Specificity of glucose oxidase

Adams, Ernest C.; Mast, R.L.; Free, Alfred H.

doi:10.1016/0003-9861(60)90495-1

Cited by 50 publications

(20 citation statements)

References 9 publications

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“…was shown to be highly specific for ,-D-glucose. Although D-mannose, D-galactose, 2-deoxy-D-glucose, and D-xylose have been shown to exhibit low activities as substrates, no greater than 2% of the activity found with glucose was found with these or 50 other carbohydrates tested (1,3). The enzyme from P. chrysosporium had 33, 13, and 7% specific activity, respectively, with sorbose, xylose, and maltose compared with that seen with glucose as the substrate.…”

Section: Resultsmentioning

confidence: 93%

Purification and characterization of glucose oxidase from ligninolytic cultures of Phanerochaete chrysosporium

Kelley¹,

Reddy²

1986

J Bacteriol

114

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Glucose oxidase, an important source of hydrogen peroxide in lignin-degrading cultures of Phanerochaete chrysosporium, was purified to electrophoretic homogeneity by a combination of ion-exchange and molecular sieve chromatography. The enzyme is a flavoprotein with an apparent native molecular weight of 180,000 and a denatured molecular weight of 80,000. This enzyme does not appear to be a glycoprotein. It gives optimal activity with D-glucose, which is stoichiometrically oxidized to D-gluconate. The enzyme has a relatively broad pH optimum of 4 to 5. It is inhibited by Ag+ (10 mM) and o-phthalate (100 mM), but not by Cu2+, NaF, or KCN (each 10 mM).

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Section: Resultsmentioning

confidence: 93%

Purification and characterization of glucose oxidase from ligninolytic cultures of Phanerochaete chrysosporium

Kelley¹,

Reddy²

1986

J Bacteriol

114

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“…GOD from Aspergillus niger is a flavin-containing glycoprotein with extreme specificity for the substrate D-glucose. GOD has also been shown to be able to oxidize saccharides other than D-glucose [2][3][4][5][6], but these studies indicated that other saccharides were more slowly oxidized than D-glucose. The differences in oxidation rates of various saccharides indicate that certain structural features of the substrates are important for the enzymatic reaction.…”

mentioning

confidence: 96%

Enzymatic Oxidation and Separation of Various Saccharides with Immobilized Glucose Oxidase

Mislovičová

Pätoprstý

Vikartovská

2010

Appl Biochem Biotechnol

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Glucose oxidase from Aspergillus niger, the specific enzyme for beta-D-glucose oxidation, can also oxidize other related saccharides at very slow or negligible rates. The present study aimed to compare the kinetics of D-glucose oxidation using immobilized glucose oxidase on bead cellulose for the oxidation of related saccharides using the same biocatalyst. The significant differences were observed between the reaction rates for D-glucose and other saccharides examined. As a result, k (cat)/K (M) ratio for D-glucose was determined to be 42 times higher than D-mannose, 61.6 times higher than D-galactose, 279 times higher than D-xylose, and 254 times higher than for D-fructose and D-cellobiose. On the basis of these differences, the ability of immobilized glucose oxidase to remove D-glucose from D-cellobiose, D-glucose from D-xylose, and D-xylose from D-lyxose was examined. Immobilized catalase on Eupergit and mixed with immobilized glucose oxidase on bead cellulose or co-immobilized with glucose oxidase on bead cellulose was used for elimination of hydrogen peroxide from the reaction mixture. The accelerated elimination of D-glucose and D-xylose in the presence of co-immobilized catalase was observed. The co-immobilized glucose oxidase and catalase were able to decrease D-glucose or D-xylose content to 0-0.005% of their initial concentrations, while a minimum decrease of low oxidized saccharides D-xylose, D-cellobiose, and D-lyxose, respectively, was observed.

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“…Based on Figure 6, a significant amount of H 2 O 2 production was detected when glucose was used as the substrate. Reference [30] shows the performance of free GOx, in which it rapidly oxidized glucose and requires a few hundreds times as much GOx to catalyze the oxidation of other type of sugars. Therefore, the high specificity of GOx-magnetic CNCs towards glucose as compared to other type of sugar suggested that the immobilization process did not affect the specificity of GOx.…”

Section: Resultsmentioning

confidence: 99%

Colorimetric Analysis of Glucose Oxidase-Magnetic Cellulose Nanocrystals (CNCs) for Glucose Detection

Yee

Hashim

Yahya

et al. 2019

Sensors

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Glucose oxidase (EC 1.1.3.4) sensors that have been developed and widely used for glucose monitoring have generally relied on electrochemical principle. In this study, the potential use of colorimetric method for glucose detection utilizing glucose oxidase-magnetic cellulose nanocrystals (CNCs) is explored. Magnetic cellulose nanocrystals (magnetic CNCs) were fabricated using iron oxide nanoparticles (IONPs) and cellulose nanocrystals (CNCs) via electrostatic self-assembly technique. Glucose oxidase was successfully immobilized on magnetic CNCs using carbodiimide-coupling reaction. About 33% of GOx was successfully attached on magnetic CNCs, and the affinity of GOx-magnetic CNCs to glucose molecules was slightly higher than free enzymes. Furthermore, immobilization does not affect the specificity of GOx-magnetic CNCs towards glucose and can detect glucose from 0.25 mM to 2.5 mM. Apart from that, GOx-magnetic CNCs stored at 4 °C for 4 weeks retained 70% of its initial activity and can be recycled for at least ten consecutive cycles.

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Specificity of glucose oxidase

Cited by 50 publications

References 9 publications

Purification and characterization of glucose oxidase from ligninolytic cultures of Phanerochaete chrysosporium

Purification and characterization of glucose oxidase from ligninolytic cultures of Phanerochaete chrysosporium

Enzymatic Oxidation and Separation of Various Saccharides with Immobilized Glucose Oxidase

Colorimetric Analysis of Glucose Oxidase-Magnetic Cellulose Nanocrystals (CNCs) for Glucose Detection

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