Improvement of the process stability of arylmalonate decarboxylase by immobilization for biocatalytic profen synthesis
Citation Link: https://doi.org/10.15480/882.1521
Publikationstyp
Journal Article
Date Issued
2017-03-16
Sprache
English
Institut
TORE-DOI
Journal
Volume
8
Start Page
448
Citation
Frontiers in microbiology (8): 448- (2017)
Publisher DOI
Scopus ID
Publisher
Frontiers Media S.A.
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.
Subjects
arylmalonate decarboxylase
biocatalysis
enantioselectivity
immobilization
process stability
profen
DDC Class
570: Biowissenschaften, Biologie