Enzyme Research

Enzyme Research / 2013 / Article / Fig 7

Research Article

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

Figure 7

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