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| Content Provider | frontiers |
|---|---|
| Author | Aßmann, Miriam Mügge, Carolin Gaßmeyer, Sarah Katharina Enoki, Junichi Hilterhaus, Lutz Kourist, Robert Liese, Andreas Kara, Selin |
| 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 hours 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. |
| ISSN | 1664302X |
| DOI | 10.3389/fmicb.2017.00448 |
| Volume Number | 8 |
| Journal | Frontiers in Microbiology |
| Language | English |
| Publisher Date | 2017-03-16 |
| Access Restriction | Open |
| Subject Keyword | Arylmalonate decarboxylase (AMDase) Biocatalysis Profenes Enantioselectivity Process stability Immobilization |
| Content Type | Text |
| Resource Type | Article |
| Subject | Microbiology Microbiology (medical) |
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