Improvement of the Process Stability of Arylmalonate Decarboxylase by Immobilization for Biocatalytic Profen Synthesis

被引:13
作者
Assmann, Miriam [1 ]
Muegge, Carolin [2 ]
Gassmeyer, Sarah Katharina [2 ]
Enoki, Junichi [2 ]
Hilterhaus, Lutz [1 ]
Kourist, Robert [2 ]
Liese, Andreas [1 ]
Kara, Selin [1 ]
机构
[1] Hamburg Univ Technol, Inst Tech Biocatalysis, Hamburg, Germany
[2] Ruhr Univ Bochum, Jr Res Grp Microbial Biotechnol, Bochum, Germany
关键词
profen; arylmalonate decarboxylase; process stability; immobilization; biocatalysis; enantioselectivity; ENZYME IMMOBILIZATION; PROTEIN; PURIFICATION; EVOLUTION;
D O I
10.3389/fmicb.2017.00448
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
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页数:8
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