Figure:

Fig.1 Asymmetric reductive amination of phenylpyruvate catalyzed by DAADH
Fig.2 a.Effect of metal ions on enzyme activity of DAADH. b.Effect of Ni2+ concentration on enzyme activity of DAADH.
Reaction conditions: Phenylpyruvate, 5 mM; NADPH, 0.2 mM; Metal ions, 10 mM, pH, 10.0; temperature, 30 °C.
Fig.3 Effect of ionic liquids on DAADH activity. Reaction conditions: Phenylpyruvate, 5 mM; NADPH, 0.2 mM; pH, 10.0; temperature, 30 °C.
Fig.4 Activity recovery rate of immobilized enzyme.
Reaction conditions: Phenylpyruvate, 5 mM; NADPH, 0.2 mM; pH, 10.0; temperature, 30 °C.
Fig.5 The optimum reaction temperature for reductive amination of DAADH.
Reaction conditions: Phenylpyruvate, 5 mM; NADPH, 0.2 mM; pH, 10.0; temperature, 30-80 °C
Fig.6 Optimal pH for reductive amination of immobilized enzymes.
Reaction conditions: Phenylpyruvate, 5 mM; NADPH, 0.2 mM; pH, 8.5-12.0; temperature, 30 °C.
Fig. 7 Reuse stability of immobilized enzyme.
Reaction conditions: Phenylpyruvate, 5 mM; NADPH, 0.2 mM; pH, 10.0; temperature, 30 °C.
Fig.8 Thermostability of free enzyme and immobilized enzyme at 50 ℃.
Reaction conditions: Phenylpyruvate, 5 mM; NADPH, 0.2 mM; pH, 10.0; temperature, 50 °C.