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  4. Improvement of the process stability of arylmalonate decarboxylase by immobilization for biocatalytic profen synthesis
 
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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
Author(s)
Aßmann, Miriam  
Mügge, Carolin  
Gaßmeyer, Sarah Katharina  
Enoki, Junichi  
Hilterhaus, Lutz  
Kourist, Robert  
Liese, Andreas  orcid-logo
Kara, Selin  
Institut
Technische Biokatalyse V-6  
TORE-DOI
10.15480/882.1521
TORE-URI
http://tubdok.tub.tuhh.de/handle/11420/1524
Journal
Frontiers in microbiology  
Volume
8
Start Page
448
Citation
Frontiers in microbiology (8): 448- (2017)
Publisher DOI
10.3389/fmicb.2017.00448
Scopus ID
2-s2.0-85016994585
Publisher
Frontiers Media
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
Funding(s)
Open Access Publizieren 2016 - 2017 / Technische Universität Hamburg-Harburg  
Lizenz
https://creativecommons.org/licenses/by/4.0/
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