Performance of D-amino acid oxidase in presence of ionic liquids
- Publikations-Art
- Zeitschriftenbeitrag (peer-reviewed)
- Autoren
- Lutz-Wahl, S., Trost, E.-M., Wagner, B., Manns, A., Fischer, L.
- Erscheinungsjahr
- 2006
- Veröffentlicht in
- J. Biotechnol.
- Band/Volume
- 124/
- DOI
- 10.1016/j.jbiotec.2006.01.023
- Seite (von - bis)
- 163-171
The activity and stability of free and immobilized D-amino acid oxidase (DAAO, EC 1.4.3.3) from Trigonopsis variabilis CBS 4095 in different water-sol. and water-insol. ionic liqs. (ILs) as well as in org. solvents were studied for comparison. The most promising ILs ([BMIM][BF4] and [MMIM][MMPO4]) were investigated in detail. The kinetic parameters (nmax = 187 nkat/g dry wt., KM = 1.38 mM) with D-phenylalanine as substrate were calcd. in 40% [BMIM][BF4]. Bioconversions of D/L-phenylalanine in 40% [BMIM][BF4] and 20% [MMIM][MMPO4] on a 3 mL scale using immobilized DAAO were performed by addn. of free catalase from Micrococcus lysodeikticus. After total conversion of substrate in presence of 20% [MMIM][MMPO4] the residual activity of the immobilized DAAO was 79% and 100% of the free catalase.