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1.1.3.4: glucose oxidase

This is an abbreviated version!
For detailed information about glucose oxidase, go to the full flat file.

Word Map on EC 1.1.3.4

Reaction

beta-D-glucose
+
O2
=
D-glucono-1,5-lactone
 +
H2O2

Synonyms

AldO, beta-D-glucose oxidase, beta-D-glucose oxygen-1-oxidoreductase, beta-D-glucose/oxygen 1-oxidoreductase, beta-D-glucose: oxygen 1-oxidoreductase, beta-D-glucose:O2 1-oxidoreductase, beta-D-glucose:O2-1-oxidoreductase, beta-D-glucose:oxygen 1-oxido-reductase, beta-D-glucose:oxygen 1-oxidoreductase, beta-D-glucose:oxygen oxidoreductase, beta-D-glucose:oxygen-1-oxidoreductase, beta-D-glucose:quinone oxidoreductase, CngoxA, corylophyline, D-glucose oxidase, D-glucose-1-oxidase, deoxin-1, glucose aerodehydrogenase, glucose oxyhydrase, glucose-1-oxidase, GO-2, GOD, GOX, GOxP5, microcid, More, notatin, oxidase, glucose, pen-GOx, penatin, yGOXpenag

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.4 glucose oxidase

General Stability

General Stability on EC 1.1.3.4 - glucose oxidase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
3°C, little loss of activity, 3 years
-
4.0 M urea, immunoaffinity-layered preparation retains 87% of original activity after 2 h and 40% of activity after 24 h of incubation, whereas the soluble enzyme loses all of its activity within 1 h of preincubation
-
after immobilization of the oxidized GOX with silver nanoparticles, the Km and Vmax of the immobilization enzyme remarkably reduce and increase, respectively. While the bioconjugate is stable in lower temperatures and also in neutral to basic pH, the enzymatic activity of the bioconjugate slightly decreases in higher temperature
-
Ca2+ and Mg2+ at 1 M induce compaction of the native conformation of the enzyme, and the enzyme shows a higher stability as compared to the native enzyme against urea denaturation, Ca2+ and Mg2+ at concentrations above 2 M induce dissociation of the native dimeric enzyme, resulting in stabilization of the enzyme monomer, 3 M Ca2+-stabilized monomer retains about 70% secondary structure present in the native enzyme dimer, however there is a complete loss of cooperative interactions between these secondary structural elements present in the enzyme
-
chemical denaturation by 6.67 M guanidine HCl is accompanied by dissociation of the homodimeric enzyme into monomers
-
comparative stability of insoluble complexes of enzyme obtained with concanavalin A and glycosyl-specific polyclonal antibodies, overview
-
comparison of stability immobilized on various materials
-
D2O stabilizes
-
divalent cations such as Ba2+, Ca2+ and Mg2+ have a slightly negative effect on stability
-
encapsulation of the enzyme in the liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine increases the enzyme stability through its decreased inhibition because of H2O2 produced in glucose oxidation
-
freezing/thawing, stable
-
high hydrostatic pressure stabilizes the aniline-, and benzoate-modified glucose oxidase at 69.1-80°C compared to atmospheric pressure. At 240 MPa and 80.0°C, the first order rate constant of inactivation (k(inact)) of aniline-modified enzyme is 0.02/min, or 3.7 times smaller than for the native enzyme, while the k(inact) for benzoate-modified enzyme is 0.26/min, or 2.8times smaller than for the native enzyme at the same temperature. At 240 MPa and 80.0°C, the k(inact) of the aniline-modified enzyme is 69times smaller than the k(inact) of native enzyme (15.3/min) at 0.1 MPa and 80.0°C. The combination of high hydrostatic pressure and hydrophobic modification makes more thermostable
K2SO4 enhances the thermal stability by primarily strengthening the hydrophobic interactions and makes the holoenzyme a more compact dimeric structure
-
KCl stabilizes
-
low temperature ultrasonic processing of GOx (23 kHz at 4°C) does not appreciably compromise bioactivity
-
most stable, highly active and high-yield glucose oxidase preparations are optained by assembling the enzyme on small amounts of immunoaffinity support using glycosyl-specific polyclonal antibodies
-
NaCl stabilizes
-
protein/water interfacial tension as a critical physicochemical attribute of excipients that is crucial for increasing enzyme kinetic stability
SDS, 1%, 30°C, pH 5.5, stable 30 h incubation
-
SDS, 1.5%, 2-mercaptoethanol, 55°C, residual activity: 24%
-
SDS, 5%, stable to
-
stabilita to 4 M urea of soluble and insoluble enzyme complexes, overview
-
the activity of glucose oxidase is retained for more than three days in the water pool of the microemulsion, while a 30% loss in activity of the enzyme occurs in aqueous medium during that period
-
the complexation between GOX, chitosan, and calcium alginate stabilizes the enzyme, GOX retains its integrity upon adsorption to calcium alginate gel beads during the coating and after release from alginate/chitosan microsphere
-
the enzyme shows a pH-dependent response to the high pressure homogenization treatment, with reduction or maintenance of activity at pH 4.5-6.0 and a remarkable activity increase (30-300%) at pH 6.5 at all tested temperatures. i.e. 15°C, 50°C and 75°C. The enzyme's thermal tolerance is reduced due to high pressure homogenization treatment and the storage for 24 h at high temperatures of 50°C and 75°C also causes a reduction of activity
-
the enzyme stability is not influenced by physiological concentration of sodium chloride (140 mM)
the maximum enzymatic activity of copolymer-conjugated GOD (poly(N-isopropylacrylamide-co-methacrylic acid-co-octadecylacrylate)-conjugated GOD) is about 40-55% of that of native GOD
-
the poly(methyl methacrylate)-bovine serum albumin particle-adsorbed GOx can retain at least 80% of the free enzyme activity
-
the stabilization of the enzyme by NaCl and lysozyme is primarily the result of charge neutralization
-
urea: 7 M, 5 min, activity fully restored
-