Glucose Dehydrogenase (FADGDH-AB)

  • Enzymes for Clinical Chemistry

The enzyme is useful for the determination of D-glucose in clinical analysis and self-monitoring blood glucose meters.

Systematic name

D-Glucose : acceptor 1-oxidoreductase

Reaction formula

D-Glucose + acceptor →→→ D-Glucono-1,5-lactone + reduced acceptor

SPECIFICATION

Appearance yellow lyophilizate
Activity ≧700 U/mg
Contaminants NAD glucose dehydrogenase  ≺1.0×10-2 U/U%
Hexokinase ≺1.0×10-2 U/U%
α-glucosidase ≺1.0×10-2 U/U%
β-glucosidase ≺1.0×10-2 U/U%
Filterability ≧90%
Storage condition below -20℃ protected from light

PROPERTIES

Molecular weight ca. 85 kDa (SDS-PAGE)
Structure monomer, one mole of FAD per mole of enzyme glycoprotein
Michaelis constant 2.2×10-2M (D-glucose)
pH Optimum 7.0–7.5
pH Stability 4.5–8.0
Optimum temperature 40–50℃
Thermal stability below 45℃
Specificity D-glucose (100), maltose (≺0.01), 
D-xylose (8.7), D-galactose (0.7) ,

sucrose (0.1) ,D-mannnose (3.9),

2-deoxy-d-glucose (52.2)

APPLICATIONS

The enzyme is useful for the determination of D-glucose in clinical analysis and self-monitoring blood glucose meters.

REFERENCES

Hatada M, Loew N, Inose-Takahashi Y, Okuda-Shimazaki J, Tsugawa W, Mulchandani A, Sode K (2018)
Development of a glucose sensor employing quick and easy modification method with mediator for altering electron acceptor preference.
Bioelectrochemistry, 121, 185-190

Okuda-Shimazaki, J, Yoshida H, Sode K (2020)
FAD dependent glucose dehydrogenases – Discovery and engineering of representative glucose sensing enzymes –
Bioelectrochemistry, 132, 107414

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