Glucose Dehydrogenase (FADGDH-AD)

  • Enzymes for Clinical Chemistry

The enzyme is useful for the determination of blood glucose.

Origin recombinant Aspergillus sojae
Systematic name

D-Glucose : acceptor 1-oxidoreductase

EC Number 1.1.5.9
Reaction formula

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

SPECIFICATION

Appearance Yellow to brown lyophilizate
Activity ≧700 U/mg lyophilizate
Contaminant NAD Glucose Dehydrogenase  ≺0.01
Hexokinase ≺0.01
α-Glucosidase ≺0.01
β-Glucosidase ≺0.01
Stabilizer Not included
Storage below -20℃ protected from light

PROPERTIES

Molecular weight ca. 90 kDa (SDS-PAGE)
Structure monomer, one mole of FAD per mole of enzyme glycoprotein
Michaelis constant 6.4×10-2M (D-Glucose)
pH Optimum 7.0–7.5
pH Stability 2.5–9.5
Optimum temperature 45℃
Thermal stability (liquid form) below 60℃
Thermal stability (powder form) stable at 30℃ for at least one month
Specificity D-glucose (100%), Maltose (0.2%), 
D-xylose (0.9%), D-galactose (0.8%) 
sucrose (<0.1%),  D-Mannose (0.4%)
2-Deoxy-D-glucose (23.5%)

APPLICATIONS

Highly stable FADGDH-AD is useful for the determination of D-glucose in clinical analysis and continuous glucose monitoring meter (CGM) for diabetes patients.

Line-up

REFERENCES

Satake R, Ichiyanagi A, Ichikawa K, Hirokawa K, Araki Y, Yoshimura T, Gomi K (2015)
Novel glucose dehydrogenase from Mucor prainii: Purification, characterization, molecular cloning and gene expression in Aspergillus sojae
Biosci Bioeng., 120, 498-503

Masakari Y, Hara C, Araki Y, Gomi K, Ito K (2020)
Improvement in the thermal stability of Mucor prainii-derived FAD-dependent glucose dehydrogenase via protein chimerization 
Enzyme Microb Technol., 132, 109387, doi: 10.1016/j.enzmictec.2019.109387.
https://doi.org/10.1016/j.enzmictec.2019.109387, (cited 2020-07-02)



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