Details
| Original language | English |
|---|---|
| Article number | 448 |
| Journal | Frontiers in microbiology |
| Volume | 8 |
| Publication status | Published - 16 Mar 2017 |
| Externally published | Yes |
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 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.
Keywords
- Arylmalonate decarboxylase, Biocatalysis, Enantioselectivity, Immobilization, Process stability, Profen
ASJC Scopus subject areas
- Immunology and Microbiology(all)
- Microbiology
- Medicine(all)
- Microbiology (medical)
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In: Frontiers in microbiology, Vol. 8, 448, 16.03.2017.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Improvement of the process stability of arylmalonate decarboxylase by immobilization for biocatalytic profen synthesis
AU - Aßmann, Miriam
AU - Mügge, Carolin
AU - Gaßmeyer, Sarah Katharina
AU - Enoki, Junichi
AU - Hilterhaus, Lutz
AU - Kourist, Robert
AU - Liese, Andreas
AU - Kara, Selin
N1 - Funding Information: Financial support from the Deutsche Bundesstiftung Umwelt (DBU), grant No. AZ30818-32, is gratefully acknowledged. This publication was furthermore supported by the German Research Foundation (DFG) and the Hamburg University of Technology (TUHH) in the funding program "Open Access Publishing." We thank the company Enginzyme (Stockholm, Sweden) for kindly providing the carriers for affinity immobilization.
PY - 2017/3/16
Y1 - 2017/3/16
N2 - 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.
AB - 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.
KW - Arylmalonate decarboxylase
KW - Biocatalysis
KW - Enantioselectivity
KW - Immobilization
KW - Process stability
KW - Profen
UR - http://www.scopus.com/inward/record.url?scp=85016994585&partnerID=8YFLogxK
U2 - 10.3389/fmicb.2017.00448
DO - 10.3389/fmicb.2017.00448
M3 - Article
AN - SCOPUS:85016994585
VL - 8
JO - Frontiers in microbiology
JF - Frontiers in microbiology
SN - 1664-302X
M1 - 448
ER -