3.7. Kinetic study of DAADH
Kinetic parameters of the DAwild and DA11 were calculated by Hanes-Woolf method within the phenylpyruvate concentration range of 0.625-10 mM, as shown in Fig. S3. Vmax of DAwild and DA11 are all 0.5 mM/min, while DA11 showed a decreased Km value as 1.00 mM (Table 6). This result indicated that the DA11 increased the affinity with substrate, and further improved enzyme catalyzed efficiency. Interfacial mutation which are outside the active sites can improved stability without decrease the enzyme activity, which can reduce the trade-off effect of activity and thermostability.