Improvement of the process stability of arylmalonate decarboxylase by immobilization for biocatalytic profen synthesis

Link:
Autor/in:
Verlag/Körperschaft:
Hamburg University of Technology
Erscheinungsjahr:
2017
Medientyp:
Text
Schlagworte:
  • arylmalonate decarboxylase
  • biocatalysis
  • enantioselectivity
  • immobilization
  • process stability
  • profen
  • 570: Biowissenschaften, Biologie
  • 570
Beschreibung:
  • 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.
Beziehungen:
DOI 10.3389/fmicb.2017.00448
Lizenzen:
  • info:eu-repo/semantics/openAccess
  • https://creativecommons.org/licenses/by/4.0/
Quellsystem:
TUHH Open Research

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oai:tore.tuhh.de:11420/1524