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Literature summary extracted from

  • Yu, E.; Prodanovic, R.; Güven, G.; Ostafe, R.; Schwaneberg, U.
    Electrochemical oxidation of glucose using mutant glucose oxidase from directed protein evolution for biosensor and biofuel cell applications (2011), Appl. Biochem. Biotechnol., 165, 1448-1457 .
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.3.4 analysis mutant glucose oxidase (B11-GOx) is obtained from directed protein evolution and wild-type enzyme. Higher glucose oxidation currents are obtained from B11-GOx both in solution and polymer electrodes compared to wild type enzyme. Improved electrocatalytic activity towards electrochemical oxidation of glucose from the mutant enzyme. The enzyme electrode with the mutant enzyme B11-GOx shows a faster electron transfer indicating a better electronic interaction with the polymer mediator. Promising application of enzymes developed by directed evolution tailored for the applications of biosensors and biofuel cells Aspergillus niger
1.1.3.4 energy production mutant glucose oxidase (B11-GOx) is obtained from directed protein evolution and wild-type enzyme. Higher glucose oxidation currents are obtained from B11-GOx both in solution and polymer electrodes compared to wild type enzyme. Improved electrocatalytic activity towards electrochemical oxidation of glucose from the mutant enzyme. The enzyme electrode with the mutant enzyme B11-GOx shows a faster electron transfer indicating a better electronic interaction with the polymer mediator. Promising application of enzymes developed by directed evolution tailored for the applications of biosensors and biofuel cells Aspergillus niger

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.4 expression of wild-type and mutant enzyme in Pichia pastoris Aspergillus niger

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.4 additional information mutant glucose oxidase (B11-GOx) is obtained from directed protein evolution and wild-type enzyme. Higher glucose oxidation currents are obtained from B11-GOx both in solution and polymer electrodes compared to wild type enzyme. Improved electrocatalytic activity towards electrochemical oxidation of glucose from the mutant enzyme. The enzyme electrode with the mutant enzyme B11-GOx shows a faster electron transfer indicating a better electronic interaction with the polymer mediator Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.4 16
-
 beta-D-glucose pH 5.5, 25°C, mutant enzyme B11-GOx Aspergillus niger
1.1.3.4 22
-
 beta-D-glucose pH 5.5, 25°C, wild-type enzyme Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.4 Aspergillus niger P13006
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.4
-
 Aspergillus niger

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.4 beta-D-glucose + O2
-
 Aspergillus niger D-glucono-1,5-lactone + H2O2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.4 58
-
 beta-D-glucose pH 5.5, 25°C, wild-type enzyme Aspergillus niger
1.1.3.4 80
-
 beta-D-glucose pH 5.5, 25°C, mutant enzyme B11-GOx Aspergillus niger

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.3.4 2.64
-
 beta-D-glucose pH 5.5, 25°C, wild-type enzyme Aspergillus niger
1.1.3.4 5
-
 beta-D-glucose pH 5.5, 25°C, mutant enzyme B11-GOx Aspergillus niger