Please use this identifier to cite or link to this item: https://doi.org/10.15480/882.1521
Publisher DOI: 10.3389/fmicb.2017.00448
Title: Improvement of the process stability of arylmalonate decarboxylase by immobilization for biocatalytic profen synthesis
Language: English
Authors: Aßmann, Miriam 
Mügge, Carolin 
Gaßmeyer, Sarah Katharina 
Enoki, Junichi 
Hilterhaus, Lutz 
Kourist, Robert 
Liese, Andreas  
Kara, Selin 
Keywords: arylmalonate decarboxylase;biocatalysis;enantioselectivity;immobilization;process stability;profen
Issue Date: 16-Mar-2017
Publisher: Frontiers Media
Source: Frontiers in microbiology (8): 448- (2017)
Journal or Series Name: Frontiers in microbiology 
Abstract (english): 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.
URI: http://tubdok.tub.tuhh.de/handle/11420/1524
DOI: 10.15480/882.1521
ISSN: 1664-302X
Institute: Technische Biokatalyse V-6 
Type: (wissenschaftlicher) Artikel
Project: Open Access Publizieren 2016 - 2017 / Technische Universität Hamburg-Harburg 
License: CC BY 4.0 (Attribution) CC BY 4.0 (Attribution)
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