The enzyme is useful for the determination of fructosyl-peptide and fructosyl-L-amino acid.
| 由来 | recombinant E. coli |
|---|---|
| 系统名称 | Fructosyl-peptide : oxygen oxidoreductase |
| EC编号 | 1.5.3 |
| 反应式 | Fructosyl-L-amino acid + H2O + O2 →→→ Peptide + Glucosone + H2O2 |
| Appearance | yellow lyophilizate | |
|---|---|---|
| Activity |
≧6.0 U/mg |
|
| Contaminants | Catalase ≦1.0 U/U％ | |
| Stabilizer | ethylenediaminetetraacetic acid (EDTA), sodium glutamate | |
| Storage condition | below -20℃ protected from light |
| Molecular weight | ca. 60kDa (gel filtration) |
|---|---|
| Structure | monomer of 52 kDa (SDS-PAGE) |
| Isoelectric point | 4.2 |
| Michaelis constant | 3.4×10-3M (fructosyl-valyl-histidine) |
| 4.4×10-3M (fructosyl-glycine) | |
| 8.9×10-3M (Nε-fructosyl-lysine) | |
| pH Optimum | 7.5–8.0 |
| pH Stability | 6.0–9.5 |
| Optimum temperature | 35–42℃ |
| Thermal stability | below 45℃ |
| Stability (powder form) | stable at 37℃ for at least one month |
| Specificity | fructosyl-valyl-histidine (100), fructosyl-glycine (53) |
| Nε-fructosyl-lysine (84) |
The enzyme is useful for the determination of fructosyl-peptide and fructosyl-L-amino acid.
Hirokawa K, Gomi K, Bakke M, Kajiyama N. (2003)
Distribution and properties of novel deglycating enzymes for fructosyl peptide in fungi.
Archives of Microbiology, 180, 227-231.
Hirokawa K, Gomi K, Kajiyama N. (2003)
Molecular cloning and expression of novel fructosyl peptide oxidases and their application for the measurement of glycated protein.
Biochem Biophys Res Commun, 311(1), 104-111.
Hirokawa K, Shimoji K, Kajiyama N. (2005)
An enzymatic method for the determination of hemoglobinA1C.
Biotechnology Letters, 27(14), 963-968.
