The enzyme is useful for the determination of fructosyl-peptide and fructosyl-L-amino acid.
| Origin | recombinant E. coli |
|---|---|
| Systematic name | Fructosyl-peptide : oxygen oxidoreductase |
| EC Number | 1.5.3 |
| Reaction formula | Fructosyl-L-amino acid + H2O + O2 →→→ Peptide + Glucosone + H2O2 |
| Appearance | yellow lyophilizate |
|---|---|
| Activity | ≧5.0 U/mg |
| Contaminants | Catalase ≦1.0 U/U％ |
| Stabilizer | sodium glutamate, ethylenediaminetetraacetic acid (EDTA) |
| Storage condition | below -20℃ protected from light |
| Molecular weight | ca. 60 kDa (gel filtration) |
|---|---|
| Structure | monomer of 52 kDa(SDS-PAGE) |
| Michaelis constant | 1.5×10-3M(fructosyl-valyl-histidine) 5.0×10-3M (fructosyl-glysine) 9.0×10-3M(Nε-fructosyl-lysine) |
| pH Optimum | 7.5–8.5 |
| pH Stability | 5.5–9.5 |
| Optimum temperature | 37–45℃ |
| Thermal stability | below 45℃ |
| Stability (powder form) | stable at -20℃ for at least 12 months |
| Specificity | fructosyl-valyl-histidine (100), fructosyl-glycine(150) |
| Nε-fructosyl-L-lysine (68.6) |
The enzyme is useful for the determination of fructosyl-peptide and fructosyl-L-amino acid.
Hirokawa K, Shimoji K, Kajiyama N. (2005)
An enzymatic method for the determination of hemoglobinA1C.
Biotechnology Letters, 27(14), 963-968.
Hirokawa K, Ichiyanagi A, Kajiyama N. (2008)
Enhancement of thermostability of fungal deglycating enzymes by directed evolution.
Applied Mcrobiology and Biotechnology, 78(5), 775-781.
Ichiyanagi A, Hirokawa K, Gomi K, Nakatsu T, Kato H, Kajiyama N. (2013)
Crystallization and preliminary crystallographic analysis of two eukaryotic fructosyl peptide oxidases.
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 69(2), 130-133.
