Glucose Dehydrogenase (FADGDH-AD) グルコースデヒドロゲナーゼ (FADGDH-AD)

  • 臨床診断用酵素


由来 recombinant A. sojae

D-Glucose : acceptor 1-oxidoreductase

EC 番号

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


Appearance yellow to brown lyophilizate
Activity ≧700 U/mg
Contaminants NAD glucose dehydrogenase  <0.01 U/U%
Hexokinase  <0.01 U/U%
α-glucosidase  <0.01 U/U%
β-glucosidase  <0.01 U/U%
Storage condition below -20℃ protected from light


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
Inhibitors Mn2+, Ag+
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%)


FADGDH-AD is useful for the determination of D-glucose in clinical analysis and continuous glucose monitoring (CGM) meter for diabetes patients. The FADGDH-AD was developed as an oxygen-insensitive alternative to Glucose oxidase (GOD) with its high stability for the applications such as bioelectrodes in glucose sensing device and glucose enzymatic fuel cells.



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., (cited 2020-07-02)