| 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 (FAOX-TE)
- The enzyme is useful for the determination of fructosyl-L-amino acid.
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SPECIFICATION
| Appearance | yellow lyophilizate | |
|---|---|---|
| Activity | ≧1.0 U/mg lyophilizate | |
| Stabilizer | trehalose | |
| Storage | below -20℃ protected from light |
PROPERTIES
| Molecular weight | ca. 88 kDa (gel filtration) |
|---|---|
| Structure | 2 subunits of 44 kDa (SDS-PAGE) |
| Isoelectric point | 4.2 |
| Michaelis constant | 5.0×10-4M (fructosyl-glycine) |
| pH Optimum | 7.5–8.5 |
| pH Stability | 6.0–10.0 |
| Optimum temperature | 40–50℃ |
| Thermal stability | below 45℃ |
| Stability (liquid form) | stable at 20℃ for at least two weeks |
| Stability (powder form) | stable at 37℃ for at least one month |
| Inhibitors | Hg2+，Pb2+ |
| Specificity | fructosyl-glycine (100), fructosyl-L-valine (132) |
| Nε-fructosyl-L-lysine (0) |
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).
- Sakaue, R. et al., Acta Cryst., F61, 196–198 (2005).
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