingredients that are sensitive to light, such as vitamins (e.g., vitamin C), glucose oxidase can help maintain their stability by mitigating oxidative damage.
• Preservation: It is used in cosmetic products like creams, serums, and lotions to preserve their effectiveness and ensure that the active ingredients do not degrade quickly when exposed to light.
• Anti-aging products: In anti-aging formulations, glucose oxidase can protect delicate ingredients from degradation, preserving their anti-aging benefits.

CAS   9001-37-0   EC number   232-601-0

Food Industry

• Oxidation control: It is used in food products to control oxidation, especially in light-sensitive products like fruit juices and beverages, helping to maintain freshness and extend shelf life.

Pharmaceuticals

• Stabilizing active compounds: In pharmaceutical formulations, glucose oxidase can be used to stabilize light-sensitive active ingredients, ensuring their potency and effectiveness throughout their shelf life.

Environmental and Safety Considerations

• Biodegradability: Glucose oxidase is a natural enzyme and is biodegradable, making it environmentally friendly when disposed of correctly.
• Safety Profile: Generally considered safe for use in cosmetics, personal care, and food applications, glucose oxidase is non-toxic. However, it is important to ensure that the enzyme is used in appropriate concentrations as excessive amounts of hydrogen peroxide can cause irritation.
• Sustainability: Since glucose oxidase is a naturally occurring enzyme, it can be sustainably sourced, particularly if derived from non-GMO sources, offering an environmentally friendly alternative to synthetic light stabilizers.

References__________________________________________________________________________

Bankar SB, Bule MV, Singhal RS, Ananthanarayan L. Glucose oxidase--an overview. Biotechnol Adv. 2009 Jul-Aug;27(4):489-501. doi: 10.1016/j.biotechadv.2009.04.003. 

Abstract. Glucose oxidase (beta-D-glucose:oxygen 1-oxidoreductase; EC 1.1.2.3.4) catalyzes the oxidation of beta-D-glucose to gluconic acid, by utilizing molecular oxygen as an electron acceptor with simultaneous production of hydrogen peroxide. Microbial glucose oxidase is currently receiving much attention due to its wide applications in chemical, pharmaceutical, food, beverage, clinical chemistry, biotechnology and other industries. Novel applications of glucose oxidase in biosensors have increased the demand in recent years. Present review discusses the production, recovery, characterization, immobilization and applications of glucose oxidase. Production of glucose oxidase by fermentation is detailed, along with recombinant methods. Various purification techniques for higher recovery of glucose oxidase are described here. Issues of enzyme kinetics, stability studies and characterization are addressed. Immobilized preparations of glucose oxidase are also discussed. Applications of glucose oxidase in various industries and as analytical enzymes are having an increasing impact on bioprocessing.

Liang Z, Yan Y, Zhang W, Luo H, Yao B, Huang H, Tu T. Review of glucose oxidase as a feed additive: production, engineering, applications, growth-promoting mechanisms, and outlook. Crit Rev Biotechnol. 2023 Dec;43(5):698-715. doi: 10.1080/07388551.2022.2057275.

Abstract. The regulation and prohibition of antibiotics used as growth promoters (AGP) in the feed field are increasing because they cause antimicrobial resistance and drug residue issues and threaten community health. Recently, glucose oxidase (GOx) has attracted increasing interest in the feed industry as an alternative to antibiotics. GOx specifically catalyzes the production of gluconic acid (GA) and hydrogen peroxide (H2O2) by consuming molecular oxygen, and plays an important role in relieving oxidative stress, preserving health, and promoting animal growth. To expand the application of GOx in the feed field, considerable efforts have been made to mine new genetic resources. Efforts have also been made to heterologously overexpress relevant genes to reduce production costs and to engineer proteins by modifying enzyme properties, both of which are bottleneck problems that limit industrial feed applications. Herein, the: different sources, diverse biochemical properties, distinct structural features, and various strategies of GOx engineering and heterologous overexpression are summarized. The mechanism through which GOx promotes growth in animal production, including the improvement of antioxidant capacity, maintenance of intestinal microbiota homeostasis, and enhancement of gut function, are also systematically addressed. Finally, a new perspective is provided for the future development of GOx applications in the feed field.

Bauer JA, Zámocká M, Majtán J, Bauerová-Hlinková V. Glucose Oxidase, an Enzyme "Ferrari": Its Structure, Function, Production and Properties in the Light of Various Industrial and Biotechnological Applications. Biomolecules. 2022 Mar 19;12(3):472. doi: 10.3390/biom12030472. 

Abstract. Glucose oxidase (GOx) is an important oxidoreductase enzyme with many important roles in biological processes. It is considered an "ideal enzyme" and is often called an oxidase "Ferrari" because of its fast mechanism of action, high stability and specificity. Glucose oxidase catalyzes the oxidation of β-d-glucose to d-glucono-δ-lactone and hydrogen peroxide in the presence of molecular oxygen. d-glucono-δ-lactone is sequentially hydrolyzed by lactonase to d-gluconic acid, and the resulting hydrogen peroxide is hydrolyzed by catalase to oxygen and water. GOx is presently known to be produced only by fungi and insects. The current main industrial producers of glucose oxidase are Aspergillus and Penicillium. An important property of GOx is its antimicrobial effect against various pathogens and its use in many industrial and medical areas. The aim of this review is to summarize the structure, function, production strains and biophysical and biochemical properties of GOx in light of its various industrial, biotechnological and medical applications.

Leskovac V, Trivić S, Wohlfahrt G, Kandrac J, Pericin D. Glucose oxidase from Aspergillus niger: the mechanism of action with molecular oxygen, quinones, and one-electron acceptors. Int J Biochem Cell Biol. 2005 Apr;37(4):731-50. doi: 10.1016/j.biocel.2004.10.014.

Abstract. Glucose oxidase from the mold Aspergillus niger (EC 1.1.3.4) oxidizes beta-D-glucose with a wide variety of oxidizing substrates. The substrates were divided into three main groups: molecular oxygen, quinones, and one-electron acceptors. The kinetic and chemical mechanism of action for each group of substrates was examined in turn with a wide variety of kinetic methods and by means of molecular modeling of enzyme-substrate complexes. There are two proposed mechanisms for the reductive half-reaction: hydride abstraction and nucleophilic attack followed by deprotonation. The former mechanism appears plausible; here, beta-D-glucose is oxidized to glucono-delta-lactone by a concerted transfer of a proton from its C1-hydroxyl to a basic group on the enzyme (His516) and a direct hydride transfer from its C1 position to the N5 position in FAD. The oxidative half-reaction proceeds via one- or two-electron transfer mechanisms, depending on the type of the oxidizing substrate. The active site of the enzyme contains, in addition to FAD, three amino acid side chains that are intimately involved in catalysis: His516 with a pK(a)=6.9, and Glu412 with pK(a)=3.4 which is hydrogen bonded to His559, with pK(a)>8. The protonation of each of these residues has a strong influence on all rate constants in the catalytic mechanism.

Wong CM, Wong KH, Chen XD. Glucose oxidase: natural occurrence, function, properties and industrial applications. Appl Microbiol Biotechnol. 2008 Apr;78(6):927-38. doi: 10.1007/s00253-008-1407-4.

Abstract. Glucose oxidase (GOX) from Aspergillus niger is a well-characterised glycoprotein consisting of two identical 80-kDa subunits with two FAD co-enzymes bound. Both the DNA sequence and protein structure at 1.9 A have been determined and reported previously. GOX catalyses the oxidation of D: -glucose (C(6)H(12)O(6)) to D: -gluconolactone (C(6)H(10)O(6)) and hydrogen peroxide. GOX is produced naturally in some fungi and insects where its catalytic product, hydrogen peroxide, acts as an anti-bacterial and anti-fungal agent. GOX is Generally Regarded As Safe, and GOX from A. niger is the basis of many industrial applications. GOX-catalysed reaction removes oxygen and generates hydrogen peroxide, a trait utilised in food preservation. GOX has also been used in baking, dry egg powder production, wine production, gluconic acid production, etc. Its electrochemical activity makes it an important component in glucose sensors and potentially in fuel cell applications. This paper will give a brief background on the natural occurrence, functions as well as the properties of glucose oxidase. A good coverage on the diverse uses of glucose oxidase in the industry is presented with a brief outline on the working principles in the various settings. Furthermore, food grade GOX preparations are relatively affordable and widely available; the readers may be encouraged to explore other potential uses of GOX. One example is that GOX-catalysed reaction generates significant amount of heat (~200 kJ/mol), and this property has been mostly neglected in the various applications described so far.