Glucose Dehydrogenase (FADGDH-AD) 葡萄糖脱氢酶| 龟甲万百欧凯米发株式会社


Glucose Dehydrogenase (FADGDH-AD) 葡萄糖脱氢酶

  • 临床检测用酶

The enzyme is useful for the determination of blood glucose and for continuous glucose monitoring (CGM) sensor.

由来 recombinant Aspergillus sojae

D-Glucose : acceptor 1-oxidoreductase


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.


  • Glucose Dehydrogenase (FADGDH-AB)


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)


  • 产品单页
  • SDS