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Literature summary for 1.1.3.4 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
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Application

Application Comment Organism
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
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)

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

Protein Variants

Protein Variants Comment Organism
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]

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

Organism

Organism UniProt Comment Textmining
Aspergillus niger P13006
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Aspergillus niger

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

kcat/KM [mM/s]

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