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Improvement of the Process Stability of Arylmalonate Decarboxylase by Immobilization for Biocatalytic Profen Synthesis.

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.

SUBMITTER: Aßmann M

PROVIDER: S-EPMC5352704 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

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Improvement of the Process Stability of Arylmalonate Decarboxylase by Immobilization for Biocatalytic Profen Synthesis.

Aßmann Miriam M Mügge Carolin C Gaßmeyer Sarah Katharina SK Enoki Junichi J Hilterhaus Lutz L Kourist Robert R Liese Andreas A Kara Selin S

Frontiers in microbiology 20170316

The enzyme arylmalonate decarboxylase (AMDase) enables the selective synthesis of enantiopure (<i>S</i>)-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 (<i>S</i>)-selective AMDase varia ...[more]

PMID: 28360905

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