Immobilization of a multi-enzyme system for L-amino acids production
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Rodriguez-Alonso, M.J.; Rodríguez Vico, Felipe![Autoridad Universidad de Almería Autoridad Universidad de Almería](/themes/Mirage2/images/autoridades/autoridad.png)
![Autoridad Universidad de Almería Autoridad Universidad de Almería](/themes/Mirage2/images/autoridades/autoridad.png)
![Autoridad Universidad de Almería Autoridad Universidad de Almería](/themes/Mirage2/images/autoridades/autoridad.png)
Fecha
2016Resumen
BACKGROUND: Four enzymes were immobilized for the production of optically pure natural and non-natural L-amino acids via
the ‘Double-Racemase Hydantoinase Process’. Immobilization constitutes an empirical process, and for each enzyme we tested
11 carriers with different functional groups; epoxide, EC-EP, EC-HFA, IB-150 and IB-350, carboxylic acid IB-C435, quaternary
ammonium IB-A161, IB-A171 and IB-A369, aromatic group IB-S861, and hydroxyl group IB-S60S and IB-S60P.
RESULTS: Each protein showed preference for binding on one or several supports: D,L-hydantoinase/IB-350, hydantoin
racemase/EC-EP, L-carbamoylase/EC-EP and carbamoyl racemase/IB-A161. The processwas optimized for each enzyme bymodifying
temperature, pH and ionic strength. For the enzymatic cascade, it was demonstrated that it was essential to use supports
having homogeneous characteristics. The product of the first reaction is the substrate of the next one, and so on. Free mass diffusion
fromone enzyme to the other...
Palabra/s clave
immobilization
enzymatic cascade
L-amino acids