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Updated: Aug 12, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
Published on: July 11, 2012
Improvement of the Process Stability of Arylmalonate Decarboxylase by Immobilization for Biocatalytic Profen
Miriam Aßmann1, Carolin Mügge2, Sarah Katharina Gaßmeyer2
1Institute of Technical Biocatalysis, Hamburg University of Technology, Hamburg, Germany.
Abstract:
The enzyme arylmalonate decarboxylase (AMDase) enables the selective synthesis of enantiopure (S)-arylpropinates in a simple single-step decarboxylation of dicarboxylic acid precursors. However, the poor enzyme stability with a half-life time of about 1.2 h under process conditions is a serious limitation of the productivity, which results in a need for high catalyst loads. By immobilization on an amino C2 acrylate carrier the operational stability of the (S)-selective AMDase variant G74C/M159L/C188G/V43I/A125P/V156L was increased to a half-life of about 8.6 days, which represents a 158-fold improvement. Further optimization was achieved by simple immobilization of the cell lysate to eliminate the cost- and time intensive enzyme purification step.
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