| Origin | recombinant E. coli |
|---|---|
| Lineage name | Fructosyl-L-amino acid : oxygen oxidoreductase |
| EC Number | 1.5.3 |
| Reaction formula | Fructosyl-L-amino acid + H2O + O2→→→ L-Amino acid + Glucosone + H2O2 |
Fructosyl-amino Acid Oxidase (FAOD-E)
- The enzyme is useful for the determination of fructosyl-L-amino acid.
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SPECIFICATION
| Appearance | yellow lyophilizate | |
|---|---|---|
| Activity | ≧4 U/mg lyophilizate | |
| Stabilizer | Trehalose | |
| Storage | below -20℃ protected from light |
PROPERTIES
| Molecular weight | ca. 45 kDa (gel filtration) |
|---|---|
| Structure | monomer of 50 kDa (SDS-PAGE) |
| Michaelis constant | 2.2×10-4M (Nε-fructosyl-L-lysine) |
| pH Optimum | 8.0–8.5 |
| pH Stability | 6.0–8.5 |
| Optimum temperature | 35–40℃ |
| Thermal stability | below 30℃ |
| Stability (liquid form) | stable at 25℃ for at least two weeks |
| Stability (powder form) | stable at 37℃ for at least one month |
| Inhibitors | Ag2+，Cu2+ |
| Specificity | Nε-fructosyl-L-lysine (100), fructosyl-L-valine (65) |
| fructosyl-glycine (30) |
APPLICATIONS
The enzyme is useful for the determination of fructosyl-L-amino acid.
REFERENCES
- Horiuchi, T. et al., Agric. Biol. Chem., 53, 103–110 (1989).
- Sakaue, R. et al., Biosci. Biotechnol. Biochem., 66, 1256–1261 (2002).
- Hirokawa, K. and Kajiyama, N., Biosci. Biotechnol. Biochem., 66, 2323–2329 (2002).
- Sakaue, R. and Kajiyama, N., Appl. Environ. Microbiol., 69, 139–145 (2003).
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