Immobilization and Biochemical Properties of the Enantioselective Recombinant NStcI Esterase of <i>Aspergillus nidulans</i>

<table>Substrate consumption by NStcI (■) or Novozym 435 (x) and product generation by NStcI (◆) or Novozym 435 (▲) during resolution of (<i>R,S</i>)-1-phenylethanol by the immobilized NStcI esterase at different times of reaction.</table>

Enzyme Research

fig7

Figure 7

Figure 7: Immobilization and Biochemical Properties of the Enantioselective Recombinant NStcI Esterase of <i>Aspergillus nidulans</i> 

Enzyme Research

Immobilization and Biochemical Properties of the Enantioselective Recombinant NStcI Esterase of Aspergillus nidulans

Figure 7